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First published online December 5, 2007

Journal of Cell Science 120, 2402e (2007)
© The Company of Biologists Limited
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In this issue

Munc18-1 sets a SNARE


Figure 1

SNARE proteins control the fusion of vesicles with target membranes. During exocytosis, fusion occurs when the vesicular SNARE synaptobrevin forms a ternary complex with the plasma membrane SNAREs syntaxin and SNAP25. The sites of SNARE-complex formation must be closely regulated to avoid inappropriate membrane fusion. Although several accessory proteins that modulate membrane trafficking are known, many questions about how they confer specificity remain. On page 4407, Rory Duncan and colleagues investigate the role of one such protein: munc18-1. The authors show that, in neuroendocrine cells, munc18-1 binds to syntaxin and promotes its trafficking to the plasma membrane. Using fluorescence lifetime imaging microscopy (FLIM), they go on to demonstrate that syntaxin and SNAP25 readily interact at the Golgi complex in the absence of munc18-1, forming stable SNARE complexes that trap the proteins and prevent their trafficking to the plasma membrane. Munc18-1 blocks the syntaxin-SNAP25 interaction. These findings indicate that a major role of munc18-1 is to avoid formation of a complex of SNAP25 and syntaxin before either protein reaches the plasma membrane.


Related articles in JCS:

Munc18-1 prevents the formation of ectopic SNARE complexes in living cells
Claire N. Medine, Colin Rickman, Luke H. Chamberlain, and Rory R. Duncan
JCS 2007 120: 4407-4415. [Abstract] [Full Text]  




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