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    PTPN4 protein tyrosine phosphatase non-receptor type 4 [ Homo sapiens (human) ]

    Gene ID: 5775, updated on 14-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    LncRNA SH3BP5-AS1 promotes hepatocellular carcinoma progression by sponging miR-6838-5p and activation of PTPN4.

    LncRNA SH3BP5-AS1 promotes hepatocellular carcinoma progression by sponging miR-6838-5p and activation of PTPN4.
    Zhao X, Zhu X, Xiao C, Hu Z., Free PMC Article

    10/11/2024
    circRNA-PTPN4 mediated regulation of FOXO3 and ZO-1 expression: implications for blood-brain barrier integrity and cognitive function in uremic encephalopathy.

    circRNA-PTPN4 mediated regulation of FOXO3 and ZO-1 expression: implications for blood-brain barrier integrity and cognitive function in uremic encephalopathy.
    Liu Y, Qin Y, Zhang Y., Free PMC Article

    05/1/2024
    E3 Ubiquitin Ligase MARCH8 Promotes Pancreatic Cancer Growth and Metastasis by Activating STAT3 via Degradation of PTPN4.

    E3 Ubiquitin Ligase MARCH8 Promotes Pancreatic Cancer Growth and Metastasis by Activating STAT3 via Degradation of PTPN4.
    Chen C, Wang Y, Zhao Q, Li GD, Wang YH, Xu LC, Huang HZ, Song G, Li WT, He XH.

    12/20/2023
    MicroRNA-375 is a therapeutic target for castration-resistant prostate cancer through the PTPN4/STAT3 axis.

    MicroRNA-375 is a therapeutic target for castration-resistant prostate cancer through the PTPN4/STAT3 axis.
    Gan J, Liu S, Zhang Y, He L, Bai L, Liao R, Zhao J, Guo M, Jiang W, Li J, Li Q, Mu G, Wu Y, Wang X, Zhang X, Zhou D, Lv H, Wang Z, Zhang Y, Qian C, Feng M, Chen H, Meng Q, Huang X., Free PMC Article

    09/17/2022
    Structural and biochemical analysis of the PTPN4 PDZ domain bound to the C-terminal tail of the human papillomavirus E6 oncoprotein.

    Structural and biochemical analysis of the PTPN4 PDZ domain bound to the C-terminal tail of the human papillomavirus E6 oncoprotein.
    Lee HS, Yun HY, Lee EW, Shin HC, Kim SJ, Ku B.

    04/9/2022
    Study identified a nonsense mutation of PTPN4 with mutation ratio of 90.90% from 1 case of rectal cancer. Overexpression of PTPN4 suppressed the growth of colorectal cancer cells. PTPN4 dephosphorylates pSTAT3 at the Tyr705 residue with a direct interaction and depresses the transcriptional activity of STAT3.

    Loss of PTPN4 activates STAT3 to promote the tumor growth in rectal cancer.
    Zhang BD, Li YR, Ding LD, Wang YY, Liu HY, Jia BQ., Free PMC Article

    07/20/2019
    Data show that mutations affect the regulation of the protein tyrosine phosphatase non-receptor type 4 (PTPN4) bidomain and indicate that the PDZ-PDZ ligand regulation of PTPN4 is a linker-mediated mechanism.

    Regulation of the Human Phosphatase PTPN4 by the inter-domain linker connecting the PDZ and the phosphatase domains.
    Caillet-Saguy C, Toto A, Guerois R, Maisonneuve P, di Silvio E, Sawyer K, Gianni S, Wolff N., Free PMC Article

    03/16/2019
    Binding assays confirmed that three (Cyto8-mtxd-1, Cyto8-mtxk-4 and Cyto8-mtxd-1k-4) out of the five designed peptides exhibit moderately or considerably increased affinity as compared to the native peptide Cyto8-RETEV

    Structure-based optimization of salt-bridge network across the complex interface of PTPN4 PDZ domain with its peptide ligands in neuroglioma.
    Xiao X, He QH, Yu LY, Wang SQ, Li Y, Yang H, Zhang AH, Ma XH, Peng YJ, Chen B.

    11/11/2017
    the p38gamma.PTPN4 interaction promotes cellular signaling, preventing cell death induction.

    Molecular Basis of the Interaction of the Human Protein Tyrosine Phosphatase Non-receptor Type 4 (PTPN4) with the Mitogen-activated Protein Kinase p38γ.
    Maisonneuve P, Caillet-Saguy C, Vaney MC, Bibi-Zainab E, Sawyer K, Raynal B, Haouz A, Delepierre M, Lafon M, Cordier F, Wolff N., Free PMC Article

    05/7/2017
    Deletion of PTPN4 has been reported in monozygotic twins with a Rett syndrome-like phenotype.

    Deletion of protein tyrosine phosphatase, non-receptor type 4 (PTPN4) in twins with a Rett syndrome-like phenotype.
    Williamson SL, Ellaway CJ, Peters GB, Pelka GJ, Tam PP, Christodoulou J., Free PMC Article

    05/28/2016
    The physiologically active PTPN4 two-domain (the PDZ and the phosphatase domains) adopts a predominant compact conformation in solution. PDZ ligand binding restores the catalytic competence of PTPN4 disrupting the transient interdomain communication.

    Regulation of the catalytic activity of the human phosphatase PTPN4 by its PDZ domain.
    Maisonneuve P, Caillet-Saguy C, Raynal B, Gilquin B, Chaffotte A, Pérez J, Zinn-Justin S, Delepierre M, Buc H, Cordier F, Wolff N.

    01/10/2015
    These findings suggest that PTPN4 negatively regulates cell proliferation and motility through dephosphorylation of CrkI.

    PTPN4 negatively regulates CrkI in human cell lines.
    Zhou J, Wan B, Shan J, Shi H, Li Y, Huo K., Free PMC Article

    03/8/2014
    PTPN4 is dispensable for T cell development and/or T cell effector functions.

    The protein tyrosine phosphatase PTPN4/PTP-MEG1, an enzyme capable of dephosphorylating the TCR ITAMs and regulating NF-kappaB, is dispensable for T cell development and/or T cell effector functions.
    Young JA, Becker AM, Medeiros JJ, Shapiro VS, Wang A, Farrar JD, Quill TA, Hooft van Huijsduijnen R, van Oers NS., Free PMC Article

    01/21/2010
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