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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

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

PP2Cbeta, PPM1B, protein phosphatase 1beta
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 has been shown to dephosphorylate cyclin-dependent kinases (CDKs), and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to cause cell-growth arrest or cell death. Alternative splicing results in multiple transcript variants encoding different isoforms. Additional transcript variants have been described, but currently do not represent full-length sequences. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, SLC3A1, V1a, NF-kappaB
Papers on PP2Cbeta
miR-186 downregulates protein phosphatase PPM1B in bladder cancer and mediates G1-S phase transition.
New
Wang et al., Guangzhou, China. In Tumour Biol, Nov 2015
Protein phosphatase PPM1B is reported to dephosphorylate IKKβ, thereby terminating IKKβ-mediated NF-κB activation.
Ppm1b negatively regulates necroptosis through dephosphorylating Rip3.
New
Impact
Han et al., Xiamen, China. In Nat Cell Biol, Apr 2015
Here we identified protein phosphatase 1B (Ppm1b) as a Rip3 phosphatase and found that Ppm1b restricts necroptosis in two settings: spontaneous necroptosis caused by Rip3 auto-phosphorylation in resting cells, and tumour necrosis factor-α (TNF)-induced necroptosis in cultured cells.
The Groucho-associated phosphatase PPM1B displaces Pax transactivation domain interacting protein (PTIP) to switch the transcription factor Pax2 from a transcriptional activator to a repressor.
New
Patel et al., Ann Arbor, United States. In J Biol Chem, Apr 2015
In this report, we identify the phosphatase PPM1B as an essential component of the Groucho4 repressor complex that is recruited by Pax2 to chromatin.
Identification of Human N-Myristoylated Proteins from Human Complementary DNA Resources by Cell-Free and Cellular Metabolic Labeling Analyses.
Utsumi et al., Yamaguchi, Japan. In Plos One, 2014
As a result, the products of 13 cDNA clones (FBXL7, PPM1B, SAMM50, PLEKHN, AIFM3, C22orf42, STK32A, FAM131C, DRICH1, MCC1, HID1, P2RX5, STK32B) were found to be human N-myristoylated proteins.
Control of adipose tissue expandability in response to high fat diet by the insulin-like growth factor-binding protein-4.
Corvera et al., Worcester, United States. In J Biol Chem, 2014
cDNA microarrays analyzed to identify genes correlating with insulin-stimulated sprouting surprisingly revealed only four positively correlating (Fads3, Tmsb10, Depdc6, and Rasl12) and four negatively correlating (Asph, IGFbp4, Ppm1b, and Adcyap1r1) genes.
PPM1B depletion induces premature senescence in human IMR-90 fibroblasts.
Yang et al., Palmerston North, New Zealand. In Mech Ageing Dev, 2014
PPM1B is a member of the protein phosphatase 2C family and plays a role in negatively regulating p53 and NF-κB thereby possibly attenuating the gene expression program of cellular senescence.
Development of a doxycycline-inducible lentiviral plasmid with an instant regulatory feature.
Park et al., Palmerston North, New Zealand. In Plasmid, 2014
To establish a universal and instant regulatory system without generating Tet-On cell lines, the cDNAs of rtTA and a testing target gene (PPM1B) were cloned in the bi-directional TRE-containing promoters.
Further delineation of genotype-phenotype correlation in homozygous 2p21 deletion syndromes: first description of patients without cystinuria.
Rauch et al., Zürich, Switzerland. In Am J Med Genet A, 2013
Larger homozygous deletions in this region encompassing the PPM1B, SLC3A1, PREPL, and C2orf34 (CAMKMT) genes result in a more severe phenotype, the 2p21 deletion syndrome.
The serine/threonine phosphatase PPM1B (PP2Cβ) selectively modulates PPARγ activity.
