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

Authors
Citation
Md. Resh, Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins, BBA-MOL CEL, 1451(1), 1999, pp. 1-16
Citations number
137
Categorie Soggetti
Cell & Developmental Biology
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
ISSN journal
01674889 → ACNP
Volume
1451
Issue
1
Year of publication
1999
Pages
1 - 16
Database
ISI
SICI code
0167-4889(19990812)1451:1<1:FAOPNI>2.0.ZU;2-B
Abstract
Covalent attachment of myristate and/or palmitate occurs on a wide variety of viral and cellular proteins. This review will highlight the latest advan ces in our understanding of the enzymology of N-myristoylation and palmitoy lation as well as the functional consequences of fatty acylation of key sig naling proteins. The role of myristate and palmitate in promoting membrane binding as well as specific membrane targeting will be reviewed, with empha sis on the Src family of tyrosine protein kinases and alpha subunits of het erotrimeric G proteins. The use of myristoyl switches and regulated depalmi toylation as mechanisms for achieving reversible membrane binding and regul ated signaling will also be explored. (C) 1999 Elsevier Science B.V. All ri ghts reserved.