Document Detail


The Membrane Fusion Enigma: SNAREs, Sec1/Munc18 Proteins, and Their Accomplices-Guilty as Charged?
MedLine Citation:
PMID:  23057743     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
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.
Authors:
Josep Rizo; Thomas C Südhof
Related Documents :
24043423 - Characterisation of native protein complexes and protein isoform variation using size-f...
23799143 - Characterization of pud-1 and pud-2, two proteins up-regulated in a long-lived daf-2 mu...
22899913 - The aggregation of huntingtin and α-synuclein.
Publication Detail:
Type:  Journal Article    
Journal Detail:
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:
Created Date:  2012-10-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9600627     Medline TA:  Annu Rev Cell Dev Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  279-308     Citation Subset:  IM    
Affiliation:
Departments of Biophysics, Biochemistry and Pharmacology, University of Texas Southwestern Medical Center, Dallas, Texas 75390; email: jose@arnie.swmed.edu.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Structural basis of the unfolded protein response.
Next Document:  Bioengineering methods for analysis of cells in vitro.