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

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

Research output: Contribution to journalArticlepeer-review

71 Scopus citations


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.

Original languageEnglish
Pages (from-to)4175-4180
Number of pages6
JournalFEBS Letters
Issue number19
StatePublished - Oct 2010


  • Postsynaptic density95-discs large-zonula occludens
  • Tight junction
  • Transcriptional coactivator with PDZ binding motif
  • Zonula occluden


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