Phosphoinositide 3‐kinase and integrin signalling are involved in activation of Bruton tyrosine kinase in thrombin‐stimulated platelets

FEBS Letters

Laffargue, Muriel¹  Payrastre, Bernard¹  Blank, Ulrich²  Ragab, Ashraf¹  Chap, Hugues¹  Plantavid, Monique¹  Ragab-Thomas, Jeannie M.F.¹  Monnereau, Laurent¹  Tuech, Joel¹  Missy, Karine¹  Raynal, Patrick¹ 

[1] Institut Fédératif de Recherche en Immunologie Cellulaire et Moléculaire, Université Paul Sabatier and Centre Hospitalo-Universitaire de Toulouse, INSERM Unité 326, Phospholipides Membranaires, Signalisation Cellulaire et Lipoprotéines, Hôpital Purpan, 31059 Toulouse Cedex, France;Département d'Immuno-Allergie, Institut Pasteur, Paris, France

关键词: Bruton tyrosine kinase;    Platelet;    Phosphoinositide 3-kinase;    αIIb/β3 integrin;    Thrombin;   

DOI  :  10.1016/S0014-5793(98)01680-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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/β₃ 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.

【 授权许可】

Unknown