Literature DB >> 20850437

TAZ interacts with zonula occludens-1 and -2 proteins in a PDZ-1 dependent manner.

Eline Remue1, Kris Meerschaert, Tsutomu Oka, Ciska Boucherie, Joël Vandekerckhove, Marius Sudol, Jan Gettemans.   

Abstract

The transcriptional coactivator TAZ recognizes L/PPxY motifs in transcription factors like Runx1/2 through its WW domain. We show that the first PDZ domain of zona occludens-1 (ZO-1) and 2 (ZO-2) interacts with the carboxy-terminal PDZ binding motif of TAZ. Deletion of this motif abrogates binding. ZO-2 colocalizes with TAZ in the nucleus of MDCK cells and ZO-2 expression alters TAZ localization in human embryonic kidney cells. Luciferase assays demonstrate ZO-2 inhibition of TAZ-mediated transactivation. We propose that zonula occludens is a negative regulator of TAZ and suggest that selected tight junction proteins control nuclear translocation and activity of TAZ.
Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Year:  2010        PMID: 20850437     DOI: 10.1016/j.febslet.2010.09.020

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  38 in total

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