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Phosphoinositide 3‐kinase and integrin signalling are involved in activation of Bruton tyrosine kinase in thrombin‐stimulated platelets
Author(s) -
Laffargue Muriel,
Ragab-Thomas Jeannie M.F.,
Ragab Ashraf,
Tuech Joel,
Missy Karine,
Monnereau Laurent,
Blank Ulrich,
Plantavid Monique,
Payrastre Bernard,
Raynal Patrick,
Chap Hugues
Publication year - 1999
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/s0014-5793(98)01680-9
Subject(s) - bruton's tyrosine kinase , pleckstrin homology domain , phosphoinositide 3 kinase , proto oncogene tyrosine protein kinase src , tyrosine kinase , microbiology and biotechnology , receptor tyrosine kinase , chemistry , integrin , ror1 , kinase , phosphorylation , signal transduction , biochemistry , biology , protein kinase b , platelet derived growth factor receptor , receptor , growth factor
Bruton tyrosine kinase (Btk) plays a crucial role in the differentiation of B lymphocytes and belongs to the group of Tec kinases, which are characterised by the presence of a pleckstrin homology domain. Here we show that Btk is activated and undergoes tyrosine phosphorylation upon challenge of platelet thrombin receptor, these responses requiring engagement of α IIb /β 3 integrin and phosphoinositide 3‐kinase activity. These data unravel a novel signalling pathway involving Btk downstream of an adhesive receptor via a complex regulation implicating the products of phosphoinositide 3‐kinase, which might act to anchor Btk at the membrane.