Recent advances in the study of prenylated proteins

Biochim Biophys Acta. 2000 Apr 12;1484(2-3):93-106. doi: 10.1016/s1388-1981(00)00009-3.


Post-translational modification of proteins with isoprenoids was first recognized as a general phenomenon in 1984. In recent years, our understanding, including mechanistic studies, of the enzymatic reactions associated with these modifications and their physiological functions has increased dramatically. Of particular functional interest is the role of prenylation in facilitating protein-protein interactions and membrane-associated protein trafficking. The loss of proper localization of Ras proteins when their farnesylation is inhibited has also permitted a new target for anti-malignancy pharmaceuticals. Recent advances in the enzymology and function of protein prenylation are reviewed in this article.

Publication types

  • Review

MeSH terms

  • Alkyl and Aryl Transferases / antagonists & inhibitors
  • Amino Acid Sequence
  • Antineoplastic Agents / chemistry
  • Drug Design
  • Farnesyltranstransferase
  • Humans
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Protein Prenylation*
  • Protein Processing, Post-Translational
  • Saccharomyces cerevisiae
  • ras Proteins / metabolism


  • Antineoplastic Agents
  • Membrane Proteins
  • Alkyl and Aryl Transferases
  • Farnesyltranstransferase
  • ras Proteins