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Information on EC 3.1.1.89 - protein phosphatase methylesterase-1
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3.1.1.89 protein phosphatase methylesterase-1IUBMB Comments
A key regulator of protein phosphatase 2A. The methyl ester is formed by EC 2.1.1.233 (leucine carboxy methyltransferase-1). Occurs mainly in the nucleus.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
[phosphatase 2A protein]-leucine methyl ester
+
=
[phosphatase 2A protein]-leucine
+
Synonyms
ppme1, pp2a methylesterase, protein phosphatase methylesterase-1, phosphatase methylesterase-1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PME-1
PPME1
protein phosphatase methylesterase-1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[phosphatase 2A protein]-leucine methyl ester + H2O = [phosphatase 2A protein]-leucine + methanol
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SYSTEMATIC NAME
IUBMB Comments
[phosphatase 2A protein]-leucine ester acylhydrolase
A key regulator of protein phosphatase 2A. The methyl ester is formed by EC 2.1.1.233 (leucine carboxy methyltransferase-1). Occurs mainly in the nucleus.
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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
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
[protein phosphatase 2A catalytic subunit]-leucine methyl ester + H2O
[protein phosphatase 2A catalytic subunit]-leucine + methanol
-
-
reversible methylation and demethylation at C-terminal residue Leu309. The activity of protein phosphatase 2A is largely unaffected by the addition of enzyme. Mutant versions of substrate protein phosphatase 2A containing an alanine residue in place of Leu309, and a deletion of Leu309 both exhibit phosphatase activity
-
r
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
-
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
-
-
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
-
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
the enzyme negatively regulates protein phosphatase 2A activity by highly complex mechanisms
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
-
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
protein phosphatase 2A (PP2A) is a conserved essential enzyme that is implicated as a tumor suppressor based on its central role in phosphorylation-dependent signaling pathways. Protein phosphatase methyl esterase (PME-1) catalyzes specifically the demethylation of the C-terminal Leu309 residue of phosphatase 2A protein catalytic subunit (PP2Ac)
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
regulates PP2A holoenzyme formation
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
reversible methyl-esterification (methylation) of Leu309 in the protein phosphatase 2A catalytic subunit (PP2Ac) is essential for proper biogenesis of the PP2A holoenzyme
-
-
r
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
the enzyme negatively regulates protein phosphatase 2A activity by highly complex mechanisms
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
protein phosphatase methyl esterase (PME-1) catalyzes specifically the demethylation of the C-terminal Leu309 residue of phosphatase 2A protein catalytic subunit (PP2Ac)
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
the enzyme specifically catalyzes PP2Ac demethylation
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-
r
additional information
?
-
-
spliced isoform PP2Acalpha2 (lacking exon 5) does not interact with PME-1. Only the longer isoform of PP2A interacts with PME-1
-
-
?
additional information
?
-
-
enzyme is tightly associated with an inactive form of protein phosphatase 2A, and neither activation nor inactivation of its phosphorylase phosphatase activity can be observed by methylation. The presence of a third subunit of protein phosphatase 2A does not prevent methylation or demethylation
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-
?
additional information
?
-
-
protein phosphatase 2A associated with PME-1 is inactive, function for PME-1 as an enzyme that stabilizes an inactivated pool of protein phosphatase 2A
-
-
?
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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
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
-
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
the enzyme negatively regulates protein phosphatase 2A activity by highly complex mechanisms
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
protein phosphatase 2A (PP2A) is a conserved essential enzyme that is implicated as a tumor suppressor based on its central role in phosphorylation-dependent signaling pathways. Protein phosphatase methyl esterase (PME-1) catalyzes specifically the demethylation of the C-terminal Leu309 residue of phosphatase 2A protein catalytic subunit (PP2Ac)
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
regulates PP2A holoenzyme formation
-
-
?
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
reversible methyl-esterification (methylation) of Leu309 in the protein phosphatase 2A catalytic subunit (PP2Ac) is essential for proper biogenesis of the PP2A holoenzyme
-
-
r
[phosphatase 2A protein]-leucine methyl ester + H2O
[phosphatase 2A protein]-leucine + methanol
the enzyme negatively regulates protein phosphatase 2A activity by highly complex mechanisms
-
-
?
additional information
?
-
-
spliced isoform PP2Acalpha2 (lacking exon 5) does not interact with PME-1. Only the longer isoform of PP2A interacts with PME-1
-
-
?
additional information
?
