Any feedback?
Information on EC 3.6.5.1 - heterotrimeric G-protein GTPase
for references in articles please use BRENDA:EC3.6.5.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.6.5.1 heterotrimeric G-protein GTPaseIUBMB Comments
This group comprises GTP-hydrolysing systems, where GTP and GDP alternate in binding. This group includes stimulatory and inhibitory G-proteins such as Gs, Gi, Go and Golf, targetting adenylate cyclase and/or K+ and Ca2+ channels; Gq stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase. Golf is instrumental in odour perception, transducin in vision and gustducin in taste recognition. At least 16 different alpha subunits (39-52 kDa), 5 beta subunits (36 kDa) and 12 gamma subunits (6-9 kDa) are known.
Specify your search results
Word Map
- 3.6.5.1
- guanine
- g-proteins
- toxin
- actin
- gdp
- cyclase
-
gtp-binding
- rhoa
- cytoskeleton
- retinal
- pertussis
- cdc42
- agonist
- rac1
- rhodopsin
-
adp-ribosylation
- photoreceptors
-
protein-coupled
- alpha-subunits
- galphas
- phospholipase
-
adenylyl
- camp
-
endocytosis
- microtubule
-
nucleotide-binding
- endosomes
- dynamin
-
gdp-bound
- adenylate
- rgs
-
fission
- cholera
-
endocytic
-
gpcrs
-
ras-related
-
dominant-negative
- cytokine
-
phototransduction
- pigmentosa
- diphtheria
-
ribosylation
-
muscarinic
-
toxin-sensitive
- opsin
-
gtp-dependent
-
gppnhp
-
pleckstrin
-
dynamin-related
-
p21-activated
- medicine
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
gtpase, transducin, gs alpha, heterotrimeric g protein, galphaq, guanosine triphosphatase, elongation factor 2, heterotrimeric g-protein, rab1a, g alpha q, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.6.1.46
-
-
formerly
-
G12
G13
Galpha protein
GPA1
GTP phosphohydrolase
GTPase
guanosine 5'-triphosphatase
-
-
-
-
guanosine triphosphatase
-
-
-
-
heterotrimeric G protein
heterotrimeric G protein family
heterotrimeric G-protein
heterotrimeric G-protein GTPase
heterotrimeric GTPase
phosphatase, guanosine tri-
-
-
-
-
ribosomal GTPase
-
-
-
-
transducin
transducin GTPase
-
-
-
-
GTP phosphohydrolase
-
-
-
-
GTPase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + H2O = GDP + phosphate
binding and hydrolysis of GTP triggers reciprocal conformational changes within a switch region within the catalytic domain
-
GTP + H2O = GDP + phosphate
in the classic paradigm of G-protein signaling, GDP-bound Galpha remains associated with the non-dissociable betagamma subunits and, in combination with a G-protein coupled receptor (GPCR), represents the inactive state of the signaling pathway. Signal perception by GPCR facilitates the exchange of GTP for bound GDP on Galpha. The GTP-bound Galpha dissociates from the Gbetagamma dimer and both entities can interact with specific downstream effectors to transduce the signal. Galpha is restored to its GDP-bound conformation by its own intrinsic GTPase activity which leads to its reassociation with the Gbetagamma dimer and GPCR. The switch-like signaling mechanism has two distinct regulatory steps: the rate of GDP-GTP exchange facilitated by a cognate GPCR, which involves GDP release and GTP binding; and the rate of GTP hydrolysis by the Galpha protein
-
GTP + H2O = GDP + phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis of phosphoric ester
phosphorous acid anhydride hydrolysis
phosphorous acid anhydride hydrolysis
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
GTP phosphohydrolase (signalling)
This group comprises GTP-hydrolysing systems, where GTP and GDP alternate in binding. This group includes stimulatory and inhibitory G-proteins such as Gs, Gi, Go and Golf, targetting adenylate cyclase and/or K+ and Ca2+ channels; Gq stimulating phospholipase C; transducin activating cGMP phosphodiesterase; gustducin activating cAMP phosphodiesterase. Golf is instrumental in odour perception, transducin in vision and gustducin in taste recognition. At least 16 different alpha subunits (39-52 kDa), 5 beta subunits (36 kDa) and 12 gamma subunits (6-9 kDa) are known.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9059-32-9
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
-
activates phosphoinositide-specific phospholipase C in the presence of aluminium fluoride
-
?
GTP + H2O
GDP + phosphate
-
conformational change induced by the exchange of GDP for GTP in transducin and gustducin
-
?
GTP + H2O
GDP + phosphate
-
Gq/11 is the physiological regulator of phospholipase C-beta1
-
-
?
GTP + H2O
GDP + phosphate
-
specific GTP/GDP-binding and GTP-hydrolysis activity of recombinant CaGalpha1 protein, no binding of ATP or ADP
-
-
?
GTP + H2O
GDP + phosphate
-
usage of fluorescence-labeled 4,4-difluoro-4-bora-3alpha,4alpha-diaza-s-indacene-GTP substrate for assays
-
-
?
GTP + H2O
GDP + phosphate
-
intrinsic GTPase activity of transducin controls inactivation of the effector enzyme, cGMP phosphodiesterase during turnoff of the visual signal
-
?
GTP + H2O
GDP + phosphate
-
cycle of G protein activation and deactivation that transmits a signal from receptor to effector: when GDP is bound the alpha subunit associated with the betagamma subunit to form an inactive heterotrimer that binds to the receptor. Both alpha and betagamma subunits can bind to the receptor. When a chemical or physical signal stimulates the receptor, the receptor becomes activated and changes its conformation. The GDP-ligated alpha-subunit responds with a conformational change that decreases GDP affinity, so that GDP is released. Leaving GDP is replaced by GTP. Once ATP is bound, the alpha subunit assumes its activated conformation and dissociates both from the receptor and from betagamma. The activated state lasts until the GTP is hydrolyzed to GDP by the intrinsic GTPase activity of the alpha-subunit. Once GTP is cleaved to GDP, the alpha and betagamma subunits reassociate, become inactive, and return to the receptor. The free alpha and betagamma subunits each activate target effectors. Galphas and Galphaolf, stimulate adenylyl cyclase and regulate Ca2+ channels. Galphai-1, Galphai-2, Galphai-3, Galphao, Galphat-1, Galphat-2, Galphagust and Galphaz inhibit adenylyl cyclase, regulate K+ and Ca2+ channels, and activate cGMP phosphodiesterase. Galphaq, Galpha11, Galpha14, Galppha15 and Galpha16 activate phospholipase C. Galpha12 and Galpha13 regulate Na/K+ exchange. The betagamma subunit is a positive regulator of K+ channels, adenylyl cyclase, phospholipase Cbeta, phospholipase A2, phosphoinositide 3-kinase and beta-adrenergic receptor kinase
-
?
GTP + H2O
GDP + phosphate
-
Galpha subunits can regulate intracellular effectors, such as adenylyl cyclase, phospholipase Cbeta, K+ and Ca+ channels, and cyclic GMP phosphodiesterase
-
?
GTP + H2O
GDP + phosphate
-
Gi1alpha, Gi2alpha and Gi3alpha are capable of preventing stimulation of adenylate cyclase by the alpha2A-adrenoceptor
-
?
GTP + H2O
GDP + phosphate
-
Gi: the G protein that mediates inhibition of adenylate cyclase
-
?
GTP + H2O
GDP + phosphate
-
GTPase that functions as a component of the rhodopsin-linked, light-activated phosphodiesterase system
-
?
additional information
?
-
-
calcium-independent PKCtheta/delta is a potential downstream target of Galpha12
-
-
?
additional information
?
-
-
analysis of interaction between Capsicum Galpha and Gbeta proteins and between Galpha and RGS activator proteins by yeast split-ubiquitin system
-
-
?
additional information
?
-
-
protein-protein interaction analysis between soybean G-protein subunits, overview. GmGalpha and GmGbeta interact in most of the possible combinations
-
-
?
additional information
?
-
-
Galpha12 and Galpha13 couple with G-protein coupled receptors, GPCRs, for various ligands, e.g. angiotensin II, endothelin, thrombin, bombesin, thromboxane A2, sphingosine-1-phosphate, and lysophosphatidic acid. The coupling specificity between G12 and G13 is usually not strict and most of these ligands can activate both G12 and G13. The RH domain of PDZ-RhoGEF interacts with Galpha13 through multiple intermolecular interfaces. One point of contact is centred on an Ile-Ile-Gly motif found N-terminal to the RGS box. This motif forms multiple contacts with the alpha helical domain of Galpha13, and is conserved in other RH-RhoGEFs. Additionally, Galpha13 interacts with an acidic stretch of residues N-terminal to the core RGS box of PDZ-RhoGEF, overview
-
-
?
additional information
?
-
-
activator/regulator protein R14-RGS by itself shows only a marginal ability to promote GTPase activity
-
-
?
additional information
?
-
-
membrane translocation of RGS8, a regulator of G-protein signaling, depends on interaction of RGS8 with enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + H2O
GDP + phosphate
-
Gq/11 is the physiological regulator of phospholipase C-beta1
-
-
?
GTP + H2O
GDP + phosphate
-
intrinsic GTPase activity of transducin controls inactivation of the effector enzyme, cGMP phosphodiesterase during turnoff of the visual signal
-
?
GTP + H2O
GDP + phosphate
-
cycle of G protein activation and deactivation that transmits a signal from receptor to effector: when GDP is bound the alpha subunit associated with the betagamma subunit to form an inactive heterotrimer that binds to the receptor. Both alpha and betagamma subunits can bind to the receptor. When a chemical or physical signal stimulates the receptor, the receptor becomes activated and changes its conformation. The GDP-ligated alpha-subunit responds with a conformational change that decreases GDP affinity, so that GDP is released. Leaving GDP is replaced by GTP. Once ATP is bound, the alpha subunit assumes its activated conformation and dissociates both from the receptor and from betagamma. The activated state lasts until the GTP is hydrolyzed to GDP by the intrinsic GTPase activity of the alpha-subunit. Once GTP is cleaved to GDP, the alpha and betagamma subunits reassociate, become inactive, and return to the receptor. The free alpha and betagamma subunits each activate target effectors. Galphas and Galphaolf, stimulate adenylyl cyclase and regulate Ca2+ channels. Galphai-1, Galphai-2, Galphai-3, Galphao, Galphat-1, Galphat-2, Galphagust and Galphaz inhibit adenylyl cyclase, regulate K+ and Ca2+ channels, and activate cGMP phosphodiesterase. Galphaq, Galpha11, Galpha14, Galppha15 and Galpha16 activate phospholipase C. Galpha12 and Galpha13 regulate Na/K+ exchange. The betagamma subunit is a positive regulator of K+ channels, adenylyl cyclase, phospholipase Cbeta, phospholipase A2, phosphoinositide 3-kinase and beta-adrenergic receptor kinase
-
?
