Protein lipidation

FEBS J. 2007 Oct;274(20):5202-10. doi: 10.1111/j.1742-4658.2007.06056.x. Epub 2007 Sep 24.


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.

Publication types

  • Review

MeSH terms

  • Acyltransferases / metabolism*
  • Acyltransferases / physiology
  • Animals
  • Golgi Matrix Proteins
  • Humans
  • Lipoylation*
  • Membrane Proteins / metabolism*
  • Palmitic Acid / metabolism*


  • GOLGA7 protein, human
  • Golgi Matrix Proteins
  • Membrane Proteins
  • Palmitic Acid
  • Acyltransferases
  • ZDHHC9 protein, human