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    PTPRA protein tyrosine phosphatase receptor type A [ Homo sapiens (human) ]

    Gene ID: 5786, updated on 9-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Glucose-mediated N-glycosylation of RPTPalpha affects its subcellular localization and Src activation.

    Glucose-mediated N-glycosylation of RPTPα affects its subcellular localization and Src activation.
    Fang J, Zhang Y, Huang C, Lu R, Yu J, Chen R, Wang Y, Zhao X, Yu J, Huang J.

    04/7/2023
    Does a rare mutation in PTPRA contribute to the development of Parkinson's disease in an Australian multi-incident family?

    Does a rare mutation in PTPRA contribute to the development of Parkinson's disease in an Australian multi-incident family?
    Hill MA, Bentley SR, Walker TL, Mellick GD, Wood SA, Sykes AM., Free PMC Article

    08/6/2022
    CircPTPRA blocks the recognition of RNA N(6)-methyladenosine through interacting with IGF2BP1 to suppress bladder cancer progression.

    CircPTPRA blocks the recognition of RNA N(6)-methyladenosine through interacting with IGF2BP1 to suppress bladder cancer progression.
    Xie F, Huang C, Liu F, Zhang H, Xiao X, Sun J, Zhang X, Jiang G., Free PMC Article

    12/4/2021
    Receptor-type protein tyrosine phosphatase alpha (PTPalpha) mediates MMP14 localization and facilitates triple-negative breast cancer cell invasion.

    Receptor-type protein tyrosine phosphatase alpha (PTPα) mediates MMP14 localization and facilitates triple-negative breast cancer cell invasion.
    Decotret LR, Wadsworth BJ, Li LV, Lim CJ, Bennewith KL, Pallen CJ., Free PMC Article

    09/18/2021
    RPTPalpha phosphatase activity is allosterically regulated by the membrane-distal catalytic domain.

    RPTPα phosphatase activity is allosterically regulated by the membrane-distal catalytic domain.
    Wen Y, Yang S, Wakabayashi K, Svensson MND, Stanford SM, Santelli E, Bottini N., Free PMC Article

    12/19/2020
    Filtered data from WES, combined with in silico analyses revealed a novel heterozygous missense variant (NM_080841:c.1730C>G:p.T577R; exon18) in Protein tyrosine phosphatase, receptor type A (PTPRA 20p13) in an Indian family with schizophrenia. Screening for variants in this gene in the WES data of an independent schizophrenia cohort (n=350) of matched ethnicity, identified five additional rare missense variants.

    Rare variants in Protein tyrosine phosphatase, receptor type A (PTPRA) in schizophrenia: Evidence from a family based study.
    John J, Kukshal P, Sharma A, Bhatia T, Nimgaonkar VL, Deshpande SN, Thelma BK., Free PMC Article

    05/16/2020
    Leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) are cell adhesion molecules involved in mediating neuronal development. The binding of LAR-RPTPs to extracellular ligands induces local clustering of LAR-RPTPs to regulate axon growth and synaptogenesis. LAR-RPTPs interact with synaptic liprin-alpha proteins via the two cytoplasmic phosphatase domains, D1 and D2.

    Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity.
    Xie X, Luo L, Liang M, Zhang W, Zhang T, Yu C, Wei Z., Free PMC Article

    04/4/2020
    miR-146a-5p may negatively regulate the PTPRA-SRC signaling to inhibit expression of fibrosis-related markers in irradiated and TGF-beta1-stimulated LX2 cells

    MicroRNA-146a-5p Attenuates Fibrosis-related Molecules in Irradiated and TGF-beta1-Treated Human Hepatic Stellate Cells by Regulating PTPRA-SRC Signaling.
    Yuan BY, Chen YH, Wu ZF, Zhuang Y, Chen GW, Zhang L, Zhang HG, Cheng JC, Lin Q, Zeng ZC.

    02/15/2020
    HePTP plays a key role in the metastasis of triple-negative breast cancer via activating Wnt/beta-catenin signaling.

    HePTP promotes migration and invasion in triple-negative breast cancer cells via activation of Wnt/β-catenin signaling.
    Yu L, Wang C, Pan F, Liu Y, Ren X, Zeng H, Shi Y.

    02/8/2020
    circPTPRA suppresses EMT and metastasis of NSCLC cell lines by sponging miR-96-5p, which upregulates the downstream tumor suppressor RASSF8.

    The circRNA circPTPRA suppresses epithelial-mesenchymal transitioning and metastasis of NSCLC cells by sponging miR-96-5p.
    Wei S, Zheng Y, Jiang Y, Li X, Geng J, Shen Y, Li Q, Wang X, Zhao C, Chen Y, Qian Z, Zhou J, Li W., Free PMC Article

    12/21/2019
    Multivariate Cox regression analysis suggested that PTPRA expression was an independent prognostic factor in SCC patients. In the cellular models, PTPRA promotes SCC cell proliferation through modulating Src activation as well as cell cycle progression. In conclusion, higher PTPRA level was associated with worse prognosis of SCC patients and PTPRA could promote the cell cycle progression

    Increased PTPRA expression leads to poor prognosis through c-Src activation and G1 phase progression in squamous cell lung cancer.
    Gu Z, Fang X, Li C, Chen C, Liang G, Zheng X, Fan Q., Free PMC Article

    05/26/2018
    VacA mediates CagA phosphorylation through RPTPalpha in AZ-521 cells.

    Helicobacter pylori VacA, acting through receptor protein tyrosine phosphatase α, is crucial for CagA phosphorylation in human duodenum carcinoma cell line AZ-521.
    Nakano M, Yahiro K, Yamasaki E, Kurazono H, Akada J, Yamaoka Y, Niidome T, Hatakeyama M, Suzuki H, Yamamoto T, Moss J, Isomoto H, Hirayama T., Free PMC Article

    12/9/2017
    A receptor type-protein tyrosine phosphatase alpha-Src family kinase-Rap1 pathway was identified as responsible for recruiting myosin IIB to the zonula adherens in epithelial cells and supporting contractile tension.