-
-
enzyme is tightly associated with an inactive form of protein phosphatase 2A, and neither activation nor inactivation of its phosphorylase phosphatase activity can be observed by methylation. The presence of a third subunit of protein phosphatase 2A does not prevent methylation or demethylation
-
-
?
additional information
?
-
-
protein phosphatase 2A associated with PME-1 is inactive, function for PME-1 as an enzyme that stabilizes an inactivated pool of protein phosphatase 2A
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-2-(4-fluorophenylsulfonyl)-3-(1-(3-nitrophenylsulfonyl)-1H-pyrrol-2-yl)acrylonitrile
-
compound inhibits PME-1 with more than100fold selectivity relative to other serine hydrolases in human cells. Application reduces the demethylated form of substrate protein phosphatase 2A in living cells
dimethyl 3-cyclopentyl-4-oxo-3-phenylcyclobutane-1,2-dicarboxylate
-
in both MDA-MB-231 and HEK-293T cells, highly potent and selective inhibition of the enzyme with IC50 values of 11.1 nM and 6.4 nM. Analysis reveals complete and selective in situ inhibition of PME-1 with no activity against more than 50 other serine hydrolases detected in MDA-MB-231 and HEK-293T cells. In both cell lines, inhibition results in significant reductions in the levels of demethylated PP2A
AMZ30
PME-1 inhibition by AMZ30 protects against PP2A inactivation and cell apoptosis mediated by alpha-syn
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Protein phosphatase methylesterase-1 (PME-1) expression predicts a favorable clinical outcome in colorectal cancer.
Alzheimer Disease
Discovery and optimization of sulfonyl acrylonitriles as selective, covalent inhibitors of protein phosphatase methylesterase-1.
Carcinoma
DNAH17-AS1 promotes pancreatic carcinoma by increasing PPME1 expression via inhibition of miR-432-5p.
Choriocarcinoma
IMP1 promotes choriocarcinoma cell migration and invasion through the novel effectors RSK2 and PPME1.
Colorectal Neoplasms
Protein phosphatase methylesterase-1 (PME-1) expression predicts a favorable clinical outcome in colorectal cancer.
Glioblastoma
Genetic amplification of PPME1 in gastric and lung cancer and its potential as a novel therapeutic target.
Lung Neoplasms
Genetic amplification of PPME1 in gastric and lung cancer and its potential as a novel therapeutic target.
Neoplasms
Discovery and optimization of sulfonyl acrylonitriles as selective, covalent inhibitors of protein phosphatase methylesterase-1.
Neoplasms
DNAH17-AS1 promotes pancreatic carcinoma by increasing PPME1 expression via inhibition of miR-432-5p.
Neoplasms
Genetic amplification of PPME1 in gastric and lung cancer and its potential as a novel therapeutic target.
Neoplasms
Long non-coding RNA HOTAIR/microRNA-761 sponge regulates PPME1 and further influences cell biological functions in thyroid carcinoma.
Neoplasms
Organic Synthesis Toward Small-Molecule Probes and Drugs Special Feature: Academic cross-fertilization by public screening yields a remarkable class of protein phosphatase methylesterase-1 inhibitors.
Stomach Neoplasms
Genetic amplification of PPME1 in gastric and lung cancer and its potential as a novel therapeutic target.
Thyroid Neoplasms
Long non-coding RNA HOTAIR/microRNA-761 sponge regulates PPME1 and further influences cell biological functions in thyroid carcinoma.
