title: The dynamic role of palmitoylation in signal transduction.
abstract: Guanine nucleotide binding protein (G protein)-linked receptors, the alpha-subunits of heterotrimeric G proteins and members of the Src family of nonreceptor tyrosine kinases are among many polypeptides that are posttranslationally modified by the addition of palmitate, a long-chain fatty acid. Attachment of palmitate to these proteins is dynamic and may be regulated by their activation. The presence of palmitate appears to play a key role in the membrane localization of either the entire polypeptide or parts of it, and may regulate the interactions of these polypeptides with other proteins.
authors.affiliation: Division of Biochemistry and Molecular Biology, University of Glasgow, UK.
authors.forename: G
authors.initials: G
authors.lastname: Milligan
authors.forename: M
authors.initials: M
authors.lastname: Parenti
authors.forename: A I
authors.initials: AI
authors.lastname: Magee
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D008969:Molecular Sequence Data; D010168:Palmitates / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction / Q000502:physiology*
chemical_list: D010168:Palmitates