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Membrane Fusion: Grappling with SNARE and SM Proteins
- Source :
- Science. 323:474-477
- Publication Year :
- 2009
- Publisher :
- American Association for the Advancement of Science (AAAS), 2009.
-
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 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.
- Subjects :
- Munc18 Proteins
Vesicle fusion
Protein Conformation
Amino Acid Motifs
Vesicular Transport Proteins
Nerve Tissue Proteins
Biology
Membrane Fusion
Synaptic Transmission
Article
Synaptotagmin 1
Synaptotagmins
Complexin
Animals
Protein Structure, Quaternary
SNARE complex assembly
Multidisciplinary
Qa-SNARE Proteins
Vesicle-Associated Membrane Protein 2
Protein Structure, Tertiary
Cell biology
Synapses
Synaptic Vesicles
SNARE Proteins
SNARE complex
Synaptic vesicle priming
Protein Binding
Subjects
Details
- ISSN :
- 10959203 and 00368075
- Volume :
- 323
- Database :
- OpenAIRE
- Journal :
- Science
- Accession number :
- edsair.doi.dedup.....8ecbb8304c332be972f00cc053489f75