GTP + H2O
GDP + phosphate
-
Galpha subunits can regulate intracellular effectors, such as adenylyl cyclase, phospholipase Cbeta, K+ and Ca+ channels, and cyclic GMP phosphodiesterase
-
?
GTP + H2O
GDP + phosphate
-
Gi1alpha, Gi2alpha and Gi3alpha are capable of preventing stimulation of adenylate cyclase by the alpha2A-adrenoceptor
-
?
GTP + H2O
GDP + phosphate
-
Gi: the G protein that mediates inhibition of adenylate cyclase
-
?
GTP + H2O
GDP + phosphate
-
GTPase that functions as a component of the rhodopsin-linked, light-activated phosphodiesterase system
-
-
?
additional information
?
-
-
calcium-independent PKCtheta/delta is a potential downstream target of Galpha12
-
-
?
additional information
?
-
-
protein-protein interaction analysis between soybean G-protein subunits, overview. GmGalpha and GmGbeta interact in most of the possible combinations
-
-
?
additional information
?
-
-
Galpha12 and Galpha13 couple with G-protein coupled receptors, GPCRs, for various ligands, e.g. angiotensin II, endothelin, thrombin, bombesin, thromboxane A2, sphingosine-1-phosphate, and lysophosphatidic acid. The coupling specificity between G12 and G13 is usually not strict and most of these ligands can activate both G12 and G13. The RH domain of PDZ-RhoGEF interacts with Galpha13 through multiple intermolecular interfaces. One point of contact is centred on an Ile-Ile-Gly motif found N-terminal to the RGS box. This motif forms multiple contacts with the alpha helical domain of Galpha13, and is conserved in other RH-RhoGEFs. Additionally, Galpha13 interacts with an acidic stretch of residues N-terminal to the core RGS box of PDZ-RhoGEF, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Al3+
-
exposure of the rye roots to Al3+ results in activation of GTPase, Al-induced secretion is inhibited by pertussis toxin
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Pasteurella multocida toxin
-
deamidates glutamine-205 of G alphaI2 to glutamic acid, inhibits intrinsic GTPase activity, causes persistent activation of the G protein
-
regulator of G protein signaling protein
Saccharomyces pombe
-
Gpa1 signaling suppressed by low stimulation
-
betagamma subunit of the hetreotrimeric G protein
-
the beta and gamma subunit of G protein form tightly associated complexes, large number of possible combinations of unique beta and gamma subunits, inhibition of steady-state GTP hydrolysis catalyzed by Gsalpha, Goalpha and myristoylated rGialpha2
-
betagamma subunit of the hetreotrimeric G protein
-
inhibits by selectively binding to and stabilization of the GDP-bound state
-
betagamma subunit of the hetreotrimeric G protein
-
the beta and gamma subunit of G protein form tightly associated complexes, large number of possible combinations of unique beta and gamma subunits, inhibition of steady-state GTP hydrolysis catalyzed by Gsalpha, Goalpha and myristoylated rGialpha2
-
Leu-Gly-Asn repeat-enriched protein
-
LGN protein, GDP dissociation inhibitor, GDI, binds to the alpha subunit of transducin in the GDP-bound state
-
Leu-Gly-Asn repeat-enriched protein
-
LGN protein, GDP dissociation inhibitor, GDI, binds to the alpha subunit of transducin in the GDP-bound state
-
pertussis toxin
-
a heterotrimeric G-protein antagonist, inhibits the enzyme
-
pertussis toxin
-
pertussis toxin-catalysed ADP-ribosylation prevents functional contacts between G-protein-coupled receptors and the Gi-like G-proteins
-
pertussis toxin
-
pertussis toxin-catalysed ADP-ribosylation prevents functional contacts between G-protein-coupled receptors and the Gi-like G-proteins
-
pertussis toxin
-
a heterotrimeric G-protein antagonist, inhibits the enzyme
-
additional information
-
GTPase rate is unaffected when transducin alpha-subunit binds to the inhibitory gamma-subunit of cGMP phosphodiesterase, altough this binding is fast and of high affinity
-
additional information
-
GTPase activity of transducin is blocked by ADP-ribosylation
-
additional information
-
tubulin binds to Gs alpha, Gi alpha1 and Gq alpha, destabilize microtubules
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AGS3 protein
-
G-protein signaling modulator 1, GPSM1, Human Genome Organization nomenclature
-
Axin protein
-
member of RA or E subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
Axin2 protein
-
member of RA or E subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
betagamma-subunit of transducin
-
from bovine retinal transducin and from rabbit liver, enhances activity of Goalpha
-
Carbachol
-
0.1 mM, in presence of regulator of G-protein signaling proteins such as RGS4, Gbeta5 with RGS6, RGS7, RGS9 or RGS11, but not carbachol alone
cell-surface receptors
-
of the seven-transmembrane-helix class, activated by catalyzing the exchange of GDP for GTP in the guanine nucleotide-binding site of the alpha-subunit
-
CIVIAKLKANLM amide
-
peptide derived from glucagon-like peptide, residues 329-340, 0.001 mM, 186% of basal GTPase activity
CIVIAKLKANLMCKTDIKCRLAK amide
-
peptide derived from glucagon-like peptide, residues 329-351, 0.001 mM, 595% of basal GTPase activity
CKTDIKCRLAK amide
-
peptide derived from glucagon-like peptide, residues 341-351, 0.001 mM, 216% of basal GTPase activity
G component
-
can bind GTP and can support light-dependent and GTP-dependent phosphodiesterase activation
-
GRK1 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK2 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK3 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK4 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK5 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK6 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
GRK7 protein
-
member of GRK or G subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
H component
-
MW 60000 Da, participates in the light-dependent activation of GTPase, G component requires the presence of H component for expression of GTPase activity
-
LARG protein
-
member of GEF or F subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
LGN protein
-
G-protein signaling modulator 2, GPSM2, Human Genome Organization nomenclature
-
muscarinic acetylcholine receptors
-
receptor m1 activates, no activation by receptor m2
-
NDP kinase
-
can transfer the gamma-phosphate of ATP directly to GDP bound to the G protein, this phosphorylation results in the activation of the signal-coupling proteins
-
p115-RhoGEF protein
-
member of GEF or F subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
PDZ-RhoGEF protein
-
member of GEF or F subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
phospholipase D
-
coincubation of enzyme with phospholipase D in equal amounts stimulates up to 35%
-
phospholipase Dalpha1
-
PLDalpha1, a GTPase activity accelerating protein (GAP). Phosphatidic acid (PA), a key product of PLDalpha1 activity, can bind with and modulate the GAP activity of RGS1, another GAP. Abscisic acid treatment likely results in the activation of PLDalpha1, which leads to PA production
-
regulator of G protein signaling protein
Saccharomyces pombe
-
Gpa1 signaling potentiated by high stimulation
-
regulator of G-protein signaling 1
-
RGS1, a GTPase activity accelerating protein (GAP). Phosphatidic acid (PA), a key product of PLDalpha1 activity, can bind with and modulate the GAP activity of RGS1. PA binding to RGS1 provides a molecular link between lipid- and G-protein mediated signaling. The RGS1K259E mutant is active and functional, but shows reduced binding of PA
-
RGS protein
-
one RGS gene in the Capsicum genome that acts as a regulator of the G-protein signaling, idetification and cloning
-
RGS10 protein
-
member of R12 or D subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS11 protein
-
member of R7 or C subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS12 protein
-
member of R12 or D subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS13 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS17 protein
-
member of RZ or A subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS18 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS19 protein
-
member of RZ or A subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS20 protein
-
member of RZ or A subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS21 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS3 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS4 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS5 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS6 protein
-
member of R7 or C subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS7 protein
-
member of R7 or C subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS8 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS9 protein
-
member of R7 or C subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS9-1 protein
-
short splice variant of RGS9, in complex with type 5 G protein beta-subunit Gbeta5L, regulated by the membrane anchor R9AP
-
SNX13 protein
-
member of SNX or H subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
SNX14 protein
-
member of SNX or H subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
SNX25 protein
-
member of SNX or H subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
cholera toxin
-
a heterotrimeric G-protein agonist, stimulates the enzyme
-
gamma-subunit of cGMP phosphodiesterase
-
accelerate GTP hydrolysis by transducin
-
gamma-subunit of cGMP phosphodiesterase
-
the GTPase activating epitope is located within the C-terminal third of phosphodiesterase
-
gamma-subunit of cGMP phosphodiesterase
-
accelerate GTP hydrolysis by transducin
-
gamma-subunit of cGMP phosphodiesterase
-
Arg33 and Arg36 in the polycationic region of the gamma-subunit of cGMP phosphodiesterase have a special function for the interaction with alpha-subunit of transducin
-
gamma-subunit of cGMP phosphodiesterase
-
Arg33 and Arg36 in the polycationic region of the gamma-subunit of cGMP phosphodiesterase have a special function for the interaction with alpha-subunit of transducin
-
RGS
-
retinal specific member of the RGS family accelerates GTP hydrolysis by transducin
RGS1 protein
-
G-protein signaling proteins, RGS proteins, accelerate the inherent GTPase activity of Galpha proteins. The GTPase-accelerating activities of GmRGS1 and -2 differ for each GmGalpha. Differential effects of GmRGS1 and GmRGS2 on GmGalpha1-4 result from a single valine versus alanine difference. GmRGS protein sequence comparisons and expression pattern, overview
-
RGS1 protein
-
two chimeric RGS proteins in soybean increase the rate of GTP hydrolysis by Galpha proteins and essentially regulate the duration of active signaling, they function primarily as GTPase accelerating proteins
