EC Number   |
General Information |
Reference |
|---|
   3.1.1.89 | malfunction |
knockdown of PME-1 downregulates the elevated dmL307-PP2A level induced by GSK-3 activation |
731809 |
| 3.1.1.89 | 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 |
749865 |
| 3.1.1.89 | 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 |
751932 |
| 3.1.1.89 | metabolism |
protein methylesterase 1 (PME-1) promotes cancerous phenotypes through the demethylation and inactivation of protein phosphatase 2A |
752312 |
| 3.1.1.89 | 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 |
749865 |
| 3.1.1.89 | 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 |
752043 |
| 3.1.1.89 | 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 |
682480 |
| 3.1.1.89 | 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 |
714919 |
| 3.1.1.89 | physiological function |
PME-1 methyl-esterase activity is necessary to maintain PP2Ac protein levels. The enzyme protects PP2Ac from ubiquitin/proteasome degradation |
751932 |
| 3.1.1.89 | 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 |
715981 |
