Palmitoylation and the trafficking of peripheral membrane proteins

被引：28

作者：

Chamberlain, Luke H. ^{[1
]}

Lemonidis, Kimon ^{[1
]}

Sanchez-Perez, Maria ^{[1
]}

Werno, Martin W. ^{[1
]}

Gorleku, Oforiwa A. ^{[1
]}

Greaves, Jennifer ^{[1
]}

机构：

[1] Univ Strathclyde, Strathdyde Inst Pharm & Biomed Sci, Glasgow G4 0RE, Lanark, Scotland

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2013年 / 41卷

基金：

英国惠康基金; 英国医学研究理事会;

关键词：

cysteine-string protein; DHHC protein; palmitoylation; 25 kDa synaptosome-associated protein (SNAP25); CYSTEINE-STRING PROTEIN; PLASMA-MEMBRANE; SYNAPTOTAGMIN-I; RICH DOMAIN; PC12; CELLS; CAAX MOTIF; RAS; PATHWAY; SNAP-25; SNAP25;

D O I：

10.1042/BST20120243

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：

Palmitoylation, the attachment of palmitate and other fatty acids on to cysteine residues, is a common post-translational modification of both integral and peripheral membrane proteins. Dynamic palmitoylation controls the intracellular distribution of peripheral membrane proteins by regulating membrane-cytosol exchange and/or by modifying the flux of the proteins through vesicular transport systems.

引用

页码：62 / 66

页数：5

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