Bruton's tyrosine kinase activity is negatively regulated by Sab, the Btk-SH3 domain-binding protein

Tomoki Yamadori, Yoshihiro Baba, Masato Matsushita, Shoji Hashimoto, Mari Kurosaki, Tomohiro Kurosaki, Tadamitsu Kishimoto, Satoshi Tsukada

Research output: Contribution to journalArticle

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Abstract

Bruton's tyrosine kinase (Btk) is a cytoplasmic tyrosine kinase that is crucial for human and murine B cell development, and its deficiency causes human X-linked agammaglobulinemia and murine X-linked immunodeficiency. In this report, we describe the function of the Btk-binding protein Sab (SH3- domain binding protein that preferentially associates with Btk), which we reported previously as a newly identified Src homology 3 domain-binding protein. Sab was shown to inhibit the auto- and transphosphorylation activity of Btk, which prompted us to propose that Sab functions as a transregulator of Btk. Forced overexpression of Sab in B cells led to the reduction of B cell antigen receptor-induced tyrosine phosphorylation of Btk and significantly reduced both early and late B cell antigen receptor-mediated events, including calcium mobilization, inositol 1,4,5