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

Brief Report

Nsec1 Binds a Closed Conformation of Syntaxin1a



Bin Yanga, Martin Steegmaiera, Lino C. Gonzalez, Jr.a, and Richard H. Schellera

a Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94305-5428
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305-5428.650-725-4436650-723-9075

scheller{at}cmgm.stanford.edu

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.

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

© 2000 The Rockefeller University Press

Abbreviations used in this paper: DSS, disuccinimidyl suberate; GST, glutathione S-transferase; NSF, N-ethylmaleimide-sensitive factor; SNAP, soluble NSF attachment protein; SNAP-25, synaptosome-associated protein of 25 kD; SNARE, SNAP receptor; VAMP, vesicle-associated membrane protein.


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