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Science 323 (5913): 474-477

Copyright © 2009 by the American Association for the Advancement of Science

Membrane Fusion: Grappling with SNARE and SM Proteins

Thomas C. Südhof1, and James E. Rothman2

Abstract: The two universally required components of the intracellular membrane fusion machinery, SNARE and SM (Sec1/Munc18-like) proteins, play complementary roles in fusion. Vesicular and target membrane–localized SNARE proteins zipper up into an {alpha}-helical bundle that pulls the two membranes tightly together to exert the force required for fusion. SM proteins, shaped like clasps, bind to trans-SNARE complexes to direct their fusogenic action. Individual fusion reactions are executed by distinct combinations of SNARE and SM proteins to ensure specificity, and are controlled by regulators that embed the SM-SNARE fusion machinery into a physiological context. This regulation is spectacularly apparent in the exquisite speed and precision of synaptic exocytosis, where synaptotagmin (the calcium-ion sensor for fusion) cooperates with complexin (the clamp activator) to control the precisely timed release of neurotransmitters that initiates synaptic transmission and underlies brain function.

1 Department of Cellular and Molecular Physiology, Stanford University, Palo Alto, CA 94304, USA. E-mail: tcs1{at}stanford.edu
2 Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA. E-mail: james.rothman{at}yale.edu


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Munc18-1 domain-1 controls vesicle docking and secretion by interacting with syntaxin-1 and chaperoning it to the plasma membrane.
G. A. Han, N. T. Malintan, N. M. N. Saw, L. Li, L. Han, F. A. Meunier, B. M. Collins, and S. Sugita (2011)
Mol. Biol. Cell 22, 4134-4149
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