What is the role of SNARE proteins in membrane fusion?

被引:89
作者
Duman, JG [1 ]
Forte, JG [1 ]
机构
[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
来源
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY | 2003年 / 285卷 / 02期
关键词
soluble N-ethylmaleimide-sensitive factor activating protein receptor;
D O I
10.1152/ajpcell.00091.2003
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Soluble N-ethylmaleimide- sensitive factor activating protein receptor (SNARE) proteins have been at the forefront of research on biological membrane fusion for some time. The subcellular localization of SNAREs and their ability to form the so-called SNARE complex may be integral to determining the specificity of intracellular fusion (the SNARE hypothesis) and/or serving as the minimal fusion machinery. Both the SNARE hypothesis and the idea of the minimal fusion machinery have been challenged by a number of experimental observations in various model systems, suggesting that SNAREs may have other functions. Considering recent advances in the SNARE literature, it appears that SNAREs may actually function as part of a complex fusion "machine." Their role in the machinery could be any one or a combination of roles, including establishing tight membrane contact, formation of a scaffolding on which to build the machine, binding of lipid surfaces, and many others. It is also possible that complexations other than the classic SNARE complex participate in membrane fusion.
引用
收藏
页码:C237 / C249
页数:13
相关论文
共 139 条
[1]   High calcium concentrations shift the mode of exocytosis to the kiss-and-run mechanism [J].
Alés, E ;
Tabares, L ;
Poyato, JM ;
Valero, V ;
Lindau, M ;
de Toledo, GA .
NATURE CELL BIOLOGY, 1999, 1 (01) :40-44
[2]   Syntaxin 3 is required for cAMP-induced acid secretion: streptolysin O-permeabilized gastric gland model [J].
Ammar, DA ;
Zhou, RH ;
Forte, JG ;
Yao, XB .
AMERICAN JOURNAL OF PHYSIOLOGY-GASTROINTESTINAL AND LIVER PHYSIOLOGY, 2002, 282 (01) :G23-G33
[3]   The N-terminal domains of syntaxin 7 and vti1b form three-helix bundles that differ in their ability to regulate SNARE complex assembly [J].
Antonin, W ;
Dulubova, I ;
Araç, D ;
Pabst, S ;
Plitzner, J ;
Rizo, J ;
Jahn, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (39) :36449-36456
[4]   Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs [J].
Antonin, W ;
Fasshauer, D ;
Becker, S ;
Jahn, R ;
Schneider, TR .
NATURE STRUCTURAL BIOLOGY, 2002, 9 (02) :107-111
[5]   A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function [J].
Antonin, W ;
Holroyd, C ;
Fasshauer, D ;
Pabst, S ;
von Mollard, GF ;
Jahn, R .
EMBO JOURNAL, 2000, 19 (23) :6453-6464
[6]   Complexin regulates the closure of the fusion pore during regulated vesicle exocytosis [J].
Archer, DA ;
Graham, ME ;
Burgoyne, RD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (21) :18249-18252
[7]   Phosphorylation of Munc18 by protein kinase C regulates the kinetics of exocytosis [J].
Barclay, JW ;
Craig, TJ ;
Fisher, RJ ;
Ciufo, LF ;
Evans, GJO ;
Morgan, A ;
Burgoyne, RD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (12) :10538-10545
[8]   Hrs-2 is an ATPase implicated in calcium-regulated secretion [J].
Bean, AJ ;
Seifert, R ;
Chen, YA ;
Sacks, R ;
Scheller, RH .
NATURE, 1997, 385 (6619) :826-829
[9]   FUNCTIONAL IMPACT OF SYNTAXIN ON GATING OF N-TYPE AND Q-TYPE CALCIUM CHANNELS [J].
BEZPROZVANNY, I ;
SCHELLER, RH ;
TSIEN, RW .
NATURE, 1995, 378 (6557) :623-626
[10]   Members of the synaptobrevin/vesicle-associated membrane protein (VAMP) family in Drosophila are functionally interchangeable in vivo for neurotransmitter release and cell viability [J].
Bhattacharya, S ;
Stewart, BA ;
Niemeyer, BA ;
Burgess, RW ;
McCabe, BD ;
Lin, P ;
Boulianne, G ;
O'Kane, CJ ;
Schwarz, TL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (21) :13867-13872