Transglutaminase 2 and nucleoside diphosphate kinase activity are correlated in epithelial membranes and are abnormal in cystic fibrosis

Kate J. Treharne, O. Giles Best, Anil Mehta

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    8 Citations (Scopus)

    Abstract

    Tissue transglutaminase (tgase2) is a multifunctional enzyme that crosslinks proteins but also acts as a G-protein, differential functions regulated by calcium and GTP. In the epithelial cell membrane, we show that manipulation of tgase2 function by monodansylcadaverine or retinoic acid ( RA) alters the activity of a membrane-bound protein kinase, nucleoside diphosphate kinase (NDPK, nm23-H1/H2) that is known to control G-protein function. We find that NDPK function is abnormally low in cystic fibrosis but can be restored by RA treatment in vitro. Our data suggest that tgase2 is overexpressed in cystic fibrosis and affects NDPK function.

    Structured summary: MINT-7219905, MINT-7219896: tgase2 (uniprotkb: P21980) physically interacts (MI: 0914) with NDPK ( uniprotkb: P15531) by anti bait coimmunoprecipitation ( MI: 0006) (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

    Original languageEnglish
    Pages (from-to)2789-2792
    Number of pages4
    JournalFEBS Letters
    Volume583
    Issue number17
    DOIs
    Publication statusPublished - 3 Sep 2009

    Keywords

    • Fibrosing colonopathy
    • phosphohistidine
    • Cross-linking
    • Cystic fibrosis transmembrane regulator
    • HETEROTRIMERIC G-PROTEINS
    • RETINOIC ACID INDUCTION
    • TISSUE TRANSGLUTAMINASE
    • AIRWAY EPITHELIUM
    • HISTIDINE PHOSPHORYLATION
    • BINDING PROTEIN
    • SWEAT-DUCT
    • CELLS
    • ACTIVATION
    • CFTR

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