Nature Structural & Molecular Biology 13, 577 - 581 (2006)
Published online: 6 July 2006; | doi:10.1038/nsmb1097
The exocyst defrocked, a framework of rods revealedMary Munson1
& Peter Novick21
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, Massachusetts 01605, USA. 2
Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut 06510, USA.
Correspondence should be addressed to Mary Munson mary.munson@umassmed.edu or Peter Novick peter.novick@yale.edu The exocyst complex is required for the interaction of vesicles with the plasma membrane in preparation for exocytic fusion. Recent crystallographic studies indicate that at least four of the eight subunits contain long, rod-like domains formed from helical bundles. These rods may pack against one another to generate the framework of the complex. How this complex assembles, how it responds to various GTPases and how it is ultimately displaced to allow bilayer fusion are key questions for the future.
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