Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins Journal Article


Author: Resh, M. D.
Article Title: Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
Abstract: 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. Copyright (C) 1999 Elsevier Science B.V.
Keywords: signal transduction; review; drug targeting; proteins; protein binding; membrane proteins; amino acid sequence; molecular sequence data; cell membrane; membrane binding; acylation; protein lipid interaction; palmitoylation; myristic acid; myristylation; transferase; fatty acylation; acyltransferases; palmitic acid; protein sorting signals; deacylation; membrane rafts; priority journal; myristoylation
Journal Title: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Volume: 1451
Issue: 1
ISSN: 0167-4889
Publisher: Elsevier B.V.  
Date Published: 1999-08-12
Start Page: 1
End Page: 16
Language: English
DOI: 10.1016/s0167-4889(99)00075-0
PUBMED: 10446384
PROVIDER: scopus
DOI/URL:
Notes: Review -- Export Date: 16 August 2016 -- Source: Scopus
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  1. Marilyn D Resh
    120 Resh