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MBC in Press, published online ahead of print January 25, 2006
Mol. Biol. Cell 10.1091/mbc.E05-07-0650

A more recent version of this article appeared on April 1, 2006
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Submitted on July 19, 2005
Revised on January 6, 2006
Accepted on January 12, 2006

ZO-1 Function in the Assembly of Tight Junctions in MDCK Epithelial Cells

Elizabeth McNeil, Christopher Capaldo, and Ian G. Macara

Center for Cell Signaling, Department of Microbiology, University of Virginia School of Medicine, Charlottesville VA 22908-0577

Monitoring Editor: Asma Nusrat

Zonula occludens-1 (ZO-1) was the first tight junction protein to be cloned, and has been implicated as an important scaffold protein. It contains multiple domains that bind a diverse set of junction proteins. However, the molecular functions of ZO-1 and related proteins such as ZO-2 and ZO-3 have remained unclear. We now show that gene silencing of ZO-1 causes a delay of ~3 h in tight junction formation in MDCK epithelial cells, but mature junctions appear functionally normal even in the continuing absence of ZO-1. Depletion of ZO-2, cingulin, or occludin, proteins that can interact with ZO-1, had no discernable effects on tight junctions. Rescue of junction assembly using murine ZO-1 mutants demonstrated that the ZO-1 C-terminus is neither necessary nor sufficient for normal assembly. Moreover, mutation of the PDZ1 domain did not block rescue. However, point mutations in the SH3 domain almost completely prevented rescue. Surprisingly, the isolated SH3 domain of ZO-1 could also rescue junction assembly. These data reveal an unexpected function for the SH3 domain of ZO-1 in regulating tight junction assembly in epithelial cells, and show that cingulin, occludin, or ZO-2 are not limiting for junction assembly in MDCK monolayers.

Address correspondence to: Ian G. Macara (igm9c{at}virginia.edu)




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