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    PTPRM protein tyrosine phosphatase receptor type M [ Homo sapiens (human) ]

    Gene ID: 5797, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    A quantitative trait GWAS on lens thickness identifies novel risk loci on PTPRM in the narrow angle individuals susceptible to PACG.

    A quantitative trait GWAS on lens thickness identifies novel risk loci on PTPRM in the narrow angle individuals susceptible to PACG.
    Chakraborty S, Sharma A, Pal S, Sharma A, Sihota R, Bhattacharjee S, Acharya M.

    08/31/2023
    Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains.

    Determinants of receptor tyrosine phosphatase homophilic adhesion: Structural comparison of PTPRK and PTPRM extracellular domains.
    Hay IM, Shamin M, Caroe ER, Mohammed ASA, Svergun DI, Jeffries CM, Graham SC, Sharpe HJ, Deane JE., Free PMC Article

    02/4/2023
    PTPRM methylation induced by FN1 promotes the development of glioblastoma by activating STAT3 signalling.

    PTPRM methylation induced by FN1 promotes the development of glioblastoma by activating STAT3 signalling.
    Song J, Zhao D, Sun G, Yang J, Lv Z, Jiao B., Free PMC Article

    12/11/2021
    High expression of PTPRM predicts poor prognosis and promotes tumor growth and lymph node metastasis in cervical cancer.

    High expression of PTPRM predicts poor prognosis and promotes tumor growth and lymph node metastasis in cervical cancer.
    Liu P, Zhang C, Liao Y, Liu J, Huang J, Xia M, Chen M, Tan H, He W, Xu M, Liu T, Ooi S, Du Q, Qin S, Zhu Y, Zou Q, Wang W, Yao S., Free PMC Article

    04/24/2021
    PSMD11, PTPRM and PTPRB as novel biomarkers of pancreatic cancer progression.

    PSMD11, PTPRM and PTPRB as novel biomarkers of pancreatic cancer progression.
    Sahni S, Krisp C, Molloy MP, Nahm C, Maloney S, Gillson J, Gill AJ, Samra J, Mittal A.

    01/9/2021
    Results suggest increased post-translational modification of RPTPmu N-glycans by GnT-V attenuates its tyrosine phosphatase activity and promotes glioma cell migration through PLCgamma-PKC pathways.

    β1,6 GlcNAc branches-modified protein tyrosine phosphatase Mu attenuates its tyrosine phosphatase activity and promotes glioma cell migration through PLCγ-PKC pathways.
    Gao Y, Yang F, Su Z, He Z, Xiao J, Xu Y, Zha X, Xu F, Wang L.

    05/11/2019
    Study determined that, in addition to the furin-processed form of PTPmicro, a pool of 200 kDa full-length PTPmicro exists at the plasma membrane that is cleaved directly by ADAM to generate a larger shed form of the PTPmicro extracellular segment.

    A protease storm cleaves a cell-cell adhesion molecule in cancer: multiple proteases converge to regulate PTPmu in glioma cells.
    Phillips-Mason PJ, Craig SE, Brady-Kalnay SM., Free PMC Article

    10/17/2015
    Decreased expression of PTPRM in breast cancer is correlated with poor prognosis and inversely correlated with disease-free survival.

    Protein tyrosine phosphatase µ (PTP µ or PTPRM), a negative regulator of proliferation and invasion of breast cancer cells, is associated with disease prognosis.
    Sun PH, Ye L, Mason MD, Jiang WG., Free PMC Article

    05/18/2013
    Loss of PTPmu by proteolysis causes glioblastoma.