Kalkhoven et al., Utrecht, Netherlands. In Biochem J, 2013
We identified the serine/threonine phosphatase PPM1B [PP (protein phosphatase), Mg(2+)/Mn(2+) dependent, 1B; also known as PP2Cβ] as a novel PPARγ-interacting protein.
N-Myristoylation is essential for protein phosphatases PPM1A and PPM1B to dephosphorylate their physiological substrates in cells.
Kobayashi et al., Sendai, Japan. In Biochem J, 2013
PPM [metal-dependent protein phosphatase, formerly called PP2C (protein phosphatase 2C)] family members play essential roles in regulating a variety of signalling pathways.
PPM1B negatively regulates antiviral response via dephosphorylating TBK1.
Yang et al., Harbin, China. In Cell Signal, 2012
Using a functional genomics approach, we have identified PPM1B as a TBK1 phosphatase.
PPM1B and P-IKKβ expression levels correlated inversely with rat gastrocnemius atrophy after denervation.
Liang et al., Taiyuan, China. In Braz J Med Biol Res, 2012
Although several studies have shown that Mg(2+)/Mn(2+)-dependent protein phosphatase 1B (PPM1B) inactivated IKKβ, few studies have investigated the role of PPM1B in denervated skeletal muscle.
Functional interactions between erythroid Krüppel-like factor (EKLF/KLF1) and protein phosphatase PPM1B/PP2Cβ.
GeneRIF
Bieker et al., New York City, United States. In J Biol Chem, 2012
Studies show that Ppm1b plays a multilayered role in regulating the availability and optimal activity of the EKLF protein in erythroid cells.
Protein phosphatase 2Cbetal regulates human pregnane X receptor-mediated CYP3A4 gene expression in HepG2 liver carcinoma cells.
GeneRIF
Chen et al., Memphis, United States. In Drug Metab Dispos, 2010
results implicate a novel and important role for PP2Cbetal in regulating hPXR activity and CYP3A4 expression by inhibiting or desensitizing signaling pathways that negatively regulate the function of pregnane X receptor in liver cells
PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation.
GeneRIF
Yang et al., Houston, United States. In Cell Signal, 2009
Protein phosphatase 1B is mediated dephosphorylation and inactivation of I-kappa B kinase as well as the termination of the Tumor Necrosis Factor-alpha-induced NF-kappaappaB activation.
Phosphatase PPM1A regulates phosphorylation of Thr-186 in the Cdk9 T-loop.
GeneRIF
Rice et al., Houston, United States. In J Biol Chem, 2008
Overexpression of PPM1A and the related PPM1B greatly reduced Cdk9 T-loop phosphorylation
Multi-system disorder syndromes associated with cystinuria type I.
Review
Creemers et al., Leuven, Belgium. In Curr Mol Med, 2008
In atypical HCS an additional gene (C2orf34) is deleted, and finally, in the 2p21 deletion syndrome the open reading frame of PPM1B is also disrupted.
Role of type 2C protein phosphatases in growth regulation and in cellular stress signaling.
Review
Lavi et al., Heidelberg, Germany. In Crit Rev Biochem Mol Biol, 2007
Here, we provide an overview of the involvement of type 2C phosphatases in these two processes, and we show that four of them (PP2Calpha, PP2Cbeta, ILKAP, and PHLPP) can be expected to function as tumor suppressor proteins, and one as an oncoprotein (PP2Cdelta /Wip1).
Disruption of the mouse protein Ser/Thr phosphatase 2Cbeta gene leads to early pre-implantation lethality.
GeneRIF
Tamura et al., Sendai, Japan. In Mech Dev, 2007
These observations suggest that relatively high PP2Cbeta expression is specifically required during the early stages of pre-implantation development.
Protein phosphatases types 2Calpha and 2Cbeta in apoptosis.
Review
Krieglstein et al., Münster, Germany. In Biochem Soc Trans, 2006
Those fatty acids capable of activating PP2Calpha and PP2Cbeta in vitro induce apoptosis in various cell types as shown here for neurons and endothelial cells.
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