-
RGS1 protein
-
human B-lymphocyte, member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS14 protein
-
member of R12 or D subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS14 protein
-
serves as a GTPase accelerating protein for receptor-coupled heterotrimeric G proteins. RGS14 is a 60 kDa protein of the D/R12 subfamily that contains a regulator of G protein signalling (RGS) domain near its N-terminus, a central region containing a pair of tandem Ras binding domains (RBD), and a GPSM (G protein signalling modulator) domain near its C-terminus. The RGS domain of RGS14 exhibits GTPase accelerating protein activity toward Galphai/o proteins, while its GPSM domain acts as a guanine nucleotide dissociation inhibitor on Galphai1 and Galphai3. The full-length protein has a greater GTPase activating activity but a weaker inhibition of nucleotide dissociation relative to its isolated RGS and GPSM regions, respectively. These differences may be attributable to an inter-domain interaction within RGS14 that promotes the activity of the RGS domain, but simultaneously inhibits the activity of the GPSM domain. The RBD region seems to play an essential role in this regulatory activity. Various potential alternative splice variants of RGS14 are identified. Purified R14-RBD alone has no appreciable effect on the GTPase activity of M2 muscarinic receptor-stimulated Galphai3. The GPSM domain of RGS14 does not inhibit receptor-stimulated GTPase activity
-
RGS16 protein
-
member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
RGS2 protein
-
G-protein signaling proteins, RGS proteins, accelerate the inherent GTPase activity of Galpha proteins. The GTPase-accelerating activities of GmRGS1 and -2 differ for each GmGalpha. Differential effects of GmRGS1 and GmRGS2 on GmGalpha1-4 result from a single valine versus alanine difference. GmRGS protein sequence comparisons and expression pattern, overview
-
RGS2 protein
-
A357V mutant of RGS1 protein, the two chimeric RGS proteins in soybean increase the rate of GTP hydrolysis by Galpha proteins and essentially regulate the duration of active signaling, they function primarily as GTPase accelerating proteins. Interaction between wild-type and mutant E319A, E319K, E319Q GmRGS2 proteins (C-terminal RGS domain) with GmGalpha proteins using split-ubiquitin based interaction assay
-
RGS2 protein
-
human T-lymphocyte, member of R4 or B subfamily of RGS protein superfamily, RGS: regulator of G-protein signaling
-
rhodopsin
-
transducin is activated by photoexcited rhodopsin which catalyzes the exchange of transducin-bound GDP for GTP and then stays active until bound GTP is hydrolyzed by the intrinsic GTPase activity
additional information
-
GTPase activity accelerating proteins (GAPs) are required to increase the rate of deactivation, and to maintain the kinetics of G-protein cycle
-
additional information
-
most monocot plant genomes do not encode for a RGS protein homologue, soybean RGS proteins in the context of their evolution in plants. Plant RGS proteins are unique due to the presence of a 7-transmembrane domain at their N-terminus which is reminiscent of a typical GPCR, evolutionary relationship analysis of RGS proteins, overview
-
additional information
-
stimulation by mouse regulator of G-protein signaling RGS18 by interaction with the alpha subunit of both Gi and Gq subfamilies, RGS18 accelerates intrinsic GTPase activity of Galphai
-
additional information
-
tubulin binds to G beta1gamma1, promotes microtubule stability
-
additional information
-
GTPase activity is stimulated by ribosomes
-
additional information
-
GTPase activity is stimulated by ribosomes up to 2000fold
-
additional information
-
presence of regulator of G-protein signaling proteins such as RGS4, Gbeta5 with RGS6, RGS7, RGS9 or RGS11 stimulates GTPase activity, additional presence of 0.1 mM carbachol stimulates further
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics of 2'-/3'-O-N'-methylanthraniloyl-labeled GTP/GDP exchange for GmGalpha1-GmGalpha4, overview. GmGalpha1 and GmGalpha4 bind GTP more rapidly thanGmGalpha2 and GmGalpha3
-
0.0036
GTP
-
illuminated uROS is used as source of photoexited rhodopsin required for transducin activation
0.0079
GTP
-
illuminated V8-uROS is used as source of photoexited rhodopsin required for transducin activation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes gna 1-3 encoding the three subunits of the enzyme
Q05425; Q05424; Q9HFW7
UniProt
brenda
genes gna 1-3 encoding the three subunits of the enzyme
Q05425; Q05424; Q9HFW7
UniProt
brenda
recombinant protein expressed in baculovirus/Sf9 system, reconstituted in vesicles
-
-
brenda
GTPase that functions as a component of the rhodopsin-linked, light-activated phosphodiesterase system
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
light-dependent localizations of the transducin-alpha subunit Gtalpha
brenda
-
light-dependent localizations of the transducin-alpha subunit Gtalpha
brenda
additional information
-
the relative levels of the G-protein alpha subunits GS alpha-L, GS alpha-S, Gialpha-1, Gialpha-2 and Goalpha are unchanged in membranes prepared from Alzheimer-diseased frontal cortex or hippocampus to control brains. The activity of the G-protein associated high affinity GTPase is reduced in the frontal cortex by 25% and in the hippocampus by 27%
brenda
additional information
-
expression pattern of each of the G-protein genes, ofCaGalpha1, CaGbeta1, CaGgamma1-3 and of CaRGS1 in different tissue types, overview
brenda
additional information
-
expression of four Galpha, four Gbeta, and two Ggamma proteins, expression profiles by quantitative PCR during different developmental stages, overview. In general, the expression of G-protein genes is lower in roots than in aerial tissues. Except for GmGalpha4, which is highly expressed in the primary stem and the first trifoliate leaves at V1 stage, the soybean G-protein genes are expressed at comparable levels in all different developmental stages and tissue types
brenda
additional information
-
expression patterns of GmGalpha1-4 are differentially regulated in different tissues of soybean and at various growth and development phases, e.g. during seed development and seed germination
brenda
additional information
-
both Galpha12 and Galpha13 are expressed ubiquitously
brenda
additional information
no enzyme expression in H-2122 , A-549, H-661, and H-1299 cancer cells, quantitaative enzyme expression analysis, overview
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the levels of Ric-8A are critical during migration and affect the localization of polarity markers and the subcellular localization of GTPase activity
-
brenda
-
functional reconstitution of purified Gi and Go with mü-opioid receptors in guinea pig striatal membranes
brenda
-
light-dependent localization of transducin, colocalization of Gtalpha and LGN
brenda
-
light-dependent localizations of the transducin-alpha subunit Gtalpha
brenda
-
light-dependent localization of transducin, colocalization of Gtalpha and LGN
brenda
-
light-dependent localizations of the transducin-alpha subunit Gtalpha
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
expression of four Galpha, four Gbeta, and two Ggamma proteins, expression profiles by quantitative PCR, the four Galpha proteins form two distinct groups based on their GTPase activity. The proteins interact in most of the possible combinations, with some degree of interaction specificity between duplicated gene pairs
evolution
-
Galpha subunits are classified into four subfamilies, Gs, Gi, Gq and G12. Galpha12/13 and Galphaq are directly involved in the activation of RhoGTPases, molecular mechanisms for regulation of RhoGTPase activity through GPCR heterotrimeric G12/13-signalling pathways, overview. The G12/13-RH-RhoGEF signalling mechanism is well conserved over species
evolution
-
Galpha subunits are classified into four subfamilies, Gs, Gi, Gq and G12. Galpha12/13 and Galphaq are directly involved in the activation of RhoGTPases, molecular mechanisms for regulation of RhoGTPase activity through GPCR heterotrimeric G12/13-signalling pathways, overview. The G12/13-RH-RhoGEF signalling mechanism is well conserved over species
evolution
-
Galpha subunits are classified into four subfamilies, Gs, Gi, Gq and G12. Galpha12/13 and Galphaq are directly involved in the activation of RhoGTPases, molecular mechanisms for regulation of RhoGTPase activity through GPCR heterotrimeric G12/13-signalling pathways, overview. The G12/13-RH-RhoGEF signalling mechanism is well conserved over species
evolution
-
phylogenetic comparison of genes involved in the heterotrimeric G-proteins signaling system, detailed overview over eukaryotic lineages and structural similarities. Identification of heterotrimeric G-protein subunits, RGS domain proteins and 7TM receptors. Through much of eukaryotic evolution, cells contain both 7TM receptors that acted as GEFs and those as GAPs (with C-terminal RGS domains) for Galphas
evolution
-
plants also possess relatively fewer G-protein subunits when compared with the mammalian systems. A highly elaborated plant G-protein network is present in soybean where recent genome duplication has led to existence of 4 Galpha, 4 Gbeta, 12 Ggamma, and 2 RGS proteins
evolution
-
the core G-protein components and their activation/deactivation chemistries are broadly conserved throughout the eukaryotic evolution, while their regulatory mechanisms seem to have been rewired in plants to meet specific needs. Plants such as Arabidopsis, which have a limited number of G-protein components and their regulators, offer a unique opportunity to dissect the mechanistic details of distinct signaling pathways
malfunction
-
deletion of any component of the Galpha13-RhoGEF-RhoA-signalling pathway results in a similar phenotype consisting of embryonic lethality at the stage of gastrulation
malfunction
-
overexpression of constitutively active Galpha12 or 13 induces several cellular effects which suggest stimulation of Rho activity in cells, such as formation of actin stress fibres or neurite retraction in neuronal cells. NIH3T3 transforming activity of constitutively active mutant of Galpha12 can be prevented by blocking its palmitoylation
malfunction
Q05425; Q05424; Q9HFW7