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0006
(E)-2-(4-fluorophenylsulfonyl)-3-(1-(3-nitrophenylsulfonyl)-1H-pyrrol-2-yl)acrylonitrile
Homo sapiens
-
pH 7.5, 37°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
in human glioma cell, high PME-1 expression correlates with tumor progression and kinase inhibitor resistance
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
PME-1 is localised in the cytoplasm of adult rat ventricular myocytes
brenda
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enzyme is predominantly localized in the nucleus and harbors a functional nuclear localization signal. This is in good correlation with the methylation status of its substrate protein phosphates PP2AC, demethylated PP2AC being substantially nuclear
brenda
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negligible localisation in the soluble membrane
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
knockdown of PME-1 downregulates the elevated dmL307-PP2A level induced by GSK-3 activation
malfunction
PME-1 knockdown by siRNA or shRNA inhibits cancer cell growth not only in in vitro but also in in vivo endometrial cancer xenograft models
malfunction
PME-1 knockdown by siRNA or shRNA inhibits cancer cell growth not only in in vitro but also in in vivo endometrial cancer xenograft models
malfunction
targeted disruption of the PME-1 gene causes perinatal lethality in mice. PME-1 knockout mouse embryonic fibroblasts (MEFs) exhibit lower PP2A activity than wild type mouse embryonic fibroblasts. Loss of PME-1 enhances poly-ubiquitination of PP2Ac and shortens the half-life of PP2Ac protein resulting in reduced PP2Ac levels
metabolism
protein methylesterase 1 (PME-1) promotes cancerous phenotypes through the demethylation and inactivation of protein phosphatase 2A
metabolism
the enzyme negatively regulates protein phosphatase 2A activity by highly complex mechanisms. It promotes oncogenic MAPK/ERK and AKT pathway activities in various cancer types. In human glioma, high PME-1 expression correlates with tumor progression and kinase inhibitor resistance
metabolism
the enzyme negatively regulates protein phosphatase 2A activity by highly complex mechanisms. It promotes oncogenic MAPK/ERK and AKT pathway activities in various cancer types. In human glioma, high PME-1 expression correlates with tumor progression and kinase inhibitor resistance
physiological function
-
maturation of C subunit of substrate protein phosphatase 2A is under the surveillance of the enzyme, PP2A methylesterase PPE1, which upon malfunction of PP2A biogenesis, prevents premature generation of the active C subunit and holoenzyme assembly by counteracting the untimely methylation of the C subunit. Deletion of PPE1 decreases the levels of trimeric complexes of protein phosphatase 2A activator RRD2, structural subunit TPD3 and C subunit
physiological function
-
overexpression of enzyme PME-1, but not of an inactive mutant, results in increased demethylation of substrate protein phosphatase PP2AC in the nucleus, whereas overexpression of a cytoplasmic PME-1 mutant lacking the nuclear localization signal results in increased demethylation in the cytoplasm, albeit without any obvious functional consequences. PME-1 associates with an inactive PP2A population, regardless of its esterase activity or localization. RNAi-mediated knock-down of PME-1 in HeLa cellsdoes not result in changes in substrate PP2AC methylation levels
physiological function
-
stable overexpression of PME-1 or of the methylation-site mutant L309DELTA of substrate protein phosphatase 2A C subunit block N2a cell differentiation and neurite formation mediated by leucine carboxyl transferase LCMT1. Selective PME-1 knockdown in N2a cells promotes the formation of very elongated and thin neurite-like projections
physiological function
generation of transgenic mice that overexpress the PP2A methylesterase, protein phosphatase methylesterase-1 (PME-1). PME-1 overexpression enhances behavioral and electrophysiological impairments caused by exogenous Abeta exposure
physiological function
PME-1 methyl-esterase activity is necessary to maintain PP2Ac protein levels. The enzyme protects PP2Ac from ubiquitin/proteasome degradation
Show AA Sequence and Transmembrane Helices (1023 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme forms stable complexes with catalytically inactive mutants of the C subunit of its substrate protein phosphatase 2A. The carboxyl terminus of protein phosphatase 2A C subunit mutant H59Q is important, but not essential, for complex formation
additional information
-
enzyme forms stable complexes with catalytically inactive mutants of the C subunit of its substrate protein phosphatase 2A. The carboxyl terminus of protein phosphatase 2A C subunit mutant H59Q is important, but not essential, for complex formation
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
PME-1 is phosphorylated in vitro by active CaMKI and dephosphorylated by salt-inducible kinase 2 (SIK2)/protein phosphatase 2 (PP2A)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of methylesterase PME-1 by itself and in complex with a protein phosphatase PP2A heterodimeric core enzyme, to 2.0 and 2.7 A resolution. PME-1 directly binds to the active site of protein phosphatase PP2A and this interaction results in the activation of PME-1 by rearranging the catalytic triad into an active conformation. These interactions also lead to inactivation of protein phosphatase PP2A by evicting the manganese ions that are required for the phosphatase activity of PP2A. PME-1 fdisplays a dual role that regulates protein phosphatase PP2A activation, methylation, and holoenzyme assembly in cells
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S156A
-
mutation abolishes the methylesterase activity, residue S156 is a functional active site serine
additional information
-
construction of deletion mutants and expression in HeLa cells. Domain 1 of the enzyme extends from amino acids 1 to 233, domain 2 from amino acids 234 to 284 and domain 3 includes amino acids 285 to 378. Domain 1 of PME-1 does not migrate into the nucleus and domain 3 shows a speckled cytoplasmic distribution, whereas domain 2 is targeted to the nucleus
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
pharmacological activation of glycogen synthase kinase-3beta (GSK-3) by wortmannin (WO) increases PME-1 expression
-
PP2A demethylation is accompanied by upregulated PME-1 expression. alpha-Synuclein increases demethylation of protein phosphatase 2A via downregulation of leucine carboxyl methyltransferase (LCMT-1) expression, and upregulation of protein phosphatase methylesterase PME-1 expression
there is no statistical difference in expression of enzyme in ischemic and non-ischemic human heart failure samples compared with non-failing heart tissue
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
pharmacology
RNAi and pharmacologic inhibition of PME-1 in vitro leads to decreased cell proliferation and invasive growth in endometrial cancer cells. Discovery of more potent PME-1 inhibitors may be beneficial for the treatment of endometrial cancer
medicine
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no difference in methylation of substrate PP2A catalytic subunit at residue Leu-309 in nonischemic heart failure samples compared with non-failing heart, and no statistical difference in expression of enzyme in ischemic and non-ischemic human heart failure samples compared with non-failing heart tissue
medicine
in a xenograft model of endometrial cancer, covalent PME-1 inhibitors decrease cell proliferation and invasive growth in vitro but have no effect in vivo at the concentrations tested. Depletion of PME-1 with shRNA in an endometrial cancer xenograft model significantly reduces tumor growth
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hombauer, H.; Weismann, D.; Mudrak, I.; Stanzel, C.; Fellner, T.; Lackner, D.H.; Ogris, E.
