Document Detail


An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming.
MedLine Citation:
PMID:  11460165     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The priming step of synaptic vesicle exocytosis is thought to require the formation of the SNARE complex, which comprises the proteins synaptobrevin, SNAP-25 and syntaxin. In solution syntaxin adopts a default, closed configuration that is incompatible with formation of the SNARE complex. Specifically, the amino terminus of syntaxin binds the SNARE motif and occludes interactions with the other SNARE proteins. The N terminus of syntaxin also binds the presynaptic protein UNC-13 (ref. 5). Studies in mouse, Drosophila and Caenorhabditis elegans suggest that UNC-13 functions at a post-docking step of exocytosis, most likely during synaptic vesicle priming. Therefore, UNC-13 binding to the N terminus of syntaxin may promote the open configuration of syntaxin. To test this model, we engineered mutations into C. elegans syntaxin that cause the protein to adopt the open configuration constitutively. Here we demonstrate that the open form of syntaxin can bypass the requirement for UNC-13 in synaptic vesicle priming. Thus, it is likely that UNC-13 primes synaptic vesicles for fusion by promoting the open configuration of syntaxin.
Authors:
J E Richmond; R M Weimer; E M Jorgensen
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Nature     Volume:  412     ISSN:  0028-0836     ISO Abbreviation:  Nature     Publication Date:  2001 Jul 
Date Detail:
Created Date:  2001-07-19     Completed Date:  2001-08-16     Revised Date:  2013-06-09    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  England    
Other Details:
Languages:  eng     Pagination:  338-41     Citation Subset:  IM    
Affiliation:
Department of Biology, University of Utah, Salt Lake City 84112-0840, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Caenorhabditis elegans
Caenorhabditis elegans Proteins*
Calcium / metabolism
Helminth Proteins / metabolism*
Magnetic Resonance Spectroscopy
Membrane Fusion
Membrane Proteins / chemistry,  genetics,  metabolism*
Mutagenesis
Protein Binding
Protein Conformation
Qa-SNARE Proteins
SNARE Proteins
Synaptic Vesicles / metabolism*
Vesicular Transport Proteins*
Grant Support
ID/Acronym/Agency:
R03 MH059820-01/MH/NIMH NIH HHS; R03 MH059820-02/MH/NIMH NIH HHS
Chemical
Reg. No./Substance:
0/Caenorhabditis elegans Proteins; 0/Helminth Proteins; 0/Membrane Proteins; 0/Qa-SNARE Proteins; 0/SNARE Proteins; 0/Unc-13 protein, C elegans; 0/Vesicular Transport Proteins; 7440-70-2/Calcium
Comments/Corrections

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


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