none of the activated Galpha alleles restore female fertility to DELTAgnb-1 mutants, and the gna-3Q208L allele inhibits formation of female reproductive structures, consistent with a need for Galpha proteins to cycle through the inactive GDP-bound form for these processes. During the sexual cycle, DELTAgnb-1 and DELTAgna-1 mutants are male fertile but female sterile, Although these strains produce protoperithecia and trichogynes, their trichogynes have a defect in chemotropism and are not attracted by male cells. DELTAgna-2 and DELTAgna-3 mutants produce protoperithecia and develop perithecia after fertilization with wild-type males. Mutant phenotypes during asexual growth and development, overview
malfunction
-
decreased expression of Gbeta and group I Ggamma genes leads to a significant decrease in nodule number, whereas the converse is true for the overexpression of specific Gbeta and Ggamma genes. Changing the availability of free, active Galpha proteins by modulating the level of the regulatory RGS proteins results in significantly altered nodule numbers. Overexpression of mutant Galpha1Q223L and Galpha1G196S, as confirmed by evaluating the transcript level of the transformed genes, results in a significant decrease in nodule number per transformed root
malfunction
-
none of the activated Galpha alleles restore female fertility to DELTAgnb-1 mutants, and the gna-3Q208L allele inhibits formation of female reproductive structures, consistent with a need for Galpha proteins to cycle through the inactive GDP-bound form for these processes. During the sexual cycle, DELTAgnb-1 and DELTAgna-1 mutants are male fertile but female sterile, Although these strains produce protoperithecia and trichogynes, their trichogynes have a defect in chemotropism and are not attracted by male cells. DELTAgna-2 and DELTAgna-3 mutants produce protoperithecia and develop perithecia after fertilization with wild-type males. Mutant phenotypes during asexual growth and development, overview
-
metabolism
-
complex regulation of the G-protein cycle in soybean and in other plants with expanded G-protein networks
metabolism
-
the Galpha proteins form an elaborate heterotrimeric G-protein network
metabolism
-
the interaction network of rhodopsin involving the heterotrimeric G-protein transducin and the monomeric GTPase Rac1 is determined by distinct binding processes, association of transducin and rhodopsin occurs with higher affinity and speed than the binding of Rac1 to rhodopsin. In dark-adapted rod cells, Rac1 cannot compete with transducin for binding to rhodopsin, and signalling can proceed normally. The concentration of transducin has to drop significantly so that Rac1 can bind to rhodopsin, in the outer segment, this occurs only under intense illumination, when transducin is translocated to the inner segment
metabolism
-
efficient activation and deactivation of Galpha protein is critical for the regulation of heterotrimeric G-protein mediated signaling pathways. Plants such as Arabidopsis, which have a limited number of G-protein components and their regulators, offer a unique opportunity to dissect the mechanistic details of distinct signaling pathways. Interaction occurs between the regulator of G-protein signaling 1 (RGS1) and phospholipase Dalpha1 (PLDalpha1), which are two of the GTPase activity accelerating proteins (GAPs) of the Arabidopsis Galpha protein, GPA1. Phosphatidic acid (PA), a key product of phospholipase Dalpha1 (PLDalpha1) activity, can bind with and modulate the GAP activity of RGS1, uncovering a molecular link between lipid and G-protein signaling and its role in providing the specificity of response regulation. Heterotrimeric G-protein signaling mechanisms and regulation, G-protein signaling model, overview
metabolism
-
Rho guanine nucleotide exchange factor p63RhoGEF619 relocates to the plasma membrane upon activation of Galphaq coupled GPCRs, resembling the well-known activation mechanism of Rho guanine nucleotide exchange factors (RhoGEFs) activated by Galpha12/13. Synthetic recruitment of p63RhoGEF619 to the plasma membrane increases RhoGEF activity towards GTPase RhoA, but full activation requires allosteric activation via Galphaq, overview. Dual role for heterotrimeric G-protein Galphaq in RhoGEF activation, as it both recruits and allosterically activates cytosolic ARHGEF25 gene encoding three RhoGEF isoforms. Activation of the heterotrimeric G-protein Galphaq relieves the DH domain of p63RhoGEF from its autoinhibited state by allosteric interaction with the PH domain
metabolism
-
Ric-8A controls cell polarization during migration probably through Galpha subunit regulation. Ric-8A by its two function as GEF and chaperone may regulate cell polarity by regulating the localization of proteins, such as Galpha-GDP, GPR1/GPR2 and Lin-5, during asymmetric cell division. Therefore in the context of migration it may also interact with a Galpha subunit, and its downstream effectors regulating aPKC and Par3 localization, then under Ric-8A morphant condition, the localization of these proteins is abnormal. Because GTPases regulate each other, any misregulation in one can result in abnormal regulation in the others
metabolism
-
signaling pathways mediated by heterotrimeric G-protein complexes comprising Galpha, Gbeta, and Ggamma subunits and their regulatory RGS (regulator of G-protein signaling) protein are conserved in all eukaryotes. In soybean, phosphorylation-dependent regulation of G-protein cycle during nodule formation exists involving Nod factor receptor 1 (NFR1). The specific Gbeta and Ggamma proteins of a soybean heterotrimeric G-protein complex are involved in regulation of nodulation. During nodulation, the G-protein cycle is regulated by the activity of RGS proteins. Lower or higher expression of RGS proteins results in fewer or more nodules, respectively. NFR1 interacts with RGS proteins and phosphorylates them. Analysis of phosphorylated RGS protein identifies specific amino acids that, when phosphorylated, result in significantly higher GTPase accelerating activity. Active NFR1 receptors phosphorylate and activate RGS proteins, which help maintain the Galpha proteins in their inactive, trimeric conformation, resulting in successful nodule development. Alternatively, RGS proteins might also have a direct role in regulating nodulation because overexpression of their phospho-mimic version leads to partial restoration of nodule formation in nod49 mutants. The RGS proteins directly interact with, and are phosphorylated by, the NFR1 proteins. Phosphorylation of RGS proteins has important physiological consequences as overexpression of phospho-dead or phospho-mimic versions of RGS proteins results in a significant effect on nodule formation. The RGS protein-mediated acceleration of GTP hydrolysis is proposed to be the key regulatory step of plant G-protein signaling in contrast to mammalian systems where the GDP/GTP exchange mediated by the GPCRs is the rate-limiting step of the G-protein cycle. RGS proteins affect nodulation, they are positive regulators of nodule formation, detailed overview
physiological function
-
Galpha proteins regulate G-protein signaling working with RGS proteins
physiological function
-
the G12/13-RH-RhoGEF signalling mechanism is involved in critical steps for cell physiology and disease conditions, including embryonic development, oncogenesis and cancer metastasis. alpha Subunits of G12 or G13 interact with members of the RH domain containing guanine nucleotide exchange factors for Rho (RH-RhoGEF) family of proteins to directly connect G protein-mediated signalling and RhoGTPase signalling, G12/13-mediated signalling is one mechanism to regulate RhoGTPase activity in response to extracellular stimuli. Wild-type Galpha12 is the only Galpha subunit that acts as an oncogene in NIH3T3 cells
physiological function
-
the G12/13-RH-RhoGEF signalling mechanism is involved in critical steps for cell physiology and disease conditions. alpha Subunits of G12 or G13 interact with members of the RH domain containing guanine nucleotide exchange factors for Rho (RH-RhoGEF) family of proteins to directly connect G protein-mediated signalling and RhoGTPase signalling, G12/13-mediated signalling is one mechanism to regulate RhoGTPase activity in response to extracellular stimuli
physiological function
-
the G12/13-RH-RhoGEF signalling mechanism is involved in critical steps for cell physiology and disease conditions. alpha Subunits of G12 or G13 interact with members of the RH domain containing guanine nucleotide exchange factors for Rho (RH-RhoGEF) family of proteins to directly connect G protein-mediated signalling and RhoGTPase signalling, G12/13-mediated signalling is one mechanism to regulate RhoGTPase activity in response to extracellular stimuli
physiological function
-
the virulence factor and highly potent mitogen Pasteurella multocida toxin, PMT, exhibits its toxic activity through activation of heterotrimeric GTPase-dependent pathways, by deamidating a glutamine residue in the alpha subunit of these GTPases via its C-terminal C3 domain, mechanism, overview. Galpha11 and Galphaq are substrates for PMT. C-PMT deamidates Galphaq at least tenfold more efficiently than the full-length PMT. Mutant PMT C1165S is not active on the GTPases, while the mutant C-terminal part of PMT C1159S deamidates Gai/q
physiological function
G-protein, Galpha16, is a critical downstream effector of non-canonical Wnt signaling and a potent inhibitor of transformed cell growth in non small cell lung cancer, Wnt7a-stimulated ERK5 activation is Galpha16-dependent. Importance of Wnt7a signaling via its cognate receptor Frizzled9, a G-protein-coupled receptor, in inhibition of cell proliferation, anchorage-independent growth, and reversal of transformed phenotype in non small cell lung cancer primarily through activation of the tumor suppressor, PPARgamma. Galpha16 is a regulator of non small cell lung cancer cell proliferation and anchorage-independent cell growth. Galpha16 and Galphaq are important mediators of PPARgamma and E-cadherin expression in non small cell lung cancer cell lines
physiological function
Q05425; Q05424; Q9HFW7
heterotrimeric G proteins are critical regulators of growth and asexual and sexual development in the filamentous fungus Neurospora crassa, wild-type phenotype during asexual growth and development
physiological function
-
heterotrimeric G-proteins are important signal transducers in all eukaryotes. The protein complex consists of three dissimilar subunits: Galpha, Gbeta and Ggamma. The Galpha subunit is the enzymatically active protein of the complex which can exist in GTP-bound monomeric or GDP-bound trimeric conformation. The switch-like signaling mechanism has two distinct regulatory steps: the rate of GDP-GTP exchange facilitated by a cognate GPCR, which involves GDP release and GTP binding; and the rate of GTP hydrolysis by the Galpha protein. Two chimeric RGS proteins in soybean increase the rate of GTP hydrolysis by Galpha proteins and essentially regulate the duration of active signaling, they function primarily as GTPase accelerating proteins
