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Protein phosphatase 2, catalytic subunit, alpha isozyme

Replication Protein C, PP2Ac
This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. This gene encodes an alpha isoform of the catalytic subunit. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PP2A, ACID, CAN, V1a, PP1
Papers on Replication Protein C
Inflammatory stimuli promote growth and invasion of pancreatic cancer cells through NF-κB pathway dependent repression of PP2Ac.
Li et al., Suzhou, China. In Cell Cycle, Feb 2016
We used lipopolysaccharide (LPS) and macrophage-conditioned medium (MCM) to establish in vitro inflammation models, and investigated whether inflammatory stimuli affect pancreatic cancer cell growth and invasion PP2A catalytic subunit (PP2Ac)-dependently.
Quantitative proteomics reveals novel protein interaction partners of PP2A catalytic subunit in pancreatic β-cells.
Yi et al., Detroit, United States. In Mol Cell Endocrinol, Feb 2016
Using co-immunoprecipitation (co-IP) and tandem mass spectrometry, we globally identified the protein interaction partners of the PP2A catalytic subunit (PP2Ac) in insulin-secreting pancreatic β-cells.
Melatonin relieves neuropathic allodynia through spinal MT2-enhanced PP2Ac and downstream HDAC4 shuttling-dependent epigenetic modification of hmgb1 transcription.
Peng et al., Taipei, Taiwan. In J Pineal Res, Feb 2016
Here, we report that together with behavioral allodynia, spinal nerve ligation (SNL) induced a decrease in the expression of catalytic subunit of phosphatase 2A (PP2Ac) and enhanced histone deacetylase 4 (HDAC4) phosphorylation and cytoplasmic accumulation, which epigenetically alleviated HDAC4-suppressed hmgb1 gene transcription, resulting in increased High-mobility group protein B1 (HMGB1) expression selectively in the ipsilateral dorsal horn of rats.
Upregulation of PP2Ac predicts poor prognosis and contributes to aggressiveness in hepatocellular carcinoma.
Xu et al., Shanghai, China. In Cancer Biol Ther, Dec 2015
UNASSIGNED: Protein phosphatase 2A (PP2A) is a heterotrimeric protein phosphatase consisting of a 36-kD catalytic C subunit (PP2Ac).
GSK-3β is Dephosphorylated by PP2A in a Leu309 Methylation-Independent Manner.
Liu et al., Nantong, China. In J Alzheimers Dis, Nov 2015
Alteration of methylation of the catalytic subunit of PP2A (PP2Ac) at Leu309 did not affect GSK-3β phosphorylation.
The composition and function of the striatin-interacting phosphatases and kinases (STRIPAK) complex in fungi.
Teichert et al., Bochum, Germany. In Fungal Genet Biol, Nov 2015
These subunits (and their mammalian homologs) are PRO11 (striatin), PRO22 (STRIP1/2), SmMOB3 (Mob3), PRO45 (SLMAP), and PP2AA, the structural, and PP2Ac, the catalytic subunits of protein phosphatase 2A (PP2A).
Protein Phosphatase Methyl-Esterase PME-1 Protects Protein Phosphatase 2A from Ubiquitin/Proteasome Degradation.
Sato et al., Yamaguchi, Japan. In Plos One, 2014
Protein phosphatase methyl esterase (PME-1) catalyzes specifically the demethylation of the C-terminal Leu309 residue of PP2A catalytic subunit (PP2Ac).
Phospholipase C-related but catalytically inactive protein, PRIP as a scaffolding protein for phospho-regulation.
Hirata et al., Fukuoka, Japan. In Adv Biol Regul, 2013
We have reported that PRIP interacts with the catalytic subunits of protein phosphatase 1 and 2A (PP1c and PP2Ac), depending on the phosphorylation of PRIP.
The E3 ubiquitin ligase midline 1 promotes allergen and rhinovirus-induced asthma by inhibiting protein phosphatase 2A activity.
