Publikationsdatum:
1993-02-12
Beschreibung:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Philips, M R -- Pillinger, M H -- Staud, R -- Volker, C -- Rosenfeld, M G -- Weissmann, G -- Stock, J B -- AR-07176-18/AR/NIAMS NIH HHS/ -- GM 20277/GM/NIGMS NIH HHS/ -- GM-8309/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):977-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, New York University Medical Center, NY 10016.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438158" target="_blank"〉PubMed〈/a〉
Schlagwort(e):
Cell Membrane/metabolism
;
Cytosol/metabolism
;
GTP-Binding Proteins/*metabolism
;
*Guanine Nucleotide Dissociation Inhibitors
;
Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology
;
Guanosine Triphosphate/pharmacology
;
Humans
;
Methionine/analogs & derivatives/metabolism
;
Methylation
;
N-Formylmethionine Leucyl-Phenylalanine/pharmacology
;
Neutrophils/*physiology
;
Protein Methyltransferases/metabolism
;
Proto-Oncogene Proteins/*metabolism
;
Proto-Oncogene Proteins p21(ras)/metabolism
;
S-Adenosylmethionine/metabolism
;
Signal Transduction/*physiology
;
Tritium
;
rap GTP-Binding Proteins
;
rho-Specific Guanine Nucleotide Dissociation Inhibitors
Print ISSN:
0036-8075
Digitale ISSN:
1095-9203
Thema:
Biologie
,
Chemie und Pharmazie
,
Informatik
,
Medizin
,
Allgemeine Naturwissenschaft
,
Physik
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