TY - JOUR
T1 - Carboxyl methylation of ras-related proteins during signal transduction in neutrophils
AU - Philips, Mark R.
AU - Pillinger, Michael H.
AU - Staud, Roland
AU - Volker, Craig
AU - Rosenfeld, Melvin G.
AU - Weissmann, Gerald
AU - Stock, Jeffry B.
PY - 1993/2/12
Y1 - 1993/2/12
N2 - 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.
AB - 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.
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U2 - 10.1126/science.8438158
DO - 10.1126/science.8438158
M3 - Article
C2 - 8438158
AN - SCOPUS:0027537491
SN - 0036-8075
VL - 259
SP - 977
EP - 980
JO - Science
JF - Science
IS - 5097
ER -