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Vesicle-tethering complexes

Fusion of a vesicle with its target membrane is driven by formation of a SNARE complex involving proteins from the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). But can interactions between different v-SNAREs and t-SNAREs account for the specificity of membrane fusion? And is the formation of a SNARE complex really the first stage? Recent work indicates that a `tethering' process precedes SNARE complex formation and that factors involved in tethering contribute to the specificity of membrane fusion. In a Commentary on p. 2627, James Whyte and Sean Munro discuss the roles of such tethering factors. These fall into two classes: long coiled-coil proteins such as p115 and the golgins; and a group of multisubunit complexes that comprises several unrelated complexes and a subgroup that Whyte and Munro term `quatrefoil' complexes. The tethering factors probably have distinct functions. For example, the coiled-coil proteins could act as kinetic tethers that locate and passively hold vesicles, whereas the quatrefoil complexes are more likely to play a direct role, such as promoting the formation of SNARE complexes.

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Related articles in JCS:

Vesicle tethering complexes in membrane traffic

James R. C. Whyte and Sean Munro
JCS 2002 115: 2627-2637. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?