Protein farnesylation: implications for normal physiology, malignant transformation, and cancer therapy

Cancer Cell. 2005 Apr;7(4):297-300. doi: 10.1016/j.ccr.2005.04.005.

Abstract

Protein farnesylation is a lipid posttranslational modification required for the cancer-causing activity of proteins such as the GTPase Ras. Although farnesyltransferase inhibitors (FTIs) are in clinical trials, their mechanism of action and the role of protein farnesylation in normal physiology are ill understood. In this issue of Cancer Cell, two articles shed light on these important issues. Protein farnesylation was found to be essential for early embryogenesis, dispensable for adult homeostasis, and critical for progression but not initiation of tumorigenesis. Furthermore, Rab geranylgeranyltransferase was identified as a target for some FTIs. This minireview discusses the implications of these findings on normal physiology, malignant transformation, and cancer therapy.

Publication types

  • Review

MeSH terms

  • Alkyl and Aryl Transferases / antagonists & inhibitors
  • Alkyl and Aryl Transferases / metabolism
  • Animals
  • Caenorhabditis elegans
  • Cell Proliferation / drug effects
  • Cell Transformation, Neoplastic / metabolism*
  • Embryonic Development / physiology
  • Enzyme Inhibitors / pharmacology
  • Enzyme Inhibitors / therapeutic use
  • Homeostasis / physiology
  • Humans
  • Mice
  • Neoplasms / drug therapy*
  • Protein Prenylation / drug effects
  • Protein Prenylation / physiology*
  • Protein Processing, Post-Translational / physiology
  • rab GTP-Binding Proteins / metabolism
  • ras Proteins / metabolism
  • rho GTP-Binding Proteins / metabolism

Substances

  • Enzyme Inhibitors
  • Alkyl and Aryl Transferases
  • p21(ras) farnesyl-protein transferase
  • rab GTP-Binding Proteins
  • ras Proteins
  • rho GTP-Binding Proteins