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The exocyst defrocked, a framework of rods revealed

Nature Structural & Molecular Biology volume 13, pages 577–581 (2006)Cite this article

Abstract

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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Figure 1: The function of the exocyst is localized to sites of active secretion in eukaryotic cells.
Figure 2: Exocyst subunit structures.
Figure 3: A model for the assembled exocyst complex.

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Acknowledgements

We thank K. Reinisch and W. Kobertz for critical reading of this manuscript. This work was supported by grants from the US National Institutes of Heath to P.N. (GM35370 and CA46128) and M.M. (GM068803).

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  1. Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, 01605, Massachusetts, USA

    Mary Munson

  2. Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, 06510, Connecticut, USA

    Peter Novick

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Correspondence to Mary Munson or Peter Novick.

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Munson, M., Novick, P. The exocyst defrocked, a framework of rods revealed. Nat Struct Mol Biol 13, 577–581 (2006). https://doi.org/10.1038/nsmb1097

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