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.
|Number of pages||4|
|Publication status||Published - 3 Sept 2009|
- Fibrosing colonopathy
- Cystic fibrosis transmembrane regulator
- HETEROTRIMERIC G-PROTEINS
- RETINOIC ACID INDUCTION
- TISSUE TRANSGLUTAMINASE
- AIRWAY EPITHELIUM
- HISTIDINE PHOSPHORYLATION
- BINDING PROTEIN