Database for Annotation, Visualization and Integrated Discovery 2.1
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protein phosphatase 1 catalytic subunit alpha(PPP1CA) protein phosphatase 1 catalytic subunit alpha(PPP1CA) Related Genes Homo sapiens
GENERIF_SUMMARY PP1C has a role in binding to PKR protein kinase for its phosphorylation and disruption of dimerization, PP1C and Inh2 bind to KPI2 to form a regulatory complex that is localized to membranes, PPICalpha essential in proliferation in HeLa cells, PP1alpha expression interferes with oncogenic transformation., These findings provide a putative mechanism by which transcriptional activity of hnRNP K can be discretely controlled through the regulation of PP1 activity., These data suggest that amplification and overexpression of the PP1alpha gene, PPP1CA, may be involved in oral squamous cell carcinoma cell tumorigenesis and/or progression., Bcl-2 by competing with IP3R1 for the binding of PP1 can reduce the inositol trisphosphate-mediated calcium signal and protect cells from mitochondrial dysfunction and cell death., accumulation of C(16)-ceramide in mitochondria formed from the protein kinase C-dependent salvage pathway results at least in part from the action of longevity-assurance homologue 5, and the generated ceramide modulates the p38 cascade via PP1, data indicate that PP1alpha is a downstream target of the NGF/Egr-1/Cdk5 pathway during NGF-induced differentiation of PC12 cells and suggest that PP1 phosphorylation promotes neuronal differentiation, Protein phosphatase 1 regulates assembly and function of the beta-catenin degradation complex., Results suggest that the protein-tyrosine phosphatase domain of tensin exhibits isoform-specific association with PP1alpha in a restricted spatial region of adhesions that are formed during cell migration., Sds22 and Inhibitor-3 form a heterotrimeric complex with PP1, both in cell lysates and after purification. A pool of PP1 is complexly controlled by both Sds22 and Inhibitor-3., PP2B and PP1alpha cooperatively disrupt 7SK snRNP to release P-TEFb for transcription in response to Ca2+ signaling., Conserved together throughout eukaryotic evolution, I-2, PP1 and Aurora B function interdependently during mitosis., The PP1, Protein phosphatase 1 binding occurs through a conserved RVXF motif found in the KH domain of AKAP149., novel interaction between the catalytic subunit of protein phosphatase 1alpha and MEF2A. Interaction occurs within the nucleus, and binding of PP1alpha to MEF2 potently represses MEF2-dependent transcription, AR may function as a PP1 regulatory subunit and mediate PP1a recruitment to chromatin, where it can modulate transcription and splicing., Results suggest that PP1alpha bound to tensin1 has effects in reducing migration and invasion that are not mediated through DLC-1, and show the importance of PP1alpha binding to tensin1 for the regulation of cell polarization, migration, and invasion., conclusion, PP-1 ( PP-1alpha or PP-1beta ) acts as a major phosphatase to dephosphorylate AKT1 at Thr-450 and thus modulate its functions in regulating gene expression, cell survival and differentiation., mammalian Wdr82 functions in a variety of cellular processes; PTW/PP1 phosphatase complex (PNUTS, Tox4, Wdr82, PP1) has a role in the regulation of chromatin structure during the transition from mitosis into interphase, CSK21 and PP1A, whose functions are intimately associated with cell cycle regulation, might play key role in gliomagenesis., The deregulation of cellular NIPP1/PP1 holoenzyme affects RNAPII phosphorylation and pointing to NIPP1 as a potential regulatory factor in RNAPII-mediated transcription., Could use the urinary hTERT, SENP1, PPP1CA, and MCM5 mRNA to detect bladder cancer recurrence., PP1A and ASPP2 play a critical role in promoting TAZ function by antagonizing the LATS kinase through TAZ dephosphorylation., Results demonstrate that PP1-mediated inhibition of the key anti-apoptotic protein, Akt, plays an important role in SPH-mediated apoptosis in Jurkat cells., Results identify a molecular pathway by which leptin confers inhibitory action on insulin secretion, and impaired PP-1 inhibition by leptin may be involved in dysfunction of the adipoinsular axis during the development of hyperinsulinemia and NIDDM., Changes in cell polarity proteins Par-3 and PP-1 are associated with altered expression and assembly of tight junction proteins claudin-2, -3, -5 and -7 