Long coiled-coil proteins and membrane traffic

被引:176
作者
Gillingham, AK [1 ]
Munro, S [1 ]
机构
[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2003年 / 1641卷 / 2-3期
关键词
coiled-coil; vesicle tethering; golgin; Golgi; endosome; rab GTPase;
D O I
10.1016/S0167-4889(03)00088-0
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 transport between organelles is mediated by vesicles which must accurately dock and fuse with appropriate compartments. Over the past several years a large number of long coiled-coil proteins have been identified on the Golgi and on endosomes, mostly as autoantigens in autoimmune disorders. Based on their restricted intracellular distributions and their predicted rod-like structure, these proteins have been proposed to play a role in tethering vesicles to target organelles prior to fusion. However, such proteins may also play a structural role, for example as components of a Golgi matrix, or as scaffolds for the assembly of other factors important for fusion. This review will examine what is known about the function of these large coiled-coil proteins in membrane traffic. (C) 2003 Elsevier B.V. All rights reserved.
引用
收藏
页码:71 / 85
页数:15
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