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Vol. 20, Issue 1, 153-163, January 1, 2009

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An Internal Domain of Exo70p Is Required for Actin-independent Localization and Mediates Assembly of Specific Exocyst Components

Alex H. Hutagalung^*, Jeff Coleman, Marc Pypaert^,, and Peter J. Novick^*

*Department of Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA 92093; and Department of Cell Biology, Yale University, New Haven, CT 06510

Submitted February 15, 2008; Revised October 9, 2008; Accepted October 14, 2008
Monitoring Editor: Jeffrey L. Brodsky

The exocyst consists of eight rod-shaped subunits that align in a side-by-side manner to tether secretory vesicles to the plasma membrane in preparation for fusion. Two subunits, Sec3p and Exo70p, localize to exocytic sites by an actin-independent pathway, whereas the other six ride on vesicles along actin cables. Here, we demonstrate that three of the four domains of Exo70p are essential for growth. The remaining domain, domain C, is not essential but when deleted, it leads to synthetic lethality with many secretory mutations, defects in exocyst assembly of exocyst components Sec5p and Sec6p, and loss of actin-independent localization. This is analogous to a deletion of the amino-terminal domain of Sec3p, which prevents an interaction with Cdc42p or Rho1p and blocks its actin-independent localization. The two mutations are synthetically lethal, even in the presence of high copy number suppressors that can bypass complete deletions of either single gene. Although domain C binds Rho3p, loss of the Exo70p-Rho3p interaction does not account for the synthetic lethal interactions or the exocyst assembly defects. The results suggest that either Exo70p or Sec3p must associate with the plasma membrane for the exocyst to function as a vesicle tether.

Deceased.

Address correspondence to: Peter J. Novick (pnovick{at}ucsd.edu)

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