期刊文献

Phosphorylation of Bruton’s tyrosine kinase by c-Abl 收藏

通过c-Abl对Bruton酪氨酸激酶的磷酸化

原文求助发布源

作者

Carl-Magnus Bäckesjö[a]; Leonardo Vargas[a]; Giulio Superti-Furga[b]; C.I Edvard Smith[a]

作者单位

[a] Clinical Research Center, Karolinska Institutet, Huddinge University Hospital, SE-141 86 Huddinge, Sweden [b] Developmental Biology Programme, European Molecular Biology Laboratory, and Cellzome AG, Meyerhofstrasse 1, D-69117 Heidelberg, Germany Received 14 October 2002, Available online 15 November 2002

关键词

Bruton’s tyrosine kinase; Btk; c-Abl; Tyrosine phosphorylation; SH3

关键词译文

Bruton的酪氨酸激酶; Btk c-Abl酪氨酸磷酸化; SH3

发布日期

15 November 2002

页码

510–515

DOI

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

来源信息

Biochemical and Biophysical Research Communications ISSN：0006-291X, 2002年, 299卷, 3期, 510–515页

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-Abl 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.

摘要译文

Bruton酪氨酸激酶（Btk）对于B淋巴细胞发育是必需的。编码Btk的基因中的突变导致人类中的X-连锁性丙种球蛋白血症（XLA）。类似于Btk，c-Abl是细胞质与细胞质之间的酪氨酸激酶穿梭根据本地化，其涉及不同功能的核。在本报告中，我们首次描述了c-Abl和Btk物理相互作用，c-Abl可以在Btk的SH3结构域中磷酸化酪氨酸223有趣的是， Btk序列与从随机肽文库鉴定的优选的已知v-Abl底物匹配，并且与先前发现的许多c-Abl底物高度相关

Carl-Magnus Bäckesjö[a]; Leonardo Vargas[a]; Giulio Superti-Furga[b]; C.I Edvard Smith[a]. Phosphorylation of Bruton’s tyrosine kinase by c-Abl[J]. Biochemical and Biophysical Research Communications, 2002,299(3): 510–515