Multisubunit Tethering Complexes and Their Role in Membrane Fusion

被引：170

作者：

Broecker, Cornelia ^{[1
]}

Engelbrecht-Vandre, Siegfried ^{[1
]}

Ungermann, Christian ^{[1
]}

机构：

[1] Univ Osnabruck, Dept Biol Chem, D-49076 Osnabruck, Germany

来源：

CURRENT BIOLOGY | 2010年 / 20卷 / 21期

关键词：

GUANINE-NUCLEOTIDE EXCHANGE; OLIGOMERIC GOLGI-COMPLEX; COILED-COIL PROTEINS; TRANS-SNARE COMPLEX; STRUCTURAL BASIS; BINDING-SITES; GARP COMPLEX; ENDOPLASMIC-RETICULUM; SECRETORY VESICLES; VACUOLE FUSION;

D O I：

10.1016/j.cub.2010.09.015

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Protein trafficking within eukaryotic cells depends on vesicular carriers that fuse with organelles to deliver their lipid and protein content. Cells have developed an elaborate system to capture vesicles at organelles that involves the action of Rab GTPases and tethers. Vesicle fusion then takes place with the help of SNARE proteins. In this review we focus on the role of multisubunit tethering complexes of eukaryotic cells. In particular, we discuss the tethering complexes of the secretory pathway and the endolysosomal system and highlight recent evidence for the role of these complexes in interaction with Rabs, coat recognition and cooperation with SNAREs during the fusion cascade.

引用

页码：R943 / R952

页数：10

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