nSec1 Binds a Closed Conformation of Syntaxin1A

doi:10.1083/jcb.148.2.247

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© The Rockefeller University Press, 0021-9525/2000/1/247/ $5.00
The Journal of Cell Biology, Volume 148, Number 2, January 24, 2000 247-252

Brief report

nSec1 Binds a Closed Conformation of Syntaxin1A

Bin Yang^a, Martin Steegmaier^a, Lino C. Gonzalez, Jr.^a, and Richard H. Scheller^a
^a Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305-5428

Correspondence to: Richard H. Scheller, Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305-5428. Tel:650-723-9075 Fax:650-725-4436 E-mail:scheller{at}cmgm.stanford.edu.

The Sec1 family of proteins is proposed to function in vesicletrafficking by forming complexes with target membrane SNAREs(soluble N-ethylmaleimide-sensitive factor [NSF] attachmentprotein [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 syntaxin1Awith the core SNARE components, SNAP-25 (synaptosome-associatedprotein of 25 kD) and VAMP2 (vesicle-associated membrane protein2), precludes the interaction with nSec1 (also called Munc18and rbSec1). Inversely, association of nSec1 and syntaxin1Aprevents assembly of the ternary SNARE complex. Furthermore,using chemical cross-linking of rat brain membranes, we identifiednSec1 complexes containing syntaxin1A, but not SNAP-25 or VAMP2.These results support the hypothesis that Sec1 proteins functionas syntaxin chaperons during vesicle docking, priming, and membranefusion.

Key Words: membrane fusion, synaptic vesicles, exocytosis, SNARE, synapse

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