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

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. Structured summary: MINT-7994937: ZO-2 (uniprotkb:Q95168) binds (MI:0407) to TAZ (uniprotkb:Q9EPK5) by pull down (MI: 0096) MINT-7994900, MINT-7994835, MINT-7994885: ZO-1 (uniprotkb:Q07157) physically interacts (MI: 0915) with TAZ (uniprotkb: Q9EPK5) by pull down (MI: 0096) MINT-7995020: ZO-2 (uniprotkb:Q9UDY2) and TAZ (uniprotkb:Q9GZV5) colocalize (MI: 0403) by fluorescence microscopy (MI: 0416) MINT-7994953: ZO-1 (uniprotkb: Q07157) binds (MI: 0407) to TAZ (uniprotkb: Q9EPK5) by pull down (MI: 0096) MINT-7994970: TAZ (uniprotkb: 73990382) and ZO-2 (uniprotkb: Q95168) colocalize (MI: 0403) by fluorescence microscopy (MI: 0416) MINT-7994867: TAZ (uniprotkb: Q9EPK5) physically interacts (MI: 0915) with ZO-2 (uniprotkb: Q9UDY2) by pull down (MI: 0096) MINT-7994988: TAZ (uniprotkb: Q9GZV5) and ZO-1 (uniprotkb: Q07157) colocalize (MI: 0403) by fluorescence microscopy (MI: 0416) MINT-7994999: TAZ (uniprotkb: Q9EPK5) and ZO-2 (uniprotkb: Q95168) colocalize (MI: 0403) by fluorescence microscopy (MI: 0416) MINT-7994922, MINT-7994853: ZO-2 (uniprotkb: Q95168) physically interacts (MI: 0915) with TAZ (uniprotkb: Q9EPK5) by pull down (MI: 0096) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.