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.