physiological function
-
in plants, heterotrimeric G-protein complexes play important roles in signal transduction pathways related to growth and development including response to biotic and abiotic stresses and consequently affect yield of crop plants
physiological function
-
possible involvement of heterotrimeric G-protein signaling in Al-induced secretion of organic acid anions in Arabidopsis. Secretion of organic acid anions from the roots in response to aluminum is a common mechanism for Al resistance in plants
physiological function
-
possible involvement of heterotrimeric G-protein signaling in Al-induced secretion of organic acid anions in rye. Secretion of organic acid anions from the roots in response to aluminum is a common mechanism for Al resistance in plants
physiological function
-
a highly elaborated plant G-protein network is present in soybean where recent genome duplication has led to existence of 4 Galpha, 4 Gbeta, 12 Ggamma, and 2 RGS proteins. G-proteins from soybean have a direct negative role in signaling during nodulation. The Galpha proteins interact with the Nod factor receptors NFR1alpha and NFR1beta. The RGS protein-mediated acceleration of GTP hydrolysis is proposed to be the key regulatory step of plant G-protein signaling in contrast to mammalian systems where the GDP/GTP exchange mediated by the GPCRs is the rate-limiting step of the G-protein cycle
physiological function
-
efficient activation and deactivation of Galpha protein is critical for the regulation of heterotrimeric G-protein mediated signaling pathways. Heterotrimeric GTP-binding proteins (G-proteins) are key regulators of a multitude of signaling pathways in all eukaryotes. In plants, G-proteins are currently a focus of intense research due to their involvement in modulation of many agronomically important traits such as abscisic acid-dependent signaling and stress responses, plant defense responses, seed yield, organ size, symbiosis and nitrogen use efficiency. Heterotrimeric G-protein signaling mechanisms and regulation, overview. GTPase activity accelerating proteins (GAPs) are required to increase the rate of deactivation, and to maintain the kinetics of G-protein cycle. Direct role of ABA-dependent phosphatidic acid production in the regulation of G-protein cycle during seed germination and primary root growth
physiological function
-
heterotrimeric G proteins control cell migration in a variety of cellular types, also during embryogenesis. Four of the five Galpha subunit family members (Galpha12/13, Galphai/o, Galpha/11, and Galphas) are related to migration, activating different signaling cascades and promoting actin cytoskeleton reorganization through the regulation of small GTPase family proteins. The canonical cycle of heterotrimeric G protein signaling begins when a ligand binds to its receptor, which acts as a GEF and induces the activation of Galpha subunits and release from Gbetagamma by the exchange of GDP by GTP. In addition, some GEFs are ligand-independent, such as Ric-8, which accelerates the exchange of GDP for GTP on the Galpha subunit, thereby maintaining an active signaling state. The levels of Ric-8A are critical during migration and affect the localization of polarity markers and the subcellular localization of GTPase activity, suggesting that Ric-8A, probably through heterotrimeric G-protein signaling, regulates cell polarity during CNC migration, overview
physiological function
-
possible involvement of heterotrimeric G-protein signaling in Al-induced secretion of organic acid anions in Arabidopsis. Secretion of organic acid anions from the roots in response to aluminum is a common mechanism for Al resistance in plants
-
physiological function
-
heterotrimeric G proteins are critical regulators of growth and asexual and sexual development in the filamentous fungus Neurospora crassa, wild-type phenotype during asexual growth and development
-
additional information
-
Gbetagamma interacts with the N-terminal alpha helix of Galpha through one of the seven bladed propellers of the Gbeta subunit
additional information
Q05425; Q05424; Q9HFW7
relationship between the three Galpha subunits and components of the Gbetagamma dimer, physical interaction between the Gbeta and Ggamma subunits, overview
additional information
-
the complete heterotrimeric G-protein repertoire in the Capsicum annuum genome consists of one Galpha, one Gbeta and three Ggamma genes
additional information
-
the core G-protein heterotrimeric complex consists of one Glphaa, one Gbeta, and one Ggamma protein. The protein complex switches between the inactive and active states depending on the nucleotide- bound form of Galpha. During resting phase, Galpha is GDP-bound and remains associated with the Gbetagamma proteins in a trimeric conformation (GDP-Galphabetagamma). Activation occurs due to the signal-dependent exchange of GDP on Galpha for GTP. GTP-bound Galpha dissociates from the Gbetagamma dimer and both GTP-Galpha and Gbetagamma can interact with downstream effectors to transduce the signal. Deactivation occurs via the inherent GTPase activity of Galpha, which causes hydrolysis of bound GTP, to produce its GDP-bound form. GDP-Galpha reassociates with Gbetagamma generating the trimeric complex, ready to be activated for the next round of signaling
additional information
-
relationship between the three Galpha subunits and components of the Gbetagamma dimer, physical interaction between the Gbeta and Ggamma subunits, overview
-
Show AA Sequence and Transmembrane Helices (109 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20000
-
x * 58000, recombinant Galphao-CG5036 complex, SDS-PAGE, x * 38000, recombinant enzyme subunit mutant GalphaoDELTA21, SDS-PAGE, x * 20000, recombinant mutant GalphaoDELTA109, SDS-PAGE
36000
38000
-
x * 58000, recombinant Galphao-CG5036 complex, SDS-PAGE, x * 38000, recombinant enzyme subunit mutant GalphaoDELTA21, SDS-PAGE, x * 20000, recombinant mutant GalphaoDELTA109, SDS-PAGE
39000
42000
-
alpha,beta,gamma, 1 * 42000 + 1 * 36000 (beta1) + 1 * 8000 (gamma1), GL1 or Gq protein, SDS-PAGE
43000
-
alpha,beta,gamma, 1 * 43000 + 1 * 36000, (beta1) + 1 * 8000 (gamma2), GL1 protein, SDS-PAGE
45000
58000
-
x * 58000, recombinant Galphao-CG5036 complex, SDS-PAGE, x * 38000, recombinant enzyme subunit mutant GalphaoDELTA21, SDS-PAGE, x * 20000, recombinant mutant GalphaoDELTA109, SDS-PAGE
8000
80000
-
alpha,beta,gamma, 1 * 39000 + 1 * 36000 (beta1) + 1 * 80000 (gamma2), Go protein, SDS-PAGE
36000
-
alpha,beta,gamma, 1 * 42000 + 1 * 36000 (beta1) + 1 * 8000 (gamma1), GL1 or Gq protein, SDS-PAGE
36000
-
alpha,beta,gamma, 1 * 43000 + 1 * 36000, (beta1) + 1 * 8000 (gamma2), GL1 protein, SDS-PAGE
36000
-
alpha,beta,gamma, 1 * 39000 + 1 * 36000 (beta1) + 1 * 80000 (gamma2), Go protein, SDS-PAGE
39000
-
alpha,beta,gamma, 1 * 39000 + 1 * 36000 (beta1) + 1 * 80000 (gamma2), Go protein, SDS-PAGE
8000
-
alpha,beta,gamma, 1 * 42000 + 1 * 36000 (beta1) + 1 * 8000 (gamma1), GL1 or Gq protein, SDS-PAGE
8000
-
alpha,beta,gamma, 1 * 43000 + 1 * 36000, (beta1) + 1 * 8000 (gamma2), GL1 protein, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heteropentamer
heterotrimer
additional information
?
-
alpha,beta,gamma, 1 * 42000 + 1 * 36000 (beta1) + 1 * 8000 (gamma1), GL1 or Gq protein, SDS-PAGE
?
-
alpha,beta,gamma, 1 * 43000 + 1 * 36000, (beta1) + 1 * 8000 (gamma2), GL1 protein, SDS-PAGE
?
-
alpha,beta,gamma, 1 * 39000 + 1 * 36000 (beta1) + 1 * 80000 (gamma2), Go protein, SDS-PAGE
?
-
x * 58000, recombinant Galphao-CG5036 complex, SDS-PAGE, x * 38000, recombinant enzyme subunit mutant GalphaoDELTA21, SDS-PAGE, x * 20000, recombinant mutant GalphaoDELTA109, SDS-PAGE
heteropentamer
Q05425; Q05424; Q9HFW7
(alpha)3(betagamma), three Galpha subunits (GNA-1, GNA-2, and GNA-3), one Gbeta subunit (GNB-1), and one Ggamma subunit (GNG-1), the Gbetagamma dimer interacts with all three Galpha proteins, epistasis between gnb-1 and gna-1, gna-2, and gna-3 for at least one function
heteropentamer
-
(alpha)3(betagamma), three Galpha subunits (GNA-1, GNA-2, and GNA-3), one Gbeta subunit (GNB-1), and one Ggamma subunit (GNG-1), the Gbetagamma dimer interacts with all three Galpha proteins, epistasis between gnb-1 and gna-1, gna-2, and gna-3 for at least one function
-
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
existence of subunit-specific heterotrimers of G-proteins in soybean
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
heterotrimer
-
Galpha subunit, GDP-bound inactive, GTP-bound active and betagamma dimer
additional information
-
interaction of enzyme with phospholipase Dalpha1, results stimulation of enzymic activity and inhibition of phopholipase activity
additional information
domain alpha2-4 and domain alpha3-beta5 are important for interaction with tubulin
additional information
-
analysis of interaction interface between plant RGS and Galpha proteins
additional information
-
G36 with a MW of 36000 Da determined by SDS-PAGE can be Gialpha or Goalpha. G50 with a MW of 50000 Da determined by SDS-PAGE can be Gsalpha
additional information
-
G proteins consist of three polypeptides: an alpha subunit that binds and hydrolyzes GTP, a beta subunit and a gamma subunit. The beta and gamma subunit form a dimer that only dissociates when it is denatured and is therefore a functional monomer. Structure of the subunits
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
phosphoprotein
side-chain modification
additional information
-
Galpha12 and Galpha13 are not myristoylated because they lack a glycine residue as the second amino acid residue
lipoprotein
-
both Galpha12 and 13 are subjected to palmitoylation at cysteine residues near their N-terminus, palmitoylation of Galpha13 is required for its association with the plasma membrane and its ability to activate RhoA through p115RhoGEF. Palmitoylated Galpha12 but not Galpha13 localizes in lipid rafts
lipoprotein
-
most Galpha subunits, excluding alphat, are S-palmitoylated at one or more Cys near the amino terminus, others, alphao, alphaz, alphai and alphat are N-myristoylated at Gly2 as well. Lipid modifications help bind alpha subunits to the plasma membrane, juxtaposing them to their cognate receptors and effector targets
lipoprotein
-
