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Literature summary for 3.6.5.1 extracted from

  • Choudhury, S.R.; Westfall, C.S.; Pandey, S.
    The RGS proteins add to the diversity of soybean heterotrimeric G-protein signaling (2012), Plant Signal. Behav., 7, 1114-1117.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.5.1

Activating Compound

Activating Compound Comment Organism Structure
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 Glycine max
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 Glycine max
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 Glycine max

Organism

Organism UniProt Comment Textmining
Glycine max
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-
-

Reaction

Reaction Comment Organism Reaction ID
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 Glycine max
a

Subunits

Subunits Comment Organism
More analysis of interaction interface between plant RGS and Galpha proteins Glycine max

Synonyms

Synonyms Comment Organism
Galpha protein
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 Glycine max
GmGalpha protein
-
 Glycine max

General Information

General Information Comment Organism
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 Glycine max