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Media type:
E-Article
Title:
Nsec1 Binds a Closed Conformation of Syntaxin1a
Contributor:
Yang, Bin;
Steegmaier, Martin;
Gonzalez, Lino C.;
Scheller, Richard H.
imprint:
Rockefeller University Press, 2000
Published in:
The Journal of Cell Biology, 148 (2000) 2, Seite 247-252
Language:
English
DOI:
10.1083/jcb.148.2.247
ISSN:
0021-9525;
1540-8140
Origination:
Footnote:
Description:
<jats:p>The Sec1 family of proteins is proposed to function in vesicle trafficking by forming complexes with target membrane SNAREs (soluble N-ethylmaleimide-sensitive factor [NSF] attachment protein [SNAP] receptors) of the syntaxin family. Here, we demonstrate, by using in vitro binding assays, nondenaturing gel electrophoresis, and specific neurotoxin treatment, that the interaction of syntaxin1A with the core SNARE components, SNAP-25 (synaptosome-associated protein of 25 kD) and VAMP2 (vesicle-associated membrane protein 2), precludes the interaction with nSec1 (also called Munc18 and rbSec1). Inversely, association of nSec1 and syntaxin1A prevents assembly of the ternary SNARE complex. Furthermore, using chemical cross-linking of rat brain membranes, we identified nSec1 complexes containing syntaxin1A, but not SNAP-25 or VAMP2. These results support the hypothesis that Sec1 proteins function as syntaxin chaperons during vesicle docking, priming, and membrane fusion.</jats:p>