U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination
    • Showing Current items.

    PPP1CC protein phosphatase 1 catalytic subunit gamma [ Homo sapiens (human) ]

    Gene ID: 5501, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    High expression of PPP1CC promotes NHEJ-mediated DNA repair leading to radioresistance and poor prognosis in nasopharyngeal carcinoma.

    High expression of PPP1CC promotes NHEJ-mediated DNA repair leading to radioresistance and poor prognosis in nasopharyngeal carcinoma.
    Feng P, Wang Y, Liu N, Chen Y, Hu Y, Huang Z, Liu Y, Zheng S, Jiang T, Xiao X, Dai W, Huang P, Xia Y.,

    07/16/2024
    TIMAP, a Regulatory Subunit of Protein Phosphatase 1, Inhibits In Vitro Neuronal Differentiation.

    TIMAP, a Regulatory Subunit of Protein Phosphatase 1, Inhibits In Vitro Neuronal Differentiation.
    Fonódi M, Thalwieser Z, Csortos C, Boratkó A., Free PMC Article

    01/12/2024
    PP1gamma regulates neuronal insulin signaling and aggravates insulin resistance leading to AD-like phenotypes.

    PP1γ regulates neuronal insulin signaling and aggravates insulin resistance leading to AD-like phenotypes.
    Yadav Y, Sharma M, Dey CS., Free PMC Article

    04/26/2023
    Structure of the SHOC2-MRAS-PP1C complex provides insights into RAF activation and Noonan syndrome.

    Structure of the SHOC2-MRAS-PP1C complex provides insights into RAF activation and Noonan syndrome.
    Bonsor DA, Alexander P, Snead K, Hartig N, Drew M, Messing S, Finci LI, Nissley DV, McCormick F, Esposito D, Rodriguez-Viciana P, Stephen AG, Simanshu DK., Free PMC Article

    10/22/2022
    Structure-function analysis of the SHOC2-MRAS-PP1C holophosphatase complex.

    Structure-function analysis of the SHOC2-MRAS-PP1C holophosphatase complex.
    Kwon JJ, Hajian B, Bian Y, Young LC, Amor AJ, Fuller JR, Fraley CV, Sykes AM, So J, Pan J, Baker L, Lee SJ, Wheeler DB, Mayhew DL, Persky NS, Yang X, Root DE, Barsotti AM, Stamford AW, Perry CK, Burgin A, McCormick F, Lemke CT, Hahn WC, Aguirre AJ., Free PMC Article

    10/1/2022
    Structure of the MRAS-SHOC2-PP1C phosphatase complex.

    Structure of the MRAS-SHOC2-PP1C phosphatase complex.
    Hauseman ZJ, Fodor M, Dhembi A, Viscomi J, Egli D, Bleu M, Katz S, Park E, Jang DM, Porter KA, Meili F, Guo H, Kerr G, Mollé S, Velez-Vega C, Beyer KS, Galli GG, Maira SM, Stams T, Clark K, Eck MJ, Tordella L, Thoma CR, King DA., Free PMC Article

    10/1/2022
    The role of LR-TIMAP/PP1c complex in the occurrence and development of no-reflow.

    The role of LR-TIMAP/PP1c complex in the occurrence and development of no-reflow.
    Quan X, Liu X, Qin X, Wang Y, Sun T, Li Z, Zhu L, Chen J, Zhou Y, Singh S, Dong H, Zhang Z, Zhang H., Free PMC Article

    11/6/2021
    Aurora B regulates PP1gamma-Repo-Man interactions to maintain the chromosome condensation state.

    Aurora B regulates PP1γ-Repo-Man interactions to maintain the chromosome condensation state.
    Xin G, Fu J, Luo J, Deng Z, Jiang Q, Zhang C., Free PMC Article

    03/13/2021
    our work has identified both the mechanism of SLFN11 activation and PPP1CC as the enzyme responsible for its activation. Our findings open up future studies of the PPP1CC subunit(s) involved in SLFN11 activation and the putative kinase(s) that inactivates SLFN11.

    Dephosphorylation activates the interferon-stimulated Schlafen family member 11 in the DNA damage response.
    Malone D, Lardelli RM, Li M, David M., Free PMC Article

    05/9/2020
    Here the authors show how Ki-67 and RepoMan form mitotic exit phosphatases by recruiting PP1, how they distinguish between distinct PP1 isoforms and how the assembly of these two holoenzymes are dynamically regulated by Aurora B kinase during mitosis.

    The Ki-67 and RepoMan mitotic phosphatases assemble via an identical, yet novel mechanism.
    Kumar GS, Gokhan E, De Munter S, Bollen M, Vagnarelli P, Peti W, Page R., Free PMC Article

    11/4/2017
    Data suggest that PPP1CC catalyzes hydrolysis of an assortment of substrates (aryl methylphosphonates, fluorophosphate esters, phosphorothioate esters, phosphodiesters); conservative mutation of R221 to K results in a mutant that is more effective catalyst toward monoanionic substrates; PPP1CC does not catalyze the hydrolysis of a sulfate ester, which is unexpected.

    Transition States and Control of Substrate Preference in the Promiscuous Phosphatase PP1.
    Chu Y, Williams NH, Hengge AC.

    08/12/2017
    PP1gamma is upregulated in hepatocellular carcinoma (HCC) cell lines and HCC specimens and promotes cancer cell proliferation through regulation of p53. High expression of PP1gamma in HCC cells contributed to doxorubicin resistance.

    Overexpression of Protein Phosphatase 1γ (PP1γ) Is Associated with Enhanced Cell Proliferation and Poor Prognosis in Hepatocellular Carcinoma.
    Li C, Wu M, Zong G, Wan C, Liu Q, Zhou H, Hua L, Chen Y, Chen X, Lu C.