Generation of active protein phosphatase 2A is coupled to holoenzyme assembly
PLoS Biol.
5
e155
2007
Saccharomyces cerevisiae
brenda
Longin, S.; Zwaenepoel, K.; Martens, E.; Louis, J.; Rondelez, E.; Goris, J.; Janssens, V.
Spatial control of protein phosphatase 2A (de)methylation
Exp. Cell Res.
314
68-81
2008
Homo sapiens
brenda
Sontag, J.; Nunbhakdi-Craig, V.; Mitterhuber, M.; Ogris, E.; Sontag, E.
Regulation of protein phosphatase 2A methylation by LCMT1 and PME-1 plays a critical role in differentiation of neuroblastoma cells
J. Neurochem.
115
1455-1465
2010
Mus musculus
brenda
Ikehara, T.; Ikehara, S.; Imamura, S.; Shinjo, F.; Yasumoto, T.
Methylation of the C-terminal leucine residue of the PP2A catalytic subunit is unnecessary for the catalytic activity and the binding of regulatory subunit (PR55/B)
Biochem. Biophys. Res. Commun.
354
1052-1057
2007
Homo sapiens
brenda
Longin, S.; Jordens, J.; Martens, E.; Stevens, I.; Janssens, V.; Rondelez, E.; De Baere, I.; Derua, R.; Waelkens, E.; Goris, J.; Van Hoof, C.
An inactive protein phosphatase 2A population is associated with methylesterase and can be re-activated by the phosphotyrosyl phosphatase activator
Biochem. J.
380
111-119
2004
Oryctolagus cuniculus, Sus scrofa
brenda
Xing, Y.; Li, Z.; Chen, Y.; Stock, J.; Jeffrey, P.; Shi, Y.
Structural mechanism of demethylation and inactivation of protein phosphatase 2A
Cell
133
154-163
2008
Homo sapiens (Q9Y570)
brenda
Ogris, E.; Du, X.; Nelson, K.; Mak, E.; Yu, X.; Lane, W.; Pallas, D.
A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A
J. Biol. Chem.
274
14382-14391
1999
Homo sapiens (Q9Y570), Homo sapiens
brenda
DeGrande, S.; Little, S.; Nixon, D.; Wright, P.; Snyder, J.; Dun, W.; Murphy, N.; Kilic, A.; Higgins, R.; Binkley, P.; Boyden, P.; Carnes, C.; Anderson, M.; Hund, T.; Mohler, P.
Molecular mechanisms underlying cardiac protein phosphatase 2A regulation in heart
J. Biol. Chem.
288
1032-1046
2013
Homo sapiens
brenda
Bachovchin, D.A.; Zuhl, A.M.; Speers, A.E.; Wolfe, M.R.; Weerapana, E.; Brown, S.J.; Rosen, H.; Cravatt, B.F.
Discovery and optimization of sulfonyl acrylonitriles as selective, covalent inhibitors of protein phosphatase methylesterase-1
J. Med. Chem.
54
5229-5236
2011
Homo sapiens
brenda
Bachovchin, D.A.; Mohr, J.T.; Speers, A.E.; Wang, C.; Berlin, J.M.; Spicer, T.P.; Fernandez-Vega, V.; Chase, P.; Hodder, P.S.; Schuerer, S.C.; Nomura, D.K.; Rosen, H.; Fu, G.C.; Cravatt, B.F.
