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Membrane Fusion: Grappling with SNARE and SM Proteins

This article reviews recent findings on membrane fusion within the cell. 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 α-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.

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Classifications


Resource Type: Journal article/Issue, Illustration, Review
Audience Level: Undergraduate lower division 13-14, Undergraduate upper division 15-16, Graduate, Professional (degree program), Continuing education

Author and Copyright


Authors and Editors: Thomas Südhof of Department of Cellular and Molecular Physiology, Stanford University, James Rothman of Department of Cell Biology, Yale University School of Medicine
Publisher: SCIENCE
Format: text/html
Copyright and other restrictions: Yes
Cost: No

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American Association for the Advancement of Science


     
   

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