Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins

被引:1055
作者
Resh, MD [1 ]
机构
[1] Mem Sloan Kettering Canc Ctr, Cell Biol Program, New York, NY 10021 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 1999年 / 1451卷 / 01期
关键词
fatty acylation; myristoylation; palmitoylation; membrane proteins; membrane rafts;
D O I
10.1016/S0167-4889(99)00075-0
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 attachment of myristate and/or palmitate occurs on a wide variety of viral and cellular proteins. This review will highlight the latest advances in our understanding of the enzymology of N-myristoylation and palmitoylation as well as the functional consequences of fatty acylation of key signaling proteins. The role of myristate and palmitate in promoting membrane binding as well as specific membrane targeting will be reviewed, with emphasis on the Src family of tyrosine protein kinases and alpha subunits of heterotrimeric G proteins. The use of myristoyl switches and regulated depalmitoylation as mechanisms for achieving reversible membrane binding and regulated signaling will also be explored. (C) 1999 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:1 / 16
页数:16
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