DHHC palmitoyl transferases: substrate interactions and (patho)physiology

被引：269

作者：

Greaves, Jennifer ^{[1
]}

Chamberlain, Luke H. ^{[1
]}

机构：

[1] Univ Edinburgh, Ctr Integrat Physiol, Edinburgh EH8 9XD, Midlothian, Scotland

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2011年 / 36卷 / 05期

基金：

英国医学研究理事会;

关键词：

2-STEP REACTION-MECHANISM; CYSTEINE-STRING PROTEIN; NITRIC-OXIDE SYNTHASE; SACCHAROMYCES-CEREVISIAE; MEDIATED PALMITOYLATION; MEMBRANE INTERACTIONS; MENTAL-RETARDATION; GABA(A) RECEPTORS; MAJOR SUBSTRATE; ALPHA-SUBUNITS;

D O I：

10.1016/j.tibs.2011.01.003

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：

S-palmitoylation is a reversible post-translational modification that occurs on diverse cellular proteins. Palmitoylation can affect proteins in many different ways, including regulating membrane attachment, intracellular trafficking, and membrane micro-localisation. Intracellular palmitoylation reactions are mediated by a family of recently identified aspartate-histidine-histidine-cysteine (DHHC) palmitoyl transferases. More than 20 DHHC proteins are encoded by mammalian genomes, and there is now a major effort to identify DHHC-substrate pairings and to determine how interaction specificity is encoded. Recent studies have highlighted how DHHC proteins regulate cell function and influence physiology and pathophysiology.

引用

页码：245 / 253

页数：9

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