    Protein tyrosine phosphatase mu regulates glioblastoma cell growth and survival in vivo.
    Kaur H, Burden-Gulley SM, Phillips-Mason PJ, Basilion JP, Sloan AE, Brady-Kalnay SM., Free PMC Article

    09/1/2012
    Results suggest that miR-221 and -222 regulate glioma tumorigenesis at least in part through the control of PTPmu protein expression.

    miR-221/222 overexpession in human glioblastoma increases invasiveness by targeting the protein phosphate PTPμ.
    Quintavalle C, Garofalo M, Zanca C, Romano G, Iaboni M, del Basso De Caro M, Martinez-Montero JC, Incoronato M, Nuovo G, Croce CM, Condorelli G., Free PMC Article

    05/5/2012
    In A549 cells, diverse injurious stimuli dramatically reduced PTPmu protein expression.

    Diverse injurious stimuli reduce protein tyrosine phosphatase-μ expression and enhance epidermal growth factor receptor signaling in human airway epithelia.
    Hyun SW, Anglin IE, Liu A, Yang S, Sorkin JD, Lillehoj E, Tonks NK, Passaniti A, Goldblum SE., Free PMC Article

    11/26/2011
    Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator)

    Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
    Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article

    09/15/2010
    Observational study of gene-disease association. (HuGE Navigator)

    Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
    Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD, ASCOT investigators, NORDIL investigators, BRIGHT Consortium., Free PMC Article

    09/15/2010
    Clinical trial of gene-disease association and gene-environment interaction. (HuGE Navigator)

    Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score.
    Rose JE, Behm FM, Drgon T, Johnson C, Uhl GR., Free PMC Article

    06/30/2010
    Observational study and genome-wide association study of gene-disease association. (HuGE Navigator)See all PubMed (2) articles04/7/2010
    Loss of protein tyrosine phosphatase receptor type mu is associated with glioma cell migration and progression.

    PTPmu suppresses glioma cell migration and dispersal.
    Burgoyne AM, Palomo JM, Phillips-Mason PJ, Burden-Gulley SM, Major DL, Zaremba A, Robinson S, Sloan AE, Vogelbaum MA, Miller RH, Brady-Kalnay SM., Free PMC Article

    03/1/2010
    loss of cell surface PTPmu by proteolysis generates catalytically active PTPmu fragments that contribute to migration and survival of glioblastoma cells

    Proteolytic cleavage of protein tyrosine phosphatase mu regulates glioblastoma cell migration.
    Burgoyne AM, Phillips-Mason PJ, Burden-Gulley SM, Robinson S, Sloan AE, Miller RH, Brady-Kalnay SM., Free PMC Article

    01/21/2010
    BCCIP is phosphorylated by the Src tyrosine kinase and dephosphorylated by the PTPmu tyrosine phosphatase; neurite outgrowth assays suggest that BCCIP and PTPmu are in a common signal transduction pathway.

    BCCIP associates with the receptor protein tyrosine phosphatase PTPmu.
    Phillips-Mason PJ, Mourton T, Major DL, Brady-Kalnay SM., Free PMC Article

    01/21/2010
    a 3.1 angstrom crystal structure of the RPTPmu ectodomain that forms a homophilic trans (antiparallel) dimer with an extended and rigid architecture, matching the dimensions of adherens junctions is described

    Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-clamp mechanism.
    Aricescu AR, Siebold C, Choudhuri K, Chang VT, Lu W, Davis SJ, van der Merwe PA, Jones EY.

    01/21/2010
    interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs

    Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases.
    Blanchetot C, Tertoolen LG, Overvoorde J, den Hertog J.

    01/21/2010
    PTPmu may regulate Rho-GTPase-dependent functions of IQGAP1

    The receptor protein-tyrosine phosphatase PTPmu interacts with IQGAP1.
    Phillips-Mason PJ, Gates TJ, Major DL, Sacks DB, Brady-Kalnay SM.

    01/21/2010
    RPTPmu may play a role in the regulation of cardiovascular functions

    Receptor protein tyrosine phosphatase mu expression as a marker for endothelial cell heterogeneity; analysis of RPTPmu gene expression using LacZ knock-in mice.
    Koop EA, Lopes SM, Feiken E, Bluyssen HA, van der Valk M, Voest EE, Mummery CL, Moolenaar WH, Gebbink MF.

    01/21/2010
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