Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins

Covalent modification by fatty acylation and prenylation occurs on a wide variety of cellular signalling proteins. The enzymes that catalyze attachment of these lipophilic moieties to proteins have recently been identified and characterized. Each lipophilic group confers unique properties to the mod...

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Published in:Cellular Signalling 1996-09, Vol.8 (6), p.403-412
Main Author: Resh, Marilyn D
Format: Article
Language:English
Subjects:
Acylation
Acyltransferases
Animals
Fatty Acids - metabolism
G proteins
Humans
Myristoylation
Palmitoylation
Prenylation
Protein Processing, Post-Translational - physiology
Proteins - metabolism
Ras
Signal Transduction - physiology
Src family
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description Covalent modification by fatty acylation and prenylation occurs on a wide variety of cellular signalling proteins. The enzymes that catalyze attachment of these lipophilic moieties to proteins have recently been identified and characterized. Each lipophilic group confers unique properties to the modified protein, resulting in alterations in protein/protein interactions, membrane binding and targeting, and intracellular signalling. The biochemistry and cell biology of protein myristoylation, palmitoylation, farnesylation and geranylgeranylation is reviewed here, with emphasis on the Src family of tyrosine kinases, Ras proteins and G protein coupled signalling systems.
doi_str_mv 10.1016/S0898-6568(96)00088-5
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subjects Acylation
Acyltransferases
Animals
Fatty Acids - metabolism
G proteins
Humans
Myristoylation
Palmitoylation
Prenylation
Protein Processing, Post-Translational - physiology
Proteins - metabolism
Ras
Signal Transduction - physiology
Src family
title Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins
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