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Protein phosphatase, Mg2+/Mn2+ dependent, 1A

protein phosphatase 1
The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase dephosphorylates, and negatively regulates the activities of, MAP kinases and MAP kinase kinases. It has been shown to inhibit the activation of p38 and JNK kinase cascades induced by environmental stresses. This phosphatase can also dephosphorylate cyclin-dependent kinases, and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to activate the expression of the tumor suppressor gene TP53/p53, which leads to G2/M cell cycle arrest and apoptosis. Three alternatively spliced transcript variants encoding distinct isoforms have been described. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: PP1, CAN, V1a, ACID, PP2A
Papers on protein phosphatase 1
Genome-wide association study reveals sex-specific selection signals against autosomal nucleotide variants.
Lee et al., Seoul, South Korea. In J Hum Genet, Feb 2016
Further analysis with an independent data set confirmed two intragenic association signals in the genes encoding protein phosphatase 1, regulatory subunit 12B (PPP1R12B, intron 12, rs1819043) and dynein, axonemal, heavy chain 11 (DNAH11, intron 61, rs10255013), which are directly involved in the reproductive system.
Targeted redox inhibition of protein phosphatase 1 by Nox4 regulates eIF2α-mediated stress signaling.
Shah et al., Tromsø, Norway. In Embo J, Feb 2016
The serine-threonine protein phosphatase 1 (PP1) deactivates this pathway whereas prolonging eIF2α phosphorylation enhances cell survival.
UIS2: A Unique Phosphatase Required for the Development of Plasmodium Liver Stages.
Nussenzweig et al., Lucknow, India. In Plos Pathog, Jan 2016
In mammalian cells, the de-phosphorylation of eIF2α-P is mediated by the protein phosphatase 1 (PP1).
Synthesis of a norcantharidin-tethered guanosine: Protein phosphatase-1 inhibitors that change alternative splicing.
Stamm et al., Lexington, United States. In Bioorg Med Chem Lett, Jan 2016
UNASSIGNED: Phosphorylation and dephosphorylation of splicing factors play a key role in pre-mRNA splicing events, and cantharidin and norcantharidin analogs inhibit protein phosphatase-1 (PP1) and change alternative pre-mRNA splicing.
Role of glycogen phosphorylase in liver glycogen metabolism.
Agius, Newcastle upon Tyne, United Kingdom. In Mol Aspects Med, Dec 2015
The latter comprises protein phosphatase-1 in conjunction with a glycogen-targeting protein (G-subunit) of the PPP1R3 family.
Protein phosphatase 1 is a key player in nuclear events.
da Cruz E Silva et al., Aveiro, Portugal. In Cell Signal, Dec 2015
For protein phosphatase 1 (PP1) more than 200 binding subunits have been described.
Post-transcriptional Wnt Signaling Governs Epididymal Sperm Maturation.
Niehrs et al., Heidelberg, Germany. In Cell, Dec 2015
Post-transcriptional Wnt signaling impacts spermatozoa through GSK3 by (1) reducing global protein poly-ubiquitination to maintain protein homeostasis; (2) inhibiting septin 4 phosphorylation to establish a membrane diffusion barrier in the sperm tail; and (3) inhibiting protein phosphatase 1 to initiate sperm motility.
Genetic mutations strengthen functional association of LAP1 with DYT1 dystonia and muscular dystrophy.
da Cruz E Silva et al., Aveiro, Portugal. In Mutat Res Rev Mutat Res, Oct 2015
It interacts physically with lamins, torsinA, emerin and protein phosphatase 1; potentially providing a pivotal mechanism for transducing signals across the inner nuclear membrane.
Kinetochore components are required for central spindle assembly.
Dumont et al., Paris, France. In Nat Cell Biol, May 2015
Specifically, central spindle microtubule assembly is dependent on kinetochore recruitment of the scaffold protein KNL-1, as well as downstream partners BUB-1, HCP-1/2(CENP-F) and CLS-2(CLASP); and is negatively regulated by kinetochore-associated protein phosphatase 1 activity.