    An RPTPα/Src family kinase/Rap1 signaling module recruits myosin IIB to support contractile tension at apical E-cadherin junctions.
    Gomez GA, McLachlan RW, Wu SK, Caldwell BJ, Moussa E, Verma S, Bastiani M, Priya R, Parton RG, Gaus K, Sap J, Yap AS., Free PMC Article

    04/23/2016
    no evidence was seen for the association of rare, missense mutations in the PTPRA gene with schizophrenia or autism spectrum disorders

    Resequencing and association analysis of PTPRA, a possible susceptibility gene for schizophrenia and autism spectrum disorders.
    Xing J, Wang C, Kimura H, Takasaki Y, Kunimoto S, Yoshimi A, Nakamura Y, Koide T, Banno M, Kushima I, Uno Y, Okada T, Aleksic B, Ikeda M, Iwata N, Ozaki N., Free PMC Article

    08/15/2015
    Data indicate that scaffold protein RACK1 plays a role in IGF-1-mediated protein-tyrosine phosphatase alpha (PTPalpha) tyrosine phosphorylation in MCF-7 Cells.

    The interaction of protein-tyrosine phosphatase α (PTPα) and RACK1 protein enables insulin-like growth factor 1 (IGF-1)-stimulated Abl-dependent and -independent tyrosine phosphorylation of PTPα.
    Khanna RS, Le HT, Wang J, Fung TC, Pallen CJ., Free PMC Article

    06/27/2015
    recruited to epithelial adherens junctions for cadherin-dependent cell adhesion and tissue architecture formation

    RPTPα controls epithelial adherens junctions, linking E-cadherin engagement to c-Src-mediated phosphorylation of cortactin.
    Truffi M, Dubreuil V, Liang X, Vacaresse N, Nigon F, Han SP, Yap AS, Gomez GA, Sap J.

    05/16/2015
    Results suggest that inhibition of PTPalpha can have a beneficial effect on HER2-positive breast cancers, but that inhibition of additional targets is needed to block breast tumorigenesis.

    Tyrosine phosphatase PTPα contributes to HER2-evoked breast tumor initiation and maintenance.
    Meyer DS, Aceto N, Sausgruber N, Brinkhaus H, Müller U, Pallen CJ, Bentires-Alj M.

    03/15/2014
    new role for PTPalpha in the regulation of motility of mammary epithelial cells in response to ErbB2 activation.

    Receptor protein-tyrosine phosphatase α regulates focal adhesion kinase phosphorylation and ErbB2 oncoprotein-mediated mammary epithelial cell motility.
    Boivin B, Chaudhary F, Dickinson BC, Haque A, Pero SC, Chang CJ, Tonks NK., Free PMC Article

    02/22/2014
    results suggest that PTPalpha links activation of epidermal growth factor receptor (EGFR) signaling with Src activation and may provide a novel therapeutic target for treatment of breast cancer.

    PTPα-mediated Src activation by EGF in human breast cancer cells.
    Wang J, Yu L, Zheng X.

    09/21/2013
    A single-nucleotide polymorphism (rs6138953) on the PTPRA gene in the 20p13 region was found to be associated with elevated fasting glucose level.

    Combined genome-wide linkage and association analyses of fasting glucose level in healthy twins and families of Korea.
    Suh YJ, Kim S, Kim SH, Park J, Lim HA, Park HJ, Choi H, Ng D, Lee MK, Nam M., Free PMC Article

    09/14/2013
    The extracellular proteolytic processing is a novel mechanism for PTPalpha regulation.

    Proteolytic processing of the protein tyrosine phosphatase α extracellular domain is mediated by ADAM17/TACE.
    Kapp K, Siemens J, Häring HU, Lammers R.

    06/15/2013
    our results suggest that plasma PTPalpha and fibronectin may be associated with opisthorchiasis.

    Proteomic identification of plasma protein tyrosine phosphatase alpha and fibronectin associated with liver fluke, Opisthorchis viverrini, infection.
    Khoontawad J, Laothong U, Roytrakul S, Pinlaor P, Mulvenna J, Wongkham C, Yongvanit P, Pairojkul C, Mairiang E, Sithithaworn P, Pinlaor S., Free PMC Article

    03/9/2013
    convergent evidence reported here links RPTP to schizophrenia.

    Loss of function studies in mice and genetic association link receptor protein tyrosine phosphatase α to schizophrenia.
    Takahashi N, Nielsen KS, Aleksic B, Petersen S, Ikeda M, Kushima I, Vacaresse N, Ujike H, Iwata N, Dubreuil V, Mirza N, Sakurai T, Ozaki N, Buxbaum JD, Sap J., Free PMC Article

    01/28/2012
    The transformed cells were tumourigenic in nude mice, suggesting that RPTPalpha245-induced activation of Src in the human tumours may have contributed to carcinogenesis.

    Activation of Src and transformation by an RPTPα splice mutant found in human tumours.
    Huang J, Yao L, Xu R, Wu H, Wang M, White BS, Shalloway D, Zheng X., Free PMC Article

    10/8/2011
    the PTPalpha-mediated increase of NB-3 level at the cell surface represents a novel function of PTPalpha in NB-3 signaling in neural development

    Receptor-like protein-tyrosine phosphatase α enhances cell surface expression of neural adhesion molecule NB-3.
    Ye H, Zhao T, Tan YL, Liu J, Pallen CJ, Xiao ZC., Free PMC Article

    09/17/2011
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