SEARCH

SEARCH BY CITATION

Keywords:

  • DHHC-CRD;
  • fatty acylation;
  • myristoylation;
  • palmitoylation;
  • prenylation;
  • protein acyltransferase;
  • protein lipidation;
  • S-palmitoylation;
  • Ras;
  • ZDHHC

Proteins are covalently modified with a variety of lipids, including fatty acids, isoprenoids, and cholesterol. Lipid modifications play important roles in the localization and function of proteins. The focus of this review is S-palmitoylation, the reversible addition of palmitate and other long-chain fatty acids to proteins at cysteine residues in a variety of sequence contexts. The functional consequences of palmitoylation are diverse. Palmitoylation facilitates the association of proteins with membranes, mediates protein trafficking, and more recently has been appreciated as a regulator of protein stability. Members of a family of integral membrane proteins that harbor a DHHC cysteine-rich domain mediate most cellular palmitoylation events. Here we focus on DHHC proteins that modify Ras proteins in yeast and mammalian cells.