Document Detail

An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming.
MedLine Citation:
PMID:  11460165     Owner:  NLM     Status:  MEDLINE    
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.
J E Richmond; R M Weimer; E M Jorgensen
Related Documents :
15671485 - Copii coat assembly and selective export from the endoplasmic reticulum.
16601685 - Gga function is required for maturation of neuroendocrine secretory granules.
10603575 - Coat proteins regulating membrane traffic.
14745135 - The structure and function of ggas, the traffic controllers at the tgn sorting crossroads.
10749925 - Axonal membrane proteins are transported in distinct carriers: a two-color video micros...
17332375 - Creb-binding protein modulates repeat instability in a drosophila model for polyq disease.
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:  2014-09-21    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  England    
Other Details:
Languages:  eng     Pagination:  338-41     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Caenorhabditis elegans
Caenorhabditis elegans Proteins*
Calcium / metabolism
Carrier Proteins
Helminth Proteins / metabolism*
Magnetic Resonance Spectroscopy
Membrane Fusion
Membrane Proteins / chemistry,  genetics,  metabolism*
Protein Binding
Protein Conformation
Qa-SNARE Proteins
SNARE Proteins
Synaptic Vesicles / metabolism*
Vesicular Transport Proteins*
Grant Support
R03 MH059820/MH/NIMH NIH HHS; R03 MH059820-01/MH/NIMH NIH HHS; R03 MH059820-02/MH/NIMH NIH HHS
Reg. No./Substance:
0/Caenorhabditis elegans Proteins; 0/Carrier Proteins; 0/Helminth Proteins; 0/Membrane Proteins; 0/Qa-SNARE Proteins; 0/SNARE Proteins; 0/Vesicular Transport Proteins; 0/phorbol ester binding protein; SY7Q814VUP/Calcium

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

Previous Document:  Evolution and transmission of stable CTL escape mutations in HIV infection.
Next Document:  Hypermutation of multiple proto-oncogenes in B-cell diffuse large-cell lymphomas.