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

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 sig...

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Bibliographic Details
Published in:BBA - Molecular Cell Research 1999-08, Vol.1451 (1), p.1-16
Main Author: Resh, Marilyn D.
Format: Article
Language:English
Subjects:
Acylation
Acyltransferases - chemistry
Amino Acid Sequence
Cell Membrane - chemistry
Fatty acylation
Membrane proteins
Membrane rafts
Molecular Sequence Data
Myristic Acid - chemistry
Myristoylation
Palmitic Acid - chemistry
Palmitoylation
Protein Binding
Protein Sorting Signals - chemistry
Proteins - chemistry
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Summary: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 α 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.
ISSN:0167-4889
0006-3002
1879-2596
DOI:10.1016/S0167-4889(99)00075-0