Mattes et al., Newcastle, Australia. In Nat Med, 2013
MID1 decreases protein phosphatase 2A (PP2A) activity through association with its catalytic subunit PP2Ac.
Hyperactivation of protein phosphatase 2A in models of glucolipotoxicity and diabetes: potential mechanisms and functional consequences.
Matti et al., Detroit, United States. In Biochem Pharmacol, 2012
Herein, we provide an overview of PP2A subunit expression and activity in in vitro and in vivo models of glucolipotoxicity and diabetes, and revisit the existing data, which are suggestive of alterations in post-translational methylation, phosphorylation and nitration of PP2Ac under these conditions.
Glycogen synthase kinase-3β regulates leucine-309 demethylation of protein phosphatase-2A via PPMT1 and PME-1.
Liu et al., Wuhan, China. In Febs Lett, 2012
GSK-3beta can inhibit PP2A by increasing the inhibitory L309-demethylation involving upregulation of PME-1 and inhibition of PPMT1
Identification and characterization of an alternatively spliced isoform of the human protein phosphatase 2Aα catalytic subunit.
Zanchin et al., Campinas, Brazil. In J Biol Chem, 2012
Identification and characterization of an alternatively spliced isoform of the human protein phosphatase 2Aalpha catalytic subunit.
[Targeting of PP2A enzymes by viral proteins and cancer signalling].
Garcia et al., Paris, France. In Med Sci (paris), 2011
A biological strategy, used by various viruses based on the targeting of PP2A enzymes by viral proteins, in order to specifically deregulate cellular pathways of their hosts.
EphB3 suppresses non-small-cell lung cancer metastasis via a PP2A/RACK1/Akt signalling complex.
Xie et al., Shanghai, China. In Nat Commun, 2011
EphB3 suppresses non-small-cell lung cancer metastasis via a PP2A/RACK1/Akt signalling complex
Protein phosphatase 1 dephosphorylates profilin-1 at Ser-137.
Diamond et al., Saint Louis, United States. In Plos One, 2011
Data show that knockdown of the catalytic subunit of PP1 (PP1Calpha), but not PP2A (PP2ACalpha), increased pS137-PFN1 levels.
The tuberous sclerosis gene products hamartin and tuberin are multifunctional proteins with a wide spectrum of interacting partners.
Hengstschläger et al., Vienna, Austria. In Mutat Res, 2008
Tuberin interacts with 14-3-3 beta,epsilon,gamma,eta,sigma,tau,zeta, Akt, AMPK, CaM, CRB3/PATJ, cyclin A, cyclins D1, D2, D3, Dsh, ERalpha, Erk, FoxO1, HERC1, HPV16 E6, HSCP-70, HSP70-1, MK2, NEK1, p27KIP1, Pam, PC1, PP2Ac, Rabaptin-5, Rheb, RxRalpha/VDR and SMAD2/3.
Rb2/p130 and protein phosphatase 2A: key mediators of ovarian carcinoma cell growth suppression by all-trans retinoic acid.
Soprano et al., Philadelphia, United States. In Oncogene, 2006
The sites at which PP2A catalytic subunit (PP2Ac) interacts with Rb2/p130 have been localized to the NLS in the C-terminus of Rb2/p130.
Genetic manipulation of the biosynthetic process leading to phoslactomycins, potent protein phosphatase 2A inhibitors.
Reynolds et al., Portland, United States. In J Ind Microbiol Biotechnol, 2006
The cysteine-269 residue of PP2Ac-subunit has been shown to be the site of covalent modification by PLMs.
MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation.
Schweiger et al., Innsbruck, Austria. In Nat Genet, 2001
We show that mutation of MID1 leads to a marked accumulation of the catalytic subunit of protein phosphatase 2A (PP2Ac), a central cellular regulator.
HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint.
Korsmeyer et al., Saint Louis, United States. In Nature, 1997
We observed that the protein HOX11 interacted with protein serine-threonine phosphatase 2A catalytic subunit (PP2AC), as well as protein phosphatase 1 (PP1C) in mammalian cells.
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