alpha subunits alphao, alphai and alphaz are myristoylated at the N-terminal Gly, alphas and alphaq are not myristoylated. Myristoylation is necessary for membrane attachment and facilitates binding of betagamma. It is an irreversible covalent modification and does not serve a regulatory role. Some alpha subunits are palmitoylated at Cys2. Palmitoylation is reversible. Activation of the beta-adrenergic receptor leads to rapid depalmitoylation of alphas, and depalmitoylated alphas does not activate adenylyl cyclase. Depalmitoylation might be a mechanism to turn off alphas and to sensitize the cell to beta-adrenergic stimulation
phosphoprotein
-
role of Nod factor receptor 1 (NFR1)-mediated phosphorylation in regulation of the G-protein cycle during nodulation in soybean
phosphoprotein
-
phosphorylation of Galpha subunits is an important modification that regulates their function. Galpha12 is a substrate for phosphorylation by protein kinase C. Endogenous Ga12 in human platelets is phosphorylated within the first 50 N-terminal amino acid residues in response to PMA, thrombin and the TXA2 receptor agonist U46619. Phosphorylated Galpha12 loses its affinity for Gbetagamma, and the association with Gbetagamma reciprocally inhibits the phosphorylation of Ga12 by protein kinase C. Endogenous Galpha13 in platelets is phosphorylated in response to PMA, although not in vitro. PKC-mediated phosphorylation of Ga13 in cell might require additional factors
side-chain modification
-
betagamma subunit can be phosphorylated on His residues
side-chain modification
-
protein kinase K-like kinase phosphorylates G36 protein. The phosphorylation of G36 increases its Km for GTP by about 8fold without modification of Vmax. No significant modification after phosphorylation of G50 by protein kinase C or cAMP kinase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Galphao-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036, method screening, hanging-drop vapour-diffusion method, mixing of 0.0015 ml of 25 mg/ml protein solution containing 20 mM Tris-HCl pH 7.5, 2 mM MgCl2, 150 mM NaCl, 2 mM DTT, with 0.0015 ml of reservoir solution containing 20% PEG 4000, 100 mM HEPES sodium salt, pH 7.5, and equilibration against 0.3 ml of reservoir solution, 8-10 days, 22°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, model fitting and refinement
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G196S
-
the mutation in Galpha1 makes the enzyme nearly incapable of being deactivated by RGS protein
Q223L
-
the mutation in a conserved glutamine residue that is important for the GTPase activity of Galpha proteins (in Galpha1) results in a GTPase activity-lacking, constitutively active protein
CFP-TM-Galpha
-
consists of a cleavable signal peptide from human growth hormone, enhanced CFP, the amino-terminal amino acids of the rat mu-opioid receptor, including TM1 and intracellular loop1, and the human Galpha subunit
CFP-TM-Galphai3
-
C to G mutation at the -4 position to render them insensitive to PTX-mediated ADP-ribosylation
CFP-TM-GalphaoA
-
C to G mutation at the -4 position to render them insensitive to PTX-mediated ADP-ribosylation
CFP-TM-Galphasq5
-
the five aminoacids normally found in the carboxyl terminus of Galphas, QYELL, are replaced with those normally found in the carboxy terminus of Galphaq, EYNLV
R238E
-
mutant, reported to be a dominant-negative inhibitor of the rhodopsin-transducin-PDE visual system
S111N
-
mutation at carboxy-terminal end of helix alpha of helical domain, decreased nucleotide exchange kinetics, impaired adenylyl cyclase activation with GTPgammaS, but normal receptor and AlF4- activation
G202A
-
mutation of Galphai1 accelerates the rates of GTP hydrolysis and conformational change
K180P
-
mutation of Galphai1 increases the rate of conformational change and decreases the rates of GTP hydrolysis
Q209E
-
a Galphaq mutant, constructed for rasing of antibodies that specifically detect PMT-deaminated GTPase Galphaq
A26G
-
mutant, rate of poly(U)-directed poly(Phe) synthesis and the ribosome-dependent GTPase activity are decreased, the catalytic efficiency of the intrinsic SsEF-2 GTPase triggered by ethylene glycol is enhanced
G223S
Saccharomyces pombe
-
blocked interaction with regulator of G-protein signaling protein
additional information
additional information
-
mutant gpa1-3 is a heterotrimeric G-protein alpha-subunit deficient mutant generated by T-DNA insertion using the ecotype Col-0, agb1-2 is a heterotrimeric G-protein beta-subunit deficient mutant generated by T-DNA insertion
additional information
-
mutant gpa1-3 is a heterotrimeric G-protein alpha-subunit deficient mutant generated by T-DNA insertion using the ecotype Col-0, agb1-2 is a heterotrimeric G-protein beta-subunit deficient mutant generated by T-DNA insertion
-
additional information
-
protein CaG alpha1 can complement the Galpha-deficient Saccharomyces cerevisiae Gpa1 mutant YGS5
additional information
-
Galpha-RNAi mutant roots exhibit significantly higher whereas RGS-RNAi hairy roots exhibit significantly lower root hair deformation, respectively, compared with the EV control hairy roots. No additional effect on overall root length or lateral root formation is seen in Galpha-RNAi or RGS-RNAi roots
additional information
Q05425; Q05424; Q9HFW7
construction of several subunit deletion mutants, creation of double mutants lacking one Galpha gene and gnb-1 and introduced constitutively active, GTPase-deficient alleles for each Galpha gene into the DELTAgnb-1 background, phenotypes. Genetic analysis reveals that gna-3 is epistatic to gnb-1 with regard to negative control of submerged conidiation. gnb-1 is epistatic to gna-2 and gna-3 for aerial hyphal height, while gnb-1 appears to act upstream of gna-1 and gna-2 during aerial conidiation. None of the activated Galpha alleles restore female fertility to DELTAgnb-1 mutants, and the gna-3Q208L allele inhibits formation of female reproductive structures, consistent with a need for Galpha proteins to cycle through the inactive GDP-bound form for these processes. Introduction of activated Galpha alleles into the DELTAgnb-1 background restores Galpha protein levels
additional information
-
construction of several subunit deletion mutants, creation of double mutants lacking one Galpha gene and gnb-1 and introduced constitutively active, GTPase-deficient alleles for each Galpha gene into the DELTAgnb-1 background, phenotypes. Genetic analysis reveals that gna-3 is epistatic to gnb-1 with regard to negative control of submerged conidiation. gnb-1 is epistatic to gna-2 and gna-3 for aerial hyphal height, while gnb-1 appears to act upstream of gna-1 and gna-2 during aerial conidiation. None of the activated Galpha alleles restore female fertility to DELTAgnb-1 mutants, and the gna-3Q208L allele inhibits formation of female reproductive structures, consistent with a need for Galpha proteins to cycle through the inactive GDP-bound form for these processes. Introduction of activated Galpha alleles into the DELTAgnb-1 background restores Galpha protein levels
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged truncation enzyme mutants GalphaoDELTA21 and GalphaoDELTA109 from Escherichia coli strain M15 by nickel affinity chromatography, for the first followed by anion exchange chromatography and gel filtration
-
the alpha subunit of Gq family G proteins, GL1alpha(G14alpha), GL2alpha(G11alpha) and Gqalpha are expressed with G proteins beta1 and gamma2 subunits in insect cells using a baculovirus system. The trimeric forms of G proteins, GL1(GL1alphabetagamma), GL2(GL2alphabetagamma) and Gq(Gqalphabetagamma) are solubilized and purified
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of heterotrimeric G proteins, DNA and amino acid sequence determination and analysis
-
cloning of the complete heterotrimeric G-protein repertoire in the Capsicum annuum genome which consists of one Galpha, one Gbeta and three Ggamma genes, phylogenetic analysis, DNA and amino acid sequence determination and analysis, real time quantitative PCR tissue-specific enzyme expression analysis, transgenic expression of Gbeta, Ggamma1-3 genes, from pSAT5-DEST-cEYFP-C1 destination vectors containing cEYFP at the N-terminal end via Agrobacterium tumefaciens strain GV3101 transformation, in Nicotiana tabaccum leaves, co-expression of RGS protein
-
Expression of the N-terminally His6-tagged mutant Galphai/q chimeric gene, in which the native N-terminus of Galphaq is replaced with that of Galphai1, the gene also posseses a TEV cleavage site, amino acids 1-28 of rat Galphai1, a linker of Arg and Ser, and the 37-359 amino acid region of mouse Galphaq, expression of recombinant wild-type Galphaq and Galphaq mutant Q209E in Mus musculus Galphaq/11-deficient embryonic fibroblasts, Swiss3T3 cells, expression of alpha subunit cDNAs of heterotrimeric GTPases, Gs, Gi-2, G13 and G11 in human 293T cells
-
genes gna 1-3 encoding the three subunits of the enzyme, transfection of Neurospora crassa with mutant enzymes
Q05425; Q05424; Q9HFW7
Gtalpha and GtalphaR238E for expression in Escherichia coli strains DH5alpha and BL21(DE3)
-
into the pT7-7 vector for expession in Escherichia coli JM109DE3 cells
-
overexpression of heterotrimeric G-proteins Galphai1 and Galphai3 in Spodoptera frugiperda Sf 9 cell membranes using the baculovirus transfection method
-
pBRH Gtalpha transgenic construct containing the mouse Gtalpha genomic sequence flanked by the mouse opsin promoter fragment and the polyadenylation signal, EE-tagged
-
Rab1a is cloned from a mouse cardiac cDNA library, adenoviruses expressing FLAG-Rab1a are generated for infection of rat ventricular myocytes
-
recombinant expression of His6-tagged truncation enzyme mutants GalphaoDELTA21 and GalphaoDELTA109 in Escherichia coli strain M15
-
the alpha subunit of Gq family G proteins, GL1alpha(G14alpha), GL2alpha(G11alpha) and Gqalpha are expressed with G proteins beta1 and gamma2 subunits in insect cells using a baculovirus system. The trimeric forms of G proteins, GL1(GL1alphabetagamma), GL2(GL2alphabetagamma) and Gq(Gqalphabetagamma) are solubilized and purified
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
mutants of transducin represent a major tool in designing potential therapeutical strategies for a group of visual diseases
medicine
medicine
-
mutations in the gene for the alpha-subunit of cone transducin, GNAT2, cause cone-rod degeneration, CRD
medicine
the enzyme is important as a potential therapeutic target for the treatment of non small cell lung cancer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Natochin, M.; Granovsky, A.E.; Artemyev, N.O.
