Signalling functions of protein palmitoylation

被引:289
作者
Dunphy, JT [1 ]
Linder, ME [1 ]
机构
[1] Washington Univ, Sch Med, Dept Cell Biol & Physiol, St Louis, MO 63110 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 1998年 / 1436卷 / 1-2期
关键词
fatty acylation; thioacylation; protein tyrosine kinase; G protein; caveolae; cholesterol;
D O I
10.1016/S0005-2760(98)00130-1
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
Covalent lipid modifications anchor numerous signalling proteins to the cytoplasmic face of the plasma membrane. These modifications mediate protein-membrane and protein-protein interactions and are often essential for function. Protein palmitoylation, due to its reversible nature, may be particularly important for modulating protein function during cycles of activation and deactivation. Despite intense investigation, the exact functions of protein palmitoylation are not well understood. However, it is clear that palmitoylation can affect a protein's affinity for membranes, subcellular localization, and interactions with other proteins. In this review, recent advances in understanding the functions and mechanisms of protein palmitoylation are discussed, with particular emphasis on how this lipid affects the biochemistry and cell biology of signalling proteins. (C) 1998 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:245 / 261
页数:17
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