| The Membrane Fusion Enigma: SNAREs, Sec1/Munc18 Proteins, and Their Accomplices-Guilty as Charged? | |
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MedLine Citation:
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PMID: 23057743 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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Neurotransmitter release is governed by proteins that have homo-logs in most types of intracellular membrane fusion, including the Sec1/Munc18 protein Munc18-1 and the SNARE proteins syntaxin-1, synaptobrevin/VAMP, and SNAP-25. The SNAREs initiate fusion by forming tight SNARE complexes that bring the vesicle and plasma membranes together. SNARE maintenance in a functional state depends on two chaperone systems (Hsc70/αCSP/SGT and synuclein); defects in these systems lead to neurodegeneration. Munc18-1 binds to an autoinhibitory closed conformation of syntaxin-1, gating formation of SNARE complexes, and also binds to SNARE complexes, which likely underlies the crucial function of Munc18-1 in membrane fusion by an as-yet unclear mechanism. Syntaxin-1 opening is mediated by Munc13s through their MUN domain, which is homologous to diverse tethering factors and may also have a general role in fusion. MUN domain activity is likely modulated in diverse presynaptic plasticity processes that depend on Ca(2+) and RIM proteins, among others. |
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Authors:
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Josep Rizo; Thomas C Südhof |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Annual review of cell and developmental biology Volume: 28 ISSN: 1530-8995 ISO Abbreviation: Annu. Rev. Cell Dev. Biol. Publication Date: 2012 Nov |
Date Detail:
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Created Date: 2012-10-12 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9600627 Medline TA: Annu Rev Cell Dev Biol Country: United States |
Other Details:
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Languages: eng Pagination: 279-308 Citation Subset: IM |
Affiliation:
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Departments of Biophysics, Biochemistry and Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390; email: jose@arnie.swmed.edu. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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