Regulation of transducin GTPase activity by human retinal RGS
J. Biol. Chem.
272
17444-17449
1997
Homo sapiens
brenda
Ueda, H.; Misawa, H.; Katada, T.; Ui, M.; Takagi, H.; Satoh, M.
Functional reconstitution of purified Gi and Go with mue-opioid receptors in guinea pig striatal membranes pretreated with micromolar concentrations of N-ethylmaleimide
J. Neurochem.
54
841-848
1990
Bos taurus, Homo sapiens, Sus scrofa
brenda
Kikkawa, S.; Takahashi, K.; Takahashi, K.; Shimada, N.; Ui, M.; Kimura, N.; Katada, T.
Conversion of GDP into GTP by nucleosifde diphosphate kinase on the GTP-binding proteins
J. Biol. Chem.
265
21536-21540
1990
Bos taurus
brenda
Shinozawa, T.; Uchida, S.; Martin, E.; Cafiso, D.; Hubbell, W.; Bitensky, M.
Additional component required for activity and reconstitution of light-activated vertebrate photoreceptor GTPase
Proc. Natl. Acad. Sci. USA
77
1408-1411
1980
vertebrata
brenda
Ueda, N.; Iniguez-Lluhi, J.A.; Lee, E.; Smrcka, A.V.; Robishaw, J.D.; Gilman, A.G.
G protein betagamma subunits. Simplified purification and properties of novel isoforms
J. Biol. Chem.
269
4388-4395
1994
Bos taurus, Oryctolagus cuniculus
brenda
Bondarenko, V.A.; Desai, M.; Dua, S.; Yamazaki, M.; Amin, R.H.; Yousif, K.K.; Kinumi, T.; Ohashi, M.; Komori, N.; Matsumoto, H.; Jackson, K.W.; Hayashi, F.; Usukura, J.; Lipkin, V.M.; Yamazaki, A.
Residues within the polycationic region of cGMP phosphodiesterase gamma subunit crucial for the interaction with transducin alpha subunit. Identification by endogenous ADP-ribosylation and site-directed mutagenesis
J. Biol. Chem.
272
15856-15864
1997
Lithobates catesbeianus, Lithobates grylio
brenda
Ming, D.; Ruiz-Avila, L.; Margolskee, R.F.
Characterization and solubilization of bitter-responsive receptors that couple to gustducin
Proc. Natl. Acad. Sci. USA
95
8933-8938
1998
Bos taurus
brenda
Arshavsky, V.Y.; Dumke, C.L.; Zhu, Y.; Artemyev, N.O.; Skiba, N.P.; Hamm, H.E.; Bownds, M.D.
Regulation of transducin GTPase activity in bovine rod outer segments
J. Biol. Chem.
269
19882-19887
1994
Bos taurus
brenda
Rouot, B.; Brabet, P.; Homburger, V.; Toutant, M.; Bockaert, J.
Go, a major brain GTP binding protein in search of a function: purification, immunological and biochemical characteristics
Biochimie
69
339-349
1987
Bos taurus, Canis lupus familiaris, Gallus gallus, Homo sapiens, Rattus norvegicus
brenda
Wise, A.; Watson-Koken, M.A.; Rees, S.; Lee, M.; Milligan, G.
Interactions of the alpha2A-adrenoceptor with multiple Gi-family G-proteins: studies with pertussis toxin-resistant G-protein mutants
Biochem. J.
321
721-728
1997
Rattus norvegicus
brenda
Nakamura, F.; Kato, M.; Kameyama, K.; Nukada, T.; Haga, T.; Kato, H.; Takenawa, T.; Kikkawa, U.
Characterization of Gq family G proteins GL1alpha(G14alpha), GL2alpha(G11alpha), and Gqalpga expressed in the baculovirus-insect cell system
J. Biol. Chem.
270
6246-6253
1995
Bos taurus
brenda
Sprang, S.R.
G Protein mechanism: insights from structural analysis
Annu. Rev. Biochem.
66
639-678
1997
Mammalia
brenda
Berstein, G.; Blank, J.L.; Jhon, D.Y.; Exton, J.H.; Rhee, S.G.; Ross, E.M.
Phospholipase C-beta1 is a GTPase-activating protein for Gq/11, its physiologic regulator
Cell
70
411-418
1992
Bos taurus
brenda
Ross, B.M.; McLaughlin, M.; Roberts, M.; Milligan, G.; McCulloch, J.; Knowler, J.T.
Alterations in the activity of adenylate cyclase and high affinity GTPase in Alzheimer's disease
Brain Res.
622
35-42
1993
Homo sapiens
brenda
Soomets, U.; Mahlapuu, R.; Tehranian, R.; Jarvet, J.; Karelson, E.; Zilmer, M.; Iverfeldt, K.; Zorko, M.; Graeslund, A.; Langel, U.
Regulation of GTPase and adenylate cyclase activity by amyloid beta-peptide and its fragments in rat brain tissue
Brain Res.
850
179-188
1999
Rattus norvegicus
brenda
Antonny, B.; Otto-Bruc, A.; Chabre, M.; Vuong, T.M.
GTP hydrolysis by purified alpha-subunit of transducin and its complex with the cyclic GMP phosphodiesterase inhibitor
Biochemistry
32
8646-8653
1993
Bos taurus
brenda
Sauvage, C.; Rumigny, J.F.; Maitre, M.
Purification and characterization of G proteins from human brain: modification of GTPase activity upon phosphorylation
Mol. Cell. Biochem.
107
65-77
1991
Homo sapiens
brenda
Tsai, S.C.; Adamik, R.; Kanaho, Y.; Halpern, J.L.; Moss, J.
Immunological and biochemical differentiation of guanyl nucleotide binding proteins: interaction of Goalpha with rhodopsin, anti-Goalpha polyclonal antibodies, and a monoclonal antibody against transducin alpha subunit and Gialpha
Biochemistry
26
4728-4733
1987
Bos taurus
brenda
Tesmer, J.J.G.; Berman, D.M.; Gilman, A.G.; Sprang, S.R.
Structure of RGS4 bound to AlF4-activated Gialpha1: stabilization of the transition state for GTP hydrolysis
Cell
89
251-261
1997
Rattus norvegicus, Rattus norvegicus Gialpha1
brenda
Neer, E.J.
Heterotrimeric G proteins: organizers of transmembrane signals
Cell
80
249-257
1995
Homo sapiens, Mammalia
brenda
Abood, M.E.; Hurley, J.B.; Pappone, M.C.; Bourne, H.R.; Stryer, L.
Functional homology between signal-coupling proteins
J. Biol. Chem.
257
10540-10543
1982
Bos taurus
brenda
Hallbrink, M.; Holmqvist, T.; Olsson, M.; Ostenson, C.G.; Efendic, S.; Langel, U.
Different domains in the third intracellular loop of the GLP-1 receptor are responsible for Galpha(s) and Galpha(i)/Galpha(o) activation
Biochim. Biophys. Acta
1546
79-86
2001
Rattus norvegicus
brenda
Seo, H.S.; Jeong, J.Y.; Nahm, M.Y.; Kim, S.W.; Lee, S.Y.; Bahk, J.D.
The effect of pH and various cations on the GTP hydrolysis of rice heterotrimeric G-protein alpha subunit expressed in Escherichia coli
J. Biochem. Mol. Biol.
36
196-200
2003
Oryza sativa
brenda
Park, I.K.; Klug, C.A.; Li, K.; Jerabek, L.; Li, L.; Nanamori, M.; Neubig, R.R.; Hood, L.; Weissman, I.L.; Clarke, M.F.
Molecular cloning and characterization of a novel regulator of G-protein signaling from mouse hematopoietic stem cells
J. Biol. Chem.
276
915-923
2001
Homo sapiens
brenda
Hooks, S.B.; Waldo, G.L.; Corbitt, J.; Bodor, E.T.; Krumins, A.M.; Harden, T.K.
RGS6, RGS7, RGS9, and RGS11 stimulate GTPase activity of Gi family G-proteins with differential selectivity and maximal activity
J. Biol. Chem.
278
10087-10093
2003
Spodoptera frugiperda
brenda
Zhao, J.; Wang, X.
Arabidopsis phospholipase Dalpha1 interacts with the heterotrimeric G-protein alpha-subunit through a motif analogous to the DRY motif in G-protein-coupled receptors
J. Biol. Chem.
279
1794-1800
2004
Arabidopsis thaliana
brenda
Brito, M.; Guzman, L.; Romo, X.; Soto, X.; Hinrichs, M.V.; Olate, J.
S111N mutation in the helical domain of human Gs(alpha) reduces its GDP/GTP exchange rate
J. Cell. Biochem.
85
615-620
2002
Homo sapiens
brenda
Masuho, I.; Itoh, M.; Itoh, H.; Saitoh, O.
The mechanism of membrane-translocation of regulator of G-protein signaling (RGS) 8 induced by Galpha expression
J. Neurochem.
88
161-168
2004
Rattus norvegicus
brenda
Traver, S.; Splingard, A.; Gaudriault, G.; De Gunzburg, J.
The RGS (regulator of G-protein signalling) and GoLoco domains of RGS14 co-operate to regulate Gi-mediated signalling
Biochem. J.
379
627-632
2004
Mammalia
brenda
Baker, S.A.; Martemyanov, K.A.; Shavkunov, A.S.; Arshavsky, V.Y.
Kinetic mechanism of RGS9-1 potentiation by R9AP
Biochemistry
45
10690-10697
2006
Bos taurus
brenda
Siderovski, D.P.; Willard, F.S.
The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits
Int. J. Biol. Sci.
1
51-66
2005
Aspergillus nidulans, Saccharomyces cerevisiae, Caenorhabditis elegans, Homo sapiens
brenda
Nair, K.S.; Mendez, A.; Blumer, J.B.; Rosenzweig, D.H.; Slepak, V.Z.
The presence of a Leu-Gly-Asn repeat-enriched protein (LGN), a putative binding partner of transducin, in ROD photoreceptors
Invest. Ophthalmol. Vis. Sci.
46
383-389
2005
Bos taurus, Mus musculus
brenda
Kerov, V.; Chen, D.; Moussaif, M.; Chen, Y.J.; Chen, C.K.; Artemyev, N.O.
