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


Author: Resh, M. D.
Article Title: Regulation of cellular signalling by fatty acid acylation and prenylation of signal transduction proteins
Abstract: 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.
Keywords: signal transduction; carrier protein; review; nonhuman; proteins; animals; protein tyrosine kinase; protein processing, post-translational; ras protein; fatty acids; cell communication; guanine nucleotide binding protein; ras; lipophilicity; protein modification; membrane binding; acylation; palmitoylation; myristylation; fatty acid metabolism; acyltransferases; prenylation; src family; humans; human; priority journal; g proteins; myristoylation
Journal Title: Cellular Signalling
Volume: 8
Issue: 6
ISSN: 0898-6568
Publisher: Elsevier Inc.  
Date Published: 1996-09-01
Start Page: 403
End Page: 412
Language: English
DOI: 10.1016/s0898-6568(96)00088-5
PUBMED: 8958442
PROVIDER: scopus
DOI/URL:
Notes: Review -- Export Date: 22 November 2017 -- Source: Scopus
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  1. Marilyn D Resh
    120 Resh
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