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Evidence for PPP2R4 as a haploinsufficient tumor suppressor gene, defining a high-penetrance genetic mechanism for PP2A (show PPP2R2B Proteins) inhibition in human cancer.
data indicate that PTPalpha (show PTPRA Proteins) and FAK (show PTK2 Proteins), which are enriched in FAs (show FAS Proteins), interact with IP3R1 (show ITPR1 Proteins) at adjacent ER sites to spatially sequester IL-1 (show IL1A Proteins)-induced Ca(2 (show CA2 Proteins)+) signalling
oocyte-specific deletion of Ppp2r1a (show PPP2R1A Proteins) led to severe female subfertility without affecting follicle survival, growth, and ovulation.
A Pak1-PP2A-ERM signaling axis mediates F-actin rearrangement and degranulation in mast cells.
PP2A (show PPP2R2B Proteins) (Protein Phosphatase 2A(Twins)) counteracts Plk4 (show PLK4 Proteins) autophosphorylation, thus stabilizing Plk4 (show PLK4 Proteins) and promoting centriole duplication
PP2A (show PPP2R2B Proteins)-A alpha transcriptional regulation is mediated by multiple factors including AP-2alpha (show TFAP2A Proteins), CREB (show CREB1 Proteins), ETS-1 (show ETS1 Proteins), and SP-1 (show SP1 Proteins)
Data show that DSB promote PP2A to associate with Ku 70 and Ku 86.
findings show that ectopic expression of the phosphotyrosyl phosphatase activator PTPA induces cell death in mammalian cells via a mechanism involving caspase-3 (show CASP3 Proteins)-dependent apoptosis
oxidative stress regulates the phosphorylation status of nonribosomal rpS3 (show RPS3 Proteins) by both activating PKCdelta (show PKCd Proteins) and blocking the PP2A (show PPP2R2B Proteins) interaction with rpS3 (show RPS3 Proteins)
protein phosphatase 2A overexpression in NIH 3T3 cells
Isoliensinine suppresses NF-kappaB (show NFKB1 Proteins) in hepatocellular carcinoma cells through impairing PP2A/I2PP2A interaction and stimulating PP2A-dependent p65 (show GORASP1 Proteins) dephosphorylation at Ser536
BIR (show KCNJ11 Proteins) domain of XIAP (show XIAP Proteins) activated the protein phosphatase 2 (PP2A) activity by decreasing the phosphorylation of PP2A at Tyr307 in its catalytic subunit, PP2A-C. Such activated PP2A prevented the deviant phosphorylation and activation of MAPK (show MAPK1 Proteins) kinases/MAPKs, their downstream effector c-Jun (show JUN Proteins); and in turn inhibiting transcription of c-Jun (show JUN Proteins)-regulated miR (show MLXIP Proteins)-200a
T-type channel signaling is redirected towards the activation of the kinase Akt1 (show AKT1 Proteins), leading to increased expression of the anti-apoptotic protein survivin (show BIRC5 Proteins), and a decrease in the pro-apoptotic mediator FoxO3A (show FOXO3 Proteins). Finally, in iPAH cells, Akt1 (show AKT1 Proteins) is no longer able to regulate caspase 9 (show CASP9 Proteins) activation, whereas T-type channel overexpression reverses PP2A defect in iPAH cells but reinforces the deleterious effects of Akt1 (show AKT1 Proteins) activation
The present results indicate that rs959627 predicts PPP2R2 B mRNA prefrontal expression in two independent post-mortem datasets as well as lateral prefrontal activity during working memory in healthy subjects and suggest that genetic modulation of signal transduction mediated by PP2A affects complex biological phenotypes of relevance for cognitive behavior.
the present study suggested that PP2A has an important role in regulating mast cell beta2-adrenoceptors
The results of this study demonstrated that HBx of hepatitis B virus impairs interferon (show IFNA Proteins) signaling via increased expression of SOCS3 (show SOCS3 Proteins) and PP2A.
The current study describes a novel pathogenic mechanism of action for human polyomavirus 6 small tumor (sT) antigen which involves binding to protein phosphatase 2A (PP2A) via its WFG motif and zinc binding sites for activation of PP2A's downstream oncogenic pathways (MEK (show MAP2K1 Proteins)/ERK (show EPHB2 Proteins)/c-Jun (show JUN Proteins)).
The aim of this review is to shed light on the role of four different phosphatases (PTEN, PP2A, CDC25 (show RASGRF1 Proteins) and DUSP1 (show DUSP1 Proteins)) in five different solid tumors (breast cancer, lung cancer, pancreatic cancer, prostate cancer and ovarian cancer), in order to better understand the most frequent and aggressive primary cancer of the central nervous system, glioblastoma.
Oncoprotein CIP2A (show KIAA1524 Proteins) is stabilized via interaction with tumor suppressor PP2A/B56
Such effect by miR (show MLXIP Proteins)-429 was again abolished with AMPKalpha1 (show PRKAA1 Proteins) silence or mutation. Together, we propose that PP2A-c silence by miR (show MLXIP Proteins)-429 activates AMPK (show PRKAA1 Proteins) and protects osteoblastic cells from Dex.
Protein phosphatase 2A is one of the four major Ser/Thr phosphatases and is implicated in the negative control of cell growth and division. Protein phosphatase 2A holoenzymes are heterotrimeric proteins composed of a structural subunit A, a catalytic subunit C, and a regulatory subunit B. The regulatory subunit is encoded by a diverse set of genes that have been grouped into the B/PR55, B'/PR61, and B''/PR72 families. These different regulatory subunits confer distinct enzymatic specificities and intracellular localizations to the holozenzyme. The product of this gene belongs to the B' family. This gene encodes a specific phosphotyrosyl phosphatase activator of the dimeric form of protein phosphatase 2A. Alternative splicing results in multiple transcript variants encoding different isoforms.
PP2A subunit A isoform PR65-alpha
, PP2A subunit A isoform R1-alpha
, protein phosphatase PP2A
, serine/threonine protein phosphatase A subunit type 2A
, serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
, PP2A phosphatase activator
, PP2A subunit B' isoform PR53
, phosphotyrosyl phosphatase activator
, protein phosphatase 2A, regulatory subunit B' (PR 53)
, serine/threonine-protein phosphatase 2A activator
, serine/threonine-protein phosphatase 2A regulatory subunit B'
, PP2A, subunit B', PR53 isoform
, serine/threonine-protein phosphatase 2A regulatory subunit 4
, protein tyrosine phosphatase, receptor type, A