Identification and characterization of a novel SH3-domain binding protein, Sab, which preferentially associates with Bruton's tyrosine kinase (Btk)

被引:45
|
作者
Matsushita, M
Yamadori, T
Kato, S
Takemoto, Y
Inazawa, J
Baba, Y
Hashimoto, S
Sekine, S
Arai, S
Kunikata, T
Kurimoto, M
Kishimoto, T
Tsukada, S
机构
[1] Osaka Univ, Sch Med, Dept Med 3, Suita, Osaka 565, Japan
[2] Sagami Chem Res Ctr, Kanagawa 2290012, Japan
[3] Nippon Glaxo Ltd, Tsukuba Res Lab, Ibaraki, Osaka 3004247, Japan
[4] Univ Tokyo, Inst Med Sci, Lab Genome Med, Minato Ku, Tokyo 108, Japan
[5] Hayashibara Biochem Labs Inc, Fujisaki Inst, Okayama 702, Japan
关键词
D O I
10.1006/bbrc.1998.8420
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
Protein interaction cloning method was used to identify a novel molecule, Sab, which binds to the SH3 domain of Proton's tyrosine kinase (Btk), the deficient cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia and murine X-linked immunodeficiency. Immunoprecipitation using the anti-Sab antibody identified the protein product of the gene as a 70 kDa molecule. While Sab does not have a proline-rich sequence, it was shown to bind to Btk through the commonly conserved structure among SH3 domains. Remarkably, Sab exhibited a high preference for binding to Btk rather than to other cytoplasmic tyrosine kinases, which suggests a unique role of Sab in the Btk signal transduction pathway. (C) 1998 Academic Press.
引用
收藏
页码:337 / 343
页数:7
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