A complete set of SNAREs in yeast

被引:124
作者
Burri, L [1 ]
Lithgow, T [1 ]
机构
[1] Univ Melbourne, Russell Grimwade Sch Biochem & Mol Biol, Parkville, Vic 3010, Australia
关键词
anchored proteins; genomics; membrane fusion; SNARE; tail;
D O I
10.1046/j.1600-0854.2003.00151.x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Trafficking of cargo molecules through the secretory pathway relies on packaging and delivery of membrane vesicles. These vesicles, laden with cargo, carry integral membrane proteins that can determine with which target membrane the vesicle might productively fuse. The membrane fusion process is highly conserved in all eukaryotes and the central components driving membrane fusion events involved in vesicle delivery to target membranes are a set of integral membrane proteins called SNAREs. The yeast Saccharomyces cerevisiae has served as an extremely useful model for characterizing components of membrane fusion through genetics, biochemistry and bioinformatics, and it is now likely that the complete set of SNAREs is at hand. Here, we present the details from the searches for SNAREs, summarize the domain structures of the complete set, review what is known about localization of SNAREs to discrete membranes, and highlight some of the surprises that have come from the search.
引用
收藏
页码:45 / 52
页数:8
相关论文
共 70 条
[1]   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
[2]   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
[3]   Molecular recognition of cargo by the COPII complex: A most accommodating coat [J].
Barlowe, C .
CELL, 2003, 114 (04) :395-397
[4]   Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae [J].
Beilharz, T ;
Egan, B ;
Silver, PA ;
Hofmann, K ;
Lithgow, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (10) :8219-8223
[5]   Yeast functional analysis:: Identification of two essential genes involved in ER to Golgi trafficking [J].
Belgareh-Touzé, N ;
Corral-Debrinski, M ;
Launhardt, H ;
Galan, JM ;
Munder, T ;
Le Panse, S ;
Haguenauer-Tsapis, R .
TRAFFIC, 2003, 4 (09) :607-617
[6]   SYNTAXIN - A SYNAPTIC PROTEIN IMPLICATED IN DOCKING OF SYNAPTIC VESICLES AT PRESYNAPTIC ACTIVE ZONES [J].
BENNETT, MK ;
CALAKOS, N ;
SCHELLER, RH .
SCIENCE, 1992, 257 (5067) :255-259
[7]   A selective transport route from golgi to late endosomes that requires the yeast GGA proteins [J].
Black, MW ;
Pelham, HRB .
JOURNAL OF CELL BIOLOGY, 2000, 151 (03) :587-600
[8]   PURIFICATION OF AN N-ETHYLMALEIMIDE-SENSITIVE PROTEIN CATALYZING VESICULAR TRANSPORT [J].
BLOCK, MR ;
GLICK, BS ;
WILCOX, CA ;
WIELAND, FT ;
ROTHMAN, JE .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1988, 85 (21) :7852-7856
[9]   A genomic perspective on membrane compartment organization [J].
Bock, JB ;
Matern, HT ;
Peden, AA ;
Scheller, RH .
NATURE, 2001, 409 (6822) :839-841
[10]   Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p [J].
Bracher, A ;
Weissenhorn, W .
EMBO JOURNAL, 2002, 21 (22) :6114-6124