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

被引：34

作者：

Laffargue, M

Ragab-Thomas, JMF

Ragab, A

Tuech, J

Missy, K

Monnereau, L

Blank, U

Plantavid, M

Payrastre, B

Raynal, P

Chap, H ^{[1
]}

机构：

[1] Univ Toulouse 3, Inst Fed Rech Immunol Cellulaire & Mol, F-31059 Toulouse, France

[2] Ctr Hosp Univ Toulouse, INSERM U326, Hop Purpan, F-31059 Toulouse, France

[3] Inst Pasteur, Dept Immunoallergie, Paris, France

来源：

FEBS LETTERS | 1999年 / 443卷 / 01期

关键词：

Bruton tyrosine kinase; platelet; phosphoinositide; 3-kinase; alpha(IIb)/beta(3) integrin; thrombin;

D O I：

10.1016/S0014-5793(98)01680-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 alpha(IIb)/beta(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. (C) 1999 Federation of European Biochemical Societies.

引用

页码：66 / 70

页数：5

共 38 条

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