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The association of pp125 FAK , pp60 Src , CDC42Hs and Rap1B with the cytoskeleton of aggregated platelets is a reversible process regulated by calcium
Author(s) -
Dash Debabrata,
Aepfelbacher Martin,
Siess Wolfgang
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00320-9
Subject(s) - cytoskeleton , microbiology and biotechnology , bapta , platelet activation , chemistry , proto oncogene tyrosine protein kinase src , integrin , biology , signal transduction , biochemistry , extracellular , platelet , receptor , cell , immunology
The integrin α IIb β 3 ‐mediated redistribution of the tyrosine kinases pp125 FAK and pp60 Src and the small GTP‐binding proteins CDC42Hs and Rap1B from the membrane skeleton to the cytoskeleton was found to be reversible: upon prolonged platelet aggregation (up to 15 min) induced by the thrombin‐receptor activating peptide (TRAP) these signalling proteins dissociated from the cytoskeleton and reappeared in the membrane skeleton. Addition of the extracellular Ca 2+ chelator EGTA and the intracellular Ca 2+ chelator BAPTA/AM 30 s after TRAP allowed platelet aggregation and the association of pp125 FAK , pp60 Src , CDC42Hs and Rap1B with the cytoskeleton, but prevented their dissociation from the cytoskeleton. The results indicate that the prolonged elevation of cytosolic Ca 2+ in stimulated platelets leads to the dissociation of signalling proteins from the cytoskeleton.