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MBC in Press, published online ahead of print December 10, 2008
Mol. Biol. Cell 10.1091/mbc.E08-09-0968

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Submitted on September 23, 2008
Revised on November 25, 2008
Accepted on December 1, 2008

Sec6p Anchors the Assembled Exocyst Complex at Sites of Secretion

Jennifer A. Songer and Mary Munson

Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605

Monitoring Editor: Patrick J. Brennwald

The exocyst is an essential protein complex required for targeting and fusion of secretory vesicles to sites of exocytosis at the plasma membrane. To study the function of the exocyst complex, we performed a structure-based mutational analysis of the S. cerevisiae exocyst subunit Sec6p. Two "patches" of highly conserved residues are present on the surface of Sec6p; mutation of either patch does not compromise protein stability. Nevertheless, replacement of SEC6 with the patch mutants results in severe temperature-sensitive growth and secretion defects. At nonpermissive conditions, although trafficking of secretory vesicles to the plasma membrane is unimpaired, none of the exocyst subunits are polarized. This is consistent with data from other exocyst temperature-sensitive mutants, which disrupt the integrity of the complex. Surprisingly, however, these patch mutations result in mislocalized exocyst complexes that remain intact. Our results indicate that assembly and polarization of the exocyst are functionally separable events, and that Sec6p is required to anchor exocyst complexes at sites of secretion.

Address correspondence to: Mary Munson (mary.munson{at}umassmed.edu)




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N. J. Andersen and C. Yeaman
Sec3-containing Exocyst Complex Is Required for Desmosome Assembly in Mammalian Epithelial Cells
Mol. Biol. Cell, January 1, 2010; 21(1): 152 - 164.
[Abstract] [Full Text] [PDF]


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