Phosphorylation of Bruton's tyrosine kinase by c-Abl

被引：27

作者：

Bäckesjö, CM ^{[1
]}

Vargas, L

Superti-Furga, G

Smith, CIE

机构：

[1] Huddinge Univ Hosp, Karolinska Inst, Clin Res Ctr, SE-14186 Huddinge, Sweden

[2] European Mol Biol Lab, Dev Biol Programme, D-69117 Heidelberg, Germany

[3] Cellzome AG, D-69117 Heidelberg, Germany

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 299卷 / 03期

关键词：

Bruton's tyrosine kinase; Btk; c-Abl; tyrosine phosphorylation; SH3;

D O I：

10.1016/S0006-291X(02)02643-8

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's tyrosine kinase (Btk) is necessary for B-lymphocyte development. Mutation in the gene coding for Btk causes X-linked agammaglobulinemia (XLA) in humans. Similar to Btk, c-Abl is a tyrosine kinase shuttling between the cytoplasm and the nucleus where it is involved in different functions depending on the localization. In this report we describe for the first time that c-AbI and Btk physically interact and that c-Abl can phosphorylate tyrosine 223 in the SH3 domain of Btk. Interestingly, the Btk sequence matched the preferred, known v-Abl substrate identified from a randomized peptide library and was also highly related to a number of previously found c-Abl substrates. (C) 2002 Elsevier Science (USA). All rights reserved.

引用

页码：510 / 515

页数：6

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