Preventing proteostasis diseases by selective inhibition of a phosphatase regulatory subunit.
Bertolotti et al., Milano, Italy. In Science, May 2015
Here, we describe Sephin1 (selective inhibitor of a holophosphatase), a small molecule that safely and selectively inhibited a regulatory subunit of protein phosphatase 1 in vivo.
Myocardial glycogen dynamics: new perspectives on disease mechanisms.
Delbridge et al., Melbourne, Australia. In Clin Exp Pharmacol Physiol, Apr 2015
Signalling pathways appear to converge on glycogen regulatory enzymes via insulin (glycogen synthase kinase 3β, protein phosphatase 1, allosteric action of glucose-6-phosphate), β-adrenergic (phosphorylase kinase protein phosphatase 1 inhibitor), and 5' adenosine monophosphate-activated protein kinase (allosteric action of glucose-6-phosphate, direct glycogen binding, insulin receptor).
A PP1-PP2A phosphatase relay controls mitotic progression.
Hagan et al., Manchester, United Kingdom. In Nature, 2015
Although Cdc14 phosphatase drives this reversal in budding yeast, protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) activities have each been independently linked to mitotic exit control in other eukaryotes.
Structures and Activity of New Anabaenopeptins Produced by Baltic Sea Cyanobacteria.
Mazur-Marzec et al., Turku, Finland. In Mar Drugs, 2014
The activity of the peptides against carboxypeptidase A and protein phosphatase 1 as well as chymotrypsin, trypsin and thrombin was tested.
Therapeutic strategies for anchored kinases and phosphatases: exploiting short linear motifs and intrinsic disorder.
Scott et al., Seattle, United States. In Front Pharmacol, 2014
Accordingly, numerous AKAPs bind phosphatases such as protein phosphatase 1 (PP1), calcineurin (PP2B), and PP2A.
Functional interplay between the DNA-damage-response kinase ATM and ARF tumour suppressor protein in human cancer.
Gorgoulis et al., Athens, Greece. In Nat Cell Biol, 2013
Mechanistically, ATM activated protein phosphatase 1, which antagonized Nek2-dependent phosphorylation of nucleophosmin (NPM), thereby liberating ARF from NPM and rendering it susceptible to degradation by the ULF E3-ubiquitin ligase.
Cell surface expression of the major amyloid-β peptide (Aβ)-degrading enzyme, neprilysin, depends on phosphorylation by mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEK) and dephosphorylation by protein phosphatase 1a.
Saido et al., Wako, Japan. In J Biol Chem, 2012
Cell surface expression of the major amyloid-beta peptide (Abeta)-degrading enzyme, neprilysin, depends on phosphorylation by mitogen-activated protein kinase/extracellular signal-regulated kinase kinase (MEK) and dephosphorylation by protein phosphatase 1a.
[Expression and significance of LMP2 and PPM1A in gestational trophoblastic disease].
Xie et al., Hangzhou, China. In Zhonghua Fu Chan Ke Za Zhi, 2011
High expression of LMP2 and low expression of PPM1A might play an important role in the motility and invasiveness of trophoblast cells and malignant transformation of hydatidiform mole.
Protein phosphatase 1A (PPM1A) is involved in human cytotrophoblast cell invasion and migration.
Wang et al., Beijing, China. In Histochem Cell Biol, 2009
The present data indicate that PPM1A plays a critical role in the regulation of normal placentation by inhibiting trophoblast migration and invasion.
PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation.
Yang et al., Houston, United States. In Cell Signal, 2009
Protein phosphatase 1A is essential to terminate I-kappa B Kinase-mediated NF-kappaappaB activation through binding to the activated form of I-kappa B Kinase and dephosphorylating I-kappa B Kinase at the conserved residues Ser177 and Ser181.
Phosphatase PPM1A regulates phosphorylation of Thr-186 in the Cdk9 T-loop.
Rice et al., Houston, United States. In J Biol Chem, 2008
Overexpression of PPM1A and the related PPM1B greatly reduced Cdk9 T-loop phosphorylation
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