Academic cross-fertilization by public screening yields a remarkable class of protein phosphatase methylesterase-1 inhibitors
Proc. Natl. Acad. Sci. USA
108
6811-6816
2011
Homo sapiens
brenda
Yao, X.Q.; Li, X.C.; Zhang, X.X.; Yin, Y.Y.; Liu, B.; Luo, D.J.; Wang, Q.; Wang, J.Z.; Liu, G.P.
Glycogen synthase kinase-3beta regulates leucine-309 demethylation of protein phosphatase-2A via PPMT1 and PME-1
FEBS Lett.
586
2522-2528
2012
Mus musculus
brenda
Migueleti, D.; Smetana, J.; Nunes, H.; Kobarg, J.; Zanchin, N.
Identification and characterization of an alternatively spliced isoform of the human protein phosphatase 2Aalpha catalytic subunit
J. Biol. Chem.
287
4853-4862
2012
Homo sapiens
brenda
Lee, C.W.; Yang, F.C.; Chang, H.Y.; Chou, H.; Tan, B.C.; Lee, S.C.
Interaction between salt-inducible kinase 2 and protein phosphatase 2A regulates the activity of calcium/calmodulin-dependent protein kinase I and protein phosphatase methylesterase-1
J. Biol. Chem.
289
21108-21119
2014
Homo sapiens
brenda
Longman, M.; Ranieri, A.; Avkiran, M.; Snabaitis, A.
Regulation of PP2AC carboxylmethylation and cellular localisation by inhibitory class G-protein coupled receptors in cardiomyocytes
PLoS ONE
9
e86234
2014
Rattus norvegicus
brenda
Kaur, A.; Westermarck, J.
Regulation of protein phosphatase 2A (PP2A) tumor suppressor function by PME-1
Biochem. Soc. Trans.
44
1683-1693
2016
Mus musculus (Q8BVQ5), Homo sapiens (Q9Y570), Homo sapiens
brenda
Yabe, R.; Tsuji, S.; Mochida, S.; Ikehara, T.; Usui, T.; Ohama, T.; Sato, K.
A stable association with PME-1 may be dispensable for PP2A demethylation - implications for the detection of PP2A methylation and immunoprecipitation
FEBS open bio
8
1486-1496
2018
Mus musculus (Q8BVQ5)
brenda
Tian, H.; Lu, Y.; Liu, J.; Liu, W.; Lu, L.; Duan, C.; Gao, G.; Yang, H.
Leucine carboxyl methyltransferase downregulation and protein phosphatase methylesterase upregulation contribute toward the inhibition of protein phosphatase 2A by alpha-synuclein
Front. Aging Neurosci.
10
173
2018
Mus musculus (Q8BVQ5)
brenda
Hwang, J.; Lee, J.A.; Pallas, D.C.
Leucine carboxyl methyltransferase 1 (LCMT-1) methylates protein phosphatase 4 (PP4) and protein phosphatase 6 (PP6) and differentially regulates the stable formation of different PP4 holoenzymes
J. Biol. Chem.
291
21008-21019
2016
Mus musculus (Q8BVQ5)
brenda
Yabe, R.; Miura, A.; Usui, T.; Mudrak, I.; Ogris, E.; Ohama, T.; Sato, K.
Protein phosphatase methyl-esterase PME-1 protects protein phosphatase 2A from ubiquitin/proteasome degradation
PLoS ONE
10
e0145226
2015
Mus musculus (Q8BVQ5), Mus musculus
brenda
Nicholls, R.E.; Sontag, J.M.; Zhang, H.; Staniszewski, A.; Yan, S.; Kim, C.Y.; Yim, M.; Woodruff, C.M.; Arning, E.; Wasek, B.; Yin, D.; Bottiglieri, T.; Sontag, E.; Kandel, E.R.; Arancio, O.
PP2A methylation controls sensitivity and resistance to beta-amyloid-induced cognitive and electrophysiological impairments
Proc. Natl. Acad. Sci. USA
113
3347-3352
2016
Mus musculus (Q8BVQ5), Mus musculus
brenda
Pusey, M.; Bail, S.; Xu, Y.; Buiakova, O.; Nestor, M.; Yang, J.J.; Rice, L.M.
Inhibition of protein methylesterase 1 decreased cancerous phenotypes in endometrial adenocarcinoma cell lines and xenograft tumor models
Tumour Biol.
37
11835-11842
2016
Homo sapiens (Q9Y570)
brenda
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Release 2023.1 (January 2023)
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