Vesicle budding on Golgi membranes: Regulation by G proteins and myosin motors

被引：52

作者：

Stow, JL ^{[1
]}

Heimann, K ^{[1
]}

机构：

[1] Univ Queensland, Ctr Cellular & Mol Biol, Brisbane, Qld 4072, Australia

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 1998年 / 1404卷 / 1-2期

关键词：

G protein; membrane binding; constitutive secretion; transport vesicle; myosin II;

D O I：

10.1016/S0167-4889(98)00055-X

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：

One of the main functions of the Golgi complex is to generate transport vesicles for the post-Golgi trafficking of proteins in secretory pathways. Many different populations of vesicles are distinguished by unique sets of structural and regulatory proteins which participate in vesicle budding and fusion. Monomeric and heterotrimeric G proteins regulate vesicle budding and secretory traffic into and out of the Golgi complex. An inventory of G protein a subunits associated with Golgi membranes highlights their diverse involvement and potential for coupling Golgi trafficking, through various signal transduction pathways, to cell growth or other more specialized cell functions. Cytoskeletal proteins are now also known to associate specifically with the Golgi complex and Golgi-derived vesicles. Amongst these, conventional and unconventional myosins are recruited to vesicle membranes. Several roles in vesicle budding and vesicle trafficking can be proposed for these actin-based motors. (C) 1998 Elsevier Science B.V. All rights reserved.

引用

页码：161 / 171

页数：11

共 98 条

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