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

First Author  Remue E Year  2010
Journal  FEBS Lett Volume  584
Issue  19 Pages  4175-80
PubMed ID  20850437 Mgi Jnum  J:201302
Mgi Id  MGI:5512947 Doi  10.1016/j.febslet.2010.09.020
Citation  Remue E, et al. (2010) TAZ interacts with zonula occludens-1 and -2 proteins in a PDZ-1 dependent manner. FEBS Lett 584(19):4175-80
abstractText  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.
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