Integrin alpha IIb beta 3-mediated translocation of CDC42Hs to the cytoskeleton in stimulated human platelets.

The Journal of Biological Chemistry
D DashW Siess

Abstract

To investigate the function of the human Ras-related CDC42 GTP-binding protein (CDC42Hs) we studied its subcellular redistribution in platelets stimulated by thrombin-receptor activating peptide (TRAP) or ADP. In resting platelets CDC42Hs was detected exclusively in the membrane skeleton (9.6 +/- 1.5% of total) and the detergent soluble fraction (90 +/- 4%). When platelets were aggregated with TRAP or ADP, CDC42Hs (10% of total) appeared in the cytoskeleton and decreased in the membrane skeleton, whereas RhoGDI (guanine-nucleotide dissociation inhibitor) and CDC42HsGAP (GTPase-activating protein) remained exclusively in the detergent-soluble fraction. Upon prolonged platelet stimulation CDC42Hs disappeared from the cytoskeleton and reappeared in the membrane skeleton. Rac translocated to the cytoskeleton with a similar time course as CDC42Hs. When platelets were stimulated under conditions that precluded the activation of the alpha IIb beta 3 integrin and platelet aggregation, cytoskeletal association of CDC42Hs was abolished. Translocation of CDC42Hs to the cytoskeleton but not aggregation was also prevented by cytochalasins B or D or the protein tyrosine kinase inhibitor genistein. Platelet secretion and thromboxane formation...Continue Reading

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Citations

Jan 15, 1997·The EMBO Journal·B FrankeJ L Bos
Nov 21, 1998·Cell Adhesion and Communication·G E JonesA J Ridley
Feb 3, 2015·Hämostaseologie·Margitta Elvers
Jan 27, 2005·Journal of Thrombosis and Haemostasis : JTH·H KashiwagiY Tomiyama
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Mar 10, 2015·The Biochemical Journal·Robert GoggsAlastair W Poole
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