Carboxyl methylation of ras-related proteins during signal transduction in neutrophils

Mark R. Philips, Michael H. Pillinger, Roland Staud, Craig Volker, Melvin G. Rosenfeld, Gerald Weissmann, Jeffry B. Stock

Research output: Contribution to journalArticlepeer-review

178 Scopus citations

Abstract

In human neutrophils, as in other cell types, Ras-related guanosine triphosphate-binding proteins are directed toward their regulatory targets in membranes by a series of posttranslational modifications that include methyl esterification of a carboxyl-terminal prenylcysteine residue. In intact cells and in a reconstituted in vitro system, the amount of carboxyl methylation of Ras-related proteins increased in response to the chemoattractant N-formyl-methionyl-leucyl-phenylalanine (FMLP). Activation of Ras-related proteins by guanosine-5′-O-(3-thiotriphosphate) had a similar effect and induced translocation of p22rac2 from cytosol to plasma membrane. Inhibitors of prenylcysteine carboxyl methylation effectively blocked neutrophil responses to FMLP. These findings suggest a direct link between receptor-mediated signal transduction and the carboxyl methylation of Ras-related proteins.

Original languageEnglish (US)
Pages (from-to)977-980
Number of pages4
JournalScience
Volume259
Issue number5097
DOIs
StatePublished - Feb 12 1993

All Science Journal Classification (ASJC) codes

  • General

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