The exocyst defrocked, a framework of rods revealed
Open Access
- 6 July 2006
- journal article
- review article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 13 (7) , 577-581
- https://doi.org/10.1038/nsmb1097
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.Keywords
This publication has 50 references indexed in Scilit:
- The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse rolesNature Structural & Molecular Biology, 2006
- Crystal Structure of the S.cerevisiae Exocyst Component Exo70pJournal of Molecular Biology, 2005
- The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motifNature Structural & Molecular Biology, 2005
- Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivoNature Structural & Molecular Biology, 2005
- BI-DIRECTIONAL PROTEIN TRANSPORT BETWEEN THE ER AND GOLGIAnnual Review of Cell and Developmental Biology, 2004
- Protein complexes in transport vesicle targetingTrends in Cell Biology, 2000
- Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolutionNature, 1998
- Subunit structure of the mammalian exocyst complexProceedings of the National Academy of Sciences, 1997
- Sec2p Mediates Nucleotide Exchange on Sec4p and Is Involved in Polarized Delivery of Post-Golgi VesiclesThe Journal of cell biology, 1997
- SNAP receptors implicated in vesicle targeting and fusionNature, 1993