    07/15/2017
    knock-down of PP1gamma alleviates glioma proliferation by reducing p65 transportation into the nucleus.

    Protein phosphatase 1γ regulates the proliferation of human glioma via the NF-κB pathway.
    Bao Z, Duan C, Gong C, Wang L, Shen C, Wang C, Cui G.

    12/31/2016
    PP1gamma may be a novel target of the HPV-16 oncoproteins and indicate that it might be a potential novel biomarker for HPV-16 induced malignancy.

    HPV-16 impairs the subcellular distribution and levels of expression of protein phosphatase 1γ in cervical malignancy.
    Seiki T, Nagasaka K, Kranjec C, Kawana K, Maeda D, Nakamura H, Taguchi A, Matsumoto Y, Arimoto T, Wada-Hiraike O, Oda K, Nakagawa S, Yano T, Fukayama M, Banks L, Osuga Y, Fujii T., Free PMC Article

    01/16/2016
    Although no obvious defects in the progression of mitosis were observed, the timing of dephosphorylation of the mutant Ki67 in anaphase was delayed, indicating that Ki67 itself is one of the substrates of PP1gamma-Ki67.

    Ki67 antigen contributes to the timely accumulation of protein phosphatase 1γ on anaphase chromosomes.
    Takagi M, Nishiyama Y, Taguchi A, Imamoto N., Free PMC Article

    12/20/2014
    the lipin-1 N-terminal domain is important for its catalytic activity, nuclear localization, and binding to PP-1cgamma

    Conserved residues in the N terminus of lipin-1 are required for binding to protein phosphatase-1c, nuclear translocation, and phosphatidate phosphatase activity.
    Kok BPC, Skene-Arnold TD, Ling J, Benesch MGK, Dewald J, Harris TE, Holmes CFB, Brindley DN., Free PMC Article

    06/21/2014
    Protein phosphatase 1gamma promotes the alternative splicing of CaMKIIdelta through its interaction with alternative splice factor.

    PP1γ functionally augments the alternative splicing of CaMKIIδ through interaction with ASF.
    Huang C, Cao W, Liao R, Wang J, Wang Y, Tong L, Chen X, Zhu W, Zhang W.

    03/15/2014
    PP-1alpha and PP-1gamma not only antagonize each other in lung cancer cells, but also display differential functions in tumorigenicity.

    PP-1α and PP-1γ display antagonism and differential roles in tumorigenicity of lung cancer cells.
    Chen PC, Li C, Wang D, Luo ZW, Fu SJ, Li X, Li ZL, Chen XW, Li L, Huang ZX, Ji WK, Hu WF, Hu XH, Deng M, Gong L, Chen HG, Liu JP, Li DW.

    09/21/2013
    PPP1C isoforms have distinct contribution to the outside-in alphaIIbbeta3 signalling-dependent functions in HEK293 alphaIIbbeta3 cells.

    Distinct roles for the α , β and γ1 isoforms of protein phosphatase 1 in the outside-in αIIbβ3 integrin signalling-dependent functions.
    Alrehani N, Pradhan S, Khatlani T, Kailasam L, Vijayan KV., Free PMC Article

    06/29/2013
    Findings indicate that phosphatases PP1alpha and PP1gamma are key regulators of RIG-I and MDA5 antiviral signaling.

    Dephosphorylation of the RNA sensors RIG-I and MDA5 by the phosphatase PP1 is essential for innate immune signaling.
    Wies E, Wang MK, Maharaj NP, Chen K, Zhou S, Finberg RW, Gack MU., Free PMC Article

    05/18/2013
    When the Px(T)PxR motif is deleted or mutated via insertion of a phosphorylation site mimic (T311D), PP-1c fails to bind to all three ASPP proteins, ASPP1, ASPP2 and iASPP.

    Molecular mechanisms underlying the interaction of protein phosphatase-1c with ASPP proteins.
    Skene-Arnold TD, Luu HA, Uhrig RG, De Wever V, Nimick M, Maynes J, Fong A, James MN, Trinkle-Mulcahy L, Moorhead GB, Holmes CF.

    03/9/2013
    Depletion of PP1gamma enhances the localization of the SMN complex and snRNPs to Cajal bodies.

    A role for protein phosphatase PP1γ in SMN complex formation and subnuclear localization to Cajal bodies.
    Renvoisé B, Quérol G, Verrier ER, Burlet P, Lefebvre S.

    01/26/2013
    NUAK1 and PPP1CC are identified as positional candidate loci for skeletal muscle strength phenotypes.

    Identification and prioritization of NUAK1 and PPP1CC as positional candidate loci for skeletal muscle strength phenotypes.
    Windelinckx A, De Mars G, Huygens W, Peeters MW, Vincent B, Wijmenga C, Lambrechts D, Aerssens J, Vlietinck R, Beunen G, Thomis MA., Free PMC Article

    01/14/2012
    The counteracting Nek2A and PP1gamma activities on the centrosome linker are controlled by Plk1.

    Plk1 controls the Nek2A-PP1γ antagonism in centrosome disjunction.
    Mardin BR, Agircan FG, Lange C, Schiebel E.

    12/24/2011
    The ataxia telangiectasia, mutated and Rad3-related-Chk1 axis regulates H3-pThr 11 dephosphorylation on DNA damage, at least in part by the activation of PP1gamma through Chk1-dependent inhibition of cyclin dependent kinases.

    Protein phosphatase 1γ is responsible for dephosphorylation of histone H3 at Thr 11 after DNA damage.
    Shimada M, Haruta M, Niida H, Sawamoto K, Nakanishi M., Free PMC Article

    02/5/2011
    firstprevious page of 2 nextlast