Effects of farnesylcysteine analogs on protein carboxyl methylation and signal transduction

C. Volker, R. A. Miller, W. R. McCleary, A. Rao, M. Poenie, J. M. Backer, J. B. Stock

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128 Scopus citations

Abstract

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 p21(ras) 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
Volume266
Issue number32
StatePublished - Jan 1 1991

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Volker, C., Miller, R. A., McCleary, W. R., Rao, A., Poenie, M., Backer, J. M., & Stock, J. B. (1991). Effects of farnesylcysteine analogs on protein carboxyl methylation and signal transduction. Journal of Biological Chemistry, 266(32), 21515-21522.