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    PTPN23 protein tyrosine phosphatase non-receptor type 23 [ Homo sapiens (human) ]

    Gene ID: 25930, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    PTPN23[Thr] variant reduces susceptibility and tumorigenesis in esophageal squamous cell carcinoma through dephosphorylation of EGFR.

    PTPN23[Thr] variant reduces susceptibility and tumorigenesis in esophageal squamous cell carcinoma through dephosphorylation of EGFR.
    Niu S, Ma J, Li Y, Yue X, Shi K, Pan M, Song L, Tan Y, Gu L, Liu S, Chang J.

    06/8/2024
    PTPN23 ubiquitination by WDR4 suppresses EGFR and c-MET degradation to define a lung cancer therapeutic target.

    PTPN23 ubiquitination by WDR4 suppresses EGFR and c-MET degradation to define a lung cancer therapeutic target.
    Singh S, Yeat NY, Wang YT, Lin SY, Kuo IY, Wu KP, Wang WJ, Wang WC, Su WC, Wang YC, Chen RH., Free PMC Article

    11/2/2023
    Interactions of ubiquitin and CHMP5 with the V domain of HD-PTP reveals role for regulation of Vps4 ATPase.

    Interactions of ubiquitin and CHMP5 with the V domain of HD-PTP reveals role for regulation of Vps4 ATPase.
    Pashkova N, Yu L, Schnicker NJ, Tseng CC, Gakhar L, Katzmann DJ, Piper RC., Free PMC Article

    03/26/2022
    Phenotype and mutation expansion of the PTPN23 associated disorder characterized by neurodevelopmental delay and structural brain abnormalities.

    Phenotype and mutation expansion of the PTPN23 associated disorder characterized by neurodevelopmental delay and structural brain abnormalities.
    Bend R, Cohen L, Carter MT, Lyons MJ, Niyazov D, Mikati MA, Rojas SK, Person RE, Si Y, Wentzensen IM, Regeneron Genetics Center, Torti E, Lee JA, Boycott KM, Basel-Salmon L, Ferreira CR, Gonzaga-Jauregui C., Free PMC Article

    02/6/2021
    Our report provides the first description of the clinical phenotype of recessive PTPN23 variants with pathogenicity substantiated by a functional study

    Developmental epileptic encephalopathy with hypomyelination and brain atrophy associated with PTPN23 variants affecting the assembly of UsnRNPs.
    Smigiel R, Landsberg G, Schilling M, Rydzanicz M, Pollak A, Walczak A, Stodolak A, Stawinski P, Mierzewska H, Sasiadek MM, Gruss OJ, Ploski R., Free PMC Article

    03/9/2019
    Mutations in PTPN23 gene is associated with developmental and epileptic encephalopathy.

    Mutations of PTPN23 in developmental and epileptic encephalopathy.
    Sowada N, Hashem MO, Yilmaz R, Hamad M, Kakar N, Thiele H, Arold ST, Bode H, Alkuraya FS, Borck G.

    12/9/2017
    HD-PTP/PTPN23 as a prominent haploinsufficient tumor suppressor gene preventing tumor progression through control of integrin trafficking.

    Haploinsufficiency of the ESCRT Component HD-PTP Predisposes to Cancer.
    Manteghi S, Gingras MC, Kharitidi D, Galarneau L, Marques M, Yan M, Cencic R, Robert F, Paquet M, Witcher M, Pelletier J, Pause A.

    11/26/2017
    the underlying mechanism of PTPN23 function in breast tumorigenesis as that of a key phosphatase that normally suppresses the activity of FYN

    Suppression of protein tyrosine phosphatase N23 predisposes to breast tumorigenesis via activation of FYN kinase.
    Zhang S, Fan G, Hao Y, Hammell M, Wilkinson JE, Tonks NK., Free PMC Article

    11/25/2017
    The role of HD-PTP/PTPN23 in cancer and tumorigenesis is reviewed.

    Role of ESCRT component HD-PTP/PTPN23 in cancer.
    Gingras MC, Kazan JM, Pause A.

    08/12/2017
    Results present crystal structures of the coiled-coil domain of the HD-PTP phosphatase and its complex with UBAP1. The coiled-coil domain adopts an unexpected open and rigid conformation. The HD-PTP:UBAP1 structure identifies the molecular determinants of the interaction and provides a molecular basis for the specific functional cooperation between HD-PTP and UBAP1.

    Structural Basis for Selective Interaction between the ESCRT Regulator HD-PTP and UBAP1.
    Gahloth D, Levy C, Heaven G, Stefani F, Wunderley L, Mould P, Cliff MJ, Bella J, Fielding AJ, Woodman P, Tabernero L., Free PMC Article

    07/1/2017
    HD-PTP acts as an alternative to ESCRT-II and VPS20/CHMP6 as a link between the ESCRT-I and those ESCRT-III protein(s) necessary for ILV formation.

