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FEBS Lett. 2010 Oct 8;584(19):4175-80. doi: 10.1016/j.febslet.2010.09.020. Epub 2010 Sep 18.

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

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Department of Medical Protein Research, VIB, Gent, Belgium.


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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