and ZO-1, causing paracellular leakage in active coeliac disease., These findings define a novel molecular mechanism that YAP2 is positively regulated by PP1-mediated dephosphorylation in the cell survival., We have identified a novel mechanism for direct activation of P-Rex1 through PP1alpha-dependent dephosphorylation., Studies suggest that any change in substrate specificity of the spinophilin , Studies indicate that the Ser/Thr phosphatases PP1 and PP2A are responsible for the dephosphorylation and activation of Rb proteins., a novel, acute mechanism of ERM regulation dependent on PP1alpha and plasma membrane ceramide., Results identify specific protein phosphatase 1alpha-interacting proteins in human brain., Studies indicate that the diversity of the PP1 interactome and the properties of the PP1 binding code account for the exquisite specificity of PP1 in vivo., Data show that knockdown of the catalytic subunit of PP1 (PP1Calpha), but not PP2A (PP2ACalpha), increased pS137-PFN1 levels., analysis of selective regulation of NR2B by protein phosphatase-1 for the control of the NMDA receptor in neuroprotection, 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., PP1/NIPP1 is a novel molecular compass that controls directed cell migration., The molecular basis by which NIPP1 directs PP1 substrate specificity in the nucleus., PP-1alpha and PP-1gamma not only antagonize each other in lung cancer cells, but also display differential functions in tumorigenicity., PPP1C isoforms have distinct contribution to the outside-in alphaIIbbeta3 signalling-dependent functions in HEK293 alphaIIbbeta3 cells., The protein phosphatase 1 directly interacts with Mdmx and specifically dephosphorylates Mdmx at Ser367., Findings indicate that phosphatases PP1alpha and PP1gamma are key regulators of RIG-I and MDA5 antiviral signaling., Data indicate that the protein phosphatase 1 (PP1) binding domain in nuclear membrane protein lamina associated polypeptide 1B (LAP1B) was here identified as the REVRF motif at amino acids 55-59., Data show that tumor necrosis factor (TNF) tolerance in monocytic cells differentially inhibits NF-kappaB/transcription factor AP-1 and protein phosphatase 1 (PP1)-associated signaling., PP1alpha and class I histone deacetylase (HDAC1/2/3) signaling pathways are essential for the stress-induced BRD4 release from chromatin., 14-3-3zeta regulates nuclear trafficking of PP1alpha in mammalian cells, PP1alpha is an important proximal effector of Manumycin-A mediated lymphoma cell apoptosis., Data suggest that activation of TAZ (tafazzin) inhibits adipogenesis in mesenchymal stem cells; interaction of TAZ and protein phosphatases (PP1A, PP2A) up-regulates dephosphorylation and transport of TAZ to cell nucleus., Protein phosphatase 1 (PP1) activity is critical for radiosensitization in non-small cell lung cancer cells and PP1 activators can serve as promising radiosensitizers to improve therapeutic efficacy., ATG16L1 as a bona fide physiological CSNK2 and PPP1 substrate, which reveals a novel molecular link from CSNK2 to activation of the autophagy-specific ATG12-ATG5-ATG16L1 complex and autophagy induction, PARD3 promotes interaction between PP1A and LATS1 to induce LATS1 dephosphorylation and inactivation,leading to dephosphorylation and activation of TAZ, activation of the Nherf1-PP1alpha-TAZ pathway in osteoblasts is targeted by histone deacetylase inhibitors, Both PP-1 and PP-2A are directly involved in regulating eye development, and are aberrantly expressed in cataract and glaucoma patients. (Review),
SP_COMMENT catalytic activity:A phosphoprotein + H(2)O = a protein + phosphate., caution:The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data., cofactor:Binds 1 iron ion per subunit., cofactor:Binds 1 manganese ion per subunit., enzyme regulation:The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress., function:Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II., online information:The things we forget -Issue 32 of March 2003, similarity:Belongs to the PPP phosphatase family., similarity:Belongs to the PPP phosphatase family. PP-1 subfamily., subunit:PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A, PPP1R3B, PPP1R3C and PPP1R3D mediate binding to glycogen. Interacts with PPP1R9A and PPP1R9B. Part of a complex containing PPP1R15B, PP1 and NCK1/2 (By similarity). Interacts with PPP1R7. PPP1R15A and PPP1R15B mediate binding to EIF2S1. Interacts with HHV-1 ICP34.5.,