Effects of farnesylcysteine analogs on protein carboxyl methylation and signal transduction

Craig Volker, Raymond A. Miller, William R. McCleary, Arundhati Rao, Martin Poenie, Joseph M. Backer, Jeffry B. Stock

Research output: Contribution to journalArticlepeer-review

144 Scopus citations


Several proteins associated with signal transduction in eukaryotes are carboxyl methylated at COOH-terminal S-farnesylcysteine residues. These include members of the Ras superfamily and γ-subunits of heterotrimeric G-proteins. The enzymes that catalyze the carboxyl methylation reaction also methylate small molecules such as N-acetyl-S-trans,trans-farnesyl-L-cysteine (AFC). AFC inhibits carboxyl methylation of p21ras and related proteins both in vitro and in vivo. Saturating concentrations of AFC cause a >80% inhibition of chemotactic responses of mouse peritoneal macrophages. Our results suggest that carboxyl methylation may play a role in the regulation of receptor-mediated signal transduction processes in eukaryotic cells.

Original languageEnglish (US)
Pages (from-to)21515-21522
Number of pages8
JournalJournal of Biological Chemistry
Issue number32
StatePublished - 1991

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


Dive into the research topics of 'Effects of farnesylcysteine analogs on protein carboxyl methylation and signal transduction'. Together they form a unique fingerprint.

Cite this