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Curr Opin Cell Biol. 2005 Apr;17(2):190-6.

Fatty acylation and prenylation of proteins: what's hot in fat.

Author information

1
Imperial College London, Section of Cell and Molecular Biology, Division of Biomedical Sciences, Sir Alexander Fleming Building, London, SW72AZ, UK. t.magee@imperial.ac.uk

Abstract

Post-translational modification by covalent attachment of lipid groups helps proteins to associate with membranes, both intra- and extracellularly. The enzymology of protein S-acylation with fatty acids has been a stumbling block, but three pathways for this modification have now been identified in eukaryotes. It is not yet clear whether this reaction is enzymatic or facilitated by a chaperone-like mechanism. Work with Ras proteins has shown that an S-acylation/deacylation cycle, in cooperation with prenylation and carboxyl-methylation, may regulate their cycling between intracellular membrane compartments and subdomains, hence controlling their signalling activity. The two types of prenyl group, geranylgeranyl and farnesyl, themselves have surprisingly specific targeting roles for Ras superfamily members.

PMID:
15780596
DOI:
10.1016/j.ceb.2005.02.003
[Indexed for MEDLINE]

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