Transducin activation state controls its light-dependent translocation in rod photoreceptors
J. Biol. Chem.
280
41069-41076
2005
Mus musculus
brenda
Kerov, V.S.; Natochin, M.; Artemyev, N.O.
Interaction of transducin-alpha with LGN, a G-protein modulator expressed in photoreceptor cells
Mol. Cell. Neurosci.
28
485-495
2005
Mus musculus
brenda
Clark, M.A.; Lambert, N.A.
Endogenous regulator of G-protein signaling proteins regulate the kinetics of Galphaq/11-mediated modulation of ion channels in central nervous system neurons
Mol. Pharmacol.
69
1280-1287
2006
Rattus norvegicus
brenda
Barren, B.; Natochin, M.; Artemyev, N.O.
Mutation R238E in transducin-alpha yields a GTPase and effector-deficient, but not dominant-negative, G-protein alpha-subunit
Mol. Vis.
12
492-498
2006
Homo sapiens
brenda
Pina, A.L.; Baumert, U.; Loyer, M.; Koenekoop, R.K.
A three base pair deletion encoding the amino acid (lysine-270) in the alpha-cone transducin gene
Mol. Vis.
10
265-271
2004
Homo sapiens
brenda
Thomas, C.J.; Du, X.; Li, P.; Wang, Y.; Ross, E.M.; Sprang, S.R.
Uncoupling conformational change from GTP hydrolysis in a heterotrimeric G protein alpha-subunit
Proc. Natl. Acad. Sci. USA
101
7560-7565
2004
Mammalia
brenda
Digby, G.J.; Lober, R.M.; Sethi, P.R.; Lambert, N.A.
Some G protein heterotrimers physically dissociate in living cells
Proc. Natl. Acad. Sci. USA
21
17789-17794
2006
Homo sapiens
brenda
De Vendittis, E.; Adinolfi, B.S.; Amatruda, M.R.; Raimo, G.; Masullo, M.; Bocchini, V.
The A26G replacement in the consensus sequence A-X-X-X-X-G-K-[T,S] of the guanine nucleotide binding site activates the intrinsic GTPase of the elongation factor 2 from the archaeon Sulfolobus solfataricus
Eur. J. Biochem.
262
600-605
1999
Saccharolobus solfataricus
brenda
Raimo, G.; Masullo, M.; Bocchini, V.
Studies on the polypeptide elongation factor 2 from Sulfolobus solfataricus. Interaction with guanosine nucleotides and GTPase activity stimulated by ribosomes
J. Biol. Chem.
270
21082-21085
1995
Saccharolobus solfataricus
brenda
Layden, B.T.; Saengsawang, W.; Donati, R.J.; Yang, S.; Mulhearn, D.C.; Johnson, M.E.; Rasenick, M.M.
Structural model of a complex between the heterotrimeric G protein, Gsalpha, and tubulin
Biochim. Biophys. Acta
1783
964-973
2008
Bos taurus (P04896)
brenda
Wu, G.
Regulation of the trafficking and function of G protein-coupled receptors by Rab1 GTPase in cardiomyocytes
Methods Enzymol.
438
227-238
2008
Mus musculus
brenda
Shen, Y.; Han, Y.J.; Kim, J.I.; Song, P.S.
Arabidopsis nucleoside diphosphate kinase-2 as a plant GTPase activating protein
BMB Rep.
41
645-650
2008
Arabidopsis thaliana
brenda
Smith, B.; Hill, C.; Godfrey, E.L.; Rand, D.; van den Berg, H.; Thornton, S.; Hodgkin, M.; Davey, J.; Ladds, G.
Dual positive and negative regulation of GPCR signaling by GTP hydrolysis
Cell. Signal.
21
1151-1160
2009
Saccharomyces pombe
brenda
Preuss, I.; Kurig, B.; Nuernberg, B.; Orth, J.H.; Aktories, K.
Pasteurella multocida toxin activates Gbetagamma dimers of heterotrimeric G proteins
Cell. Signal.
21
551-558
2009
Homo sapiens, Mus musculus
brenda
Dave, R.H.; Saengsawang, W.; Yu, J.Z.; Donati, R.; Rasenick, M.M.
Heterotrimeric G-proteins interact directly with cytoskeletal components to modify microtubule-dependent cellular processes
Neurosignals
17
100-108
2009
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Orth, J.H.; Preuss, I.; Fester, I.; Schlosser, A.; Wilson, B.A.; Aktories, K.
Pasteurella multocida toxin activation of heterotrimeric G proteins by deamidation
Proc. Natl. Acad. Sci. USA
106
7179-7184
2009
Homo sapiens, Mus musculus
brenda
Kamitani, S.; Ao, S.; Toshima, H.; Tachibana, T.; Hashimoto, M.; Kitadokoro, K.; Fukui-Miyazaki, A.; Abe, H.; Horiguchi, Y.
Enzymatic actions of Pasteurella multocida toxin detected by monoclonal antibodies recognizing the deamidated alpha subunit of the heterotrimeric GTPase Gq
FEBS J.
278
2702-2712
2011
Pasteurella multocida
brenda
Anantharaman, V.; Abhiman, S.; de Souza, R.F.; Aravind, L.
Comparative genomics uncovers novel structural and functional features of the heterotrimeric GTPase signaling system
Gene
475
63-78
2011
Trichomonas vaginalis
brenda
Kozasa, T.; Hajicek, N.; Chow, C.R.; Suzuki, N.
Signalling mechanisms of RhoGTPase regulation by the heterotrimeric G proteins G12 and G13
J. Biochem.
150
357-369
2011
Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens
brenda
Choudhury, S.R.; Westfall, C.S.; Laborde, J.P.; Bisht, N.C.; Jez, J.M.; Pandey, S.
Two chimeric regulators of G-protein signaling (RGS) proteins differentially modulate soybean heterotrimeric G-protein cycle
J. Biol. Chem.
287
17870-17881
2012
Glycine max
brenda
Bisht, N.C.; Jez, J.M.; Pandey, S.
An elaborate heterotrimeric G-protein family from soybean expands the diversity of plant G-protein networks
New Phytol.
190
35-48
2011
Glycine max
brenda
Tishchenko, S.; Gabdulkhakov, A.; Tin, U.; Kostareva, O.; Lin, C.; Katanaev, V.L.
Crystallization and preliminary X-ray diffraction studies of Drosophila melanogaster Galphao-subunit of heterotrimeric G protein in complex with the RGS domain of CG5036
Acta Crystallogr. Sect. F
69
61-64
2013
Drosophila melanogaster
brenda
Won, S.; Michkov, A.V.; Krystofova, S.; Garud, A.V.; Borkovich, K.A.
Genetic and physical interactions between Galpha subunits and components of the Gbetagamma dimer of heterotrimeric G proteins in Neurospora crassa
Eukaryot. Cell
11
1239-1248
2012
Neurospora crassa (Q05425 and Q05424 and Q9HFW7), Neurospora crassa 74 A-OR23-1A (Q05425 and Q05424 and Q9HFW7)
brenda
Koester, M.; DellOrco, D.; Koch, K.W.
The interaction network of rhodopsin involving the heterotrimeric G-protein transducin and the monomeric GTPase Rac1 is determined by distinct binding processes
FEBS J.
281
5175-5185
2014
Bos taurus
brenda
Zhao, P.; Nunn, C.; Ramineni, S.; Hepler, J.R.; Chidiac, P.
The Ras-binding domain region of RGS14 regulates its functional interactions with heterotrimeric G proteins
J. Cell. Biochem.
114
1414-1423
2013
Homo sapiens
brenda
Romero-Castillo, R.A.; Roy Choudhury, S.; Leon-Felix, J.; Pandey, S.
Characterization of the heterotrimeric G-protein family and its transmembrane regulator from capsicum (Capsicum annuum L.)
Plant Sci.
234
97-109
2015
Capsicum annuum
brenda
Choudhury, S.R.; Westfall, C.S.; Pandey, S.
The RGS proteins add to the diversity of soybean heterotrimeric G-protein signaling
Plant Signal. Behav.
7
1114-1117
2012
Glycine max
brenda
Li, Y.; Tang, X.; Yang, L.; Yu, Y.; Li, X.
Possible involvement of heterotrimeric G-protein signaling in Al-induced secretion of organic acid anions in Arabidopsis and rye
Plant Soil
388
55-63
2015
Arabidopsis thaliana, Secale cereale, Arabidopsis thaliana Col-0
-
brenda
Avasarala, S.; Bikkavilli, R.K.; Van Scoyk, M.; Zhang, W.; Lapite, A.; Hostetter, L.; Byers, J.T.; Heasley, L.E.; Sohn, J.W.; Winn, R.A.
Heterotrimeric G-protein, Galpha16, is a critical downstream effector of non-canonical Wnt signaling and a potent inhibitor of transformed cell growth in non small cell lung cancer
PLoS ONE
8
e76895
2013
Homo sapiens (P30679)
brenda
Leal, J.I.; Villaseca, S.; Beyer, A.; Toro-Tapia, G.; Torrejon, M.
Ric-8A, a GEF for heterotrimeric G-proteins, controls cranial neural crest cell polarity during migration
Mech. Dev.
154
170-178
2018
Xenopus tropicalis
brenda
Choudhury, S.R.; Pandey, S.
Phosphorylation-dependent regulation of G-protein cycle during nodule formation in soybean
Plant Cell
27
3260-3276
2015
Glycine max
brenda
Pandey, S.
Heterotrimeric G-protein regulatory circuits in plants conserved and novel mechanisms
Plant Signal. Behav.
12
e1325983
2017
Arabidopsis thaliana
brenda
Kaiser, A.; Langer, B.; Przyborski, J.; Kersting, D.; Krueger, M.
A putative non-canonical Ras-like GTPase from P. falciparum chemical properties and characterization of the protein
PLoS ONE
10
e0140994
2015
no activity in Plasmodium falciparum
brenda
van Unen, J.; Yin, T.; Wu, Y.I.; Mastop, M.; Gadella, T.W.; Goedhart, J.
Kinetics of recruitment and allosteric activation of ARHGEF25 isoforms by the heterotrimeric G-protein Galphaq
Sci. Rep.
6
36825
2016
Homo sapiens
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.6.5.1)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