    A non-canonical ESCRT pathway, including histidine domain phosphotyrosine phosphatase (HD-PTP), is used for down-regulation of virally ubiquitinated MHC class I.
    Parkinson MD, Piper SC, Bright NA, Evans JL, Boname JM, Bowers K, Lehner PJ, Luzio JP., Free PMC Article

    12/19/2015
    Data indicate a regulatory function of non-receptor-type tyrosine phosphatase PTPN23 in maintaining a highly phosphorylated state of survival motor neuron complex protein SMN.

    The catalytically inactive tyrosine phosphatase HD-PTP/PTPN23 is a novel regulator of SMN complex localization.
    Husedzinovic A, Neumann B, Reymann J, Draeger-Meurer S, Chari A, Erfle H, Fischer U, Gruss OJ., Free PMC Article

    10/3/2015
    PTPN23 is a tumor suppressor and that repression of PTPN23 expression by miR-142-3p plays an important role in the pathogenesis of testicular germ cell tumors.

    Tumor-suppressive function of protein-tyrosine phosphatase non-receptor type 23 in testicular germ cell tumors is lost upon overexpression of miR142-3p microRNA.
    Tanaka K, Kondo K, Kitajima K, Muraoka M, Nozawa A, Hara T., Free PMC Article

    11/30/2013
    The ESCRT accessory protein HD-PTP/PTPN23 associates with epidermal growth factor receptor (EGFR) and combines with the deubiquitinating enzyme UBPY/USP8 to transfer EGFR from ESCRT-0 to ESCRT-III and drive EGFR sorting to intralumenal vesicles.

    Recruitment of UBPY and ESCRT exchange drive HD-PTP-dependent sorting of EGFR to the MVB.
    Ali N, Zhang L, Taylor S, Mironov A, Urbé S, Woodman P.

    09/21/2013
    our findings suggest an evolutionarily conserved function of HDPTP-Rab4 in the regulation of endocytic trafficking, cell adhesion and migration

    The Bro1-domain-containing protein Myopic/HDPTP coordinates with Rab4 to regulate cell adhesion and migration.
    Chen DY, Li MY, Wu SY, Lin YL, Tsai SP, Lai PL, Lin YT, Kuo JC, Meng TC, Chen GC.

    06/1/2013
    HD-PTP degradation by calpains might result in the acquisition of a more aggressive phenotype in neoplastic cells.

    The tyrosine phosphatase HD-PTP (PTPN23) is degraded by calpains in a calcium-dependent manner.
    Castiglioni S, Maier JA.

    07/14/2012
    loss of PTPN23 may increase the activity of SRC and the phosphorylation status of the E-cadherin/beta-catenin signaling complex to promote tumor growth and invasive behavior in breast cancer

    Identification of PTPN23 as a novel regulator of cell invasion in mammary epithelial cells from a loss-of-function screen of the 'PTP-ome'.
    Lin G, Aranda V, Muthuswamy SK, Tonks NK., Free PMC Article

    08/27/2011
    Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL

    Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL.
    Tanase CA., Free PMC Article

    07/9/2011
    contributes to the regulation of endothelial migration; may play a role in angiogenesis

    HD-PTP inhibits endothelial migration through its interaction with Src.
    Mariotti M, Castiglioni S, Garcia-Manteiga JM, Beguinot L, Maier JA.

    01/21/2010
    demonstrate that HD-PTP is a catalytically inactive protein tyrosine phosphatase. As such, we identify one residue involved in its inactivation and show that colony growth reduction activity is independent of its PTP activity status in cancer cell lines

    HD-PTP is a catalytically inactive tyrosine phosphatase due to a conserved divergence in its phosphatase domain.
    Gingras MC, Zhang YL, Kharitidi D, Barr AJ, Knapp S, Tremblay ML, Pause A., Free PMC Article

    01/21/2010
    in Epidermal Growth Factor (EGF) stimulated cells, Src binds to and phosphorylates HD-PTP on tyrosine residues

    Inhibition of T24 human bladder carcinoma cell migration by RNA interference suppressing the expression of HD-PTP.
    Mariotti M, Castiglioni S, Maier JA.

    01/21/2010
    We suggest that HD-PTP contributes to the regulation of endothelial motility by modulating the tyrosine phosphorylation of FAK.

    The tyrosine phosphatase HD-PTP: A novel player in endothelial migration.
    Castiglioni S, Maier JA, Mariotti M.

    01/21/2010
    data suggest that HD-PTP might participate in modulating endothelial response to angiogenic factors and play a role in regulating the complex events leading to the formation of new vessels

    The tyrosine phosphatase HD-PTP is regulated by FGF-2 through proteasome degradation.
    Mariotti M, Castiglioni S, Beguinot L, Maier JA.

    01/21/2010
    These results suggest that HD-PTP amounts might be regulated both at the transcriptional and post-transcriptional levels.

    Expression analysis and modulation by HIV-Tat of the tyrosine phosphatase HD-PTP.
    Mariotti M, Castiglioni S, Maier JA.

    01/21/2010
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