Protein lipidation

被引：198

作者：

Nadolski, Marissa J. ^{[1
]}

Linder, Maurine E. ^{[1
]}

机构：

[1] Washington Univ, Sch Med, Dept Cell Biol & Physiol, St Louis, MO 63110 USA

来源：

FEBS JOURNAL | 2007年 / 274卷 / 20期

关键词：

DHHC-CRD; fatty acylation; myristoylation; palmitoylation; prenylation; protein acyltransferase; protein lipidation; S-palmitoylation; Ras; ZDHHC;

D O I：

10.1111/j.1742-4658.2007.06056.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：

Proteins are covalently modified with a variety of lipids, including fatty acids, isoprenoids, and cholesterol. Lipid modifications play important roles in the localization and function of proteins. The focus of this review is S-palmitoylation, the reversible addition of palmitate and other long-chain fatty acids to proteins at cysteine residues in a variety of sequence contexts. The functional consequences of palmitoylation are diverse. Palmitoylation facilitates the association of proteins with membranes, mediates protein trafficking, and more recently has been appreciated as a regulator of protein stability. Members of a family of integral membrane proteins that harbor a DHHC cysteine-rich domain mediate most cellular palmitoylation events. Here we focus on DHHC proteins that modify Ras proteins in yeast and mammalian cells.

引用

页码：5202 / 5210

页数：9

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