The dynamic role of palmitoylation in signal transduction

Trends Biochem Sci. 1995 May;20(5):181-7. doi: 10.1016/s0968-0004(00)89004-0.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Molecular Sequence Data
  • Palmitates / metabolism*
  • Protein Processing, Post-Translational
  • Signal Transduction / physiology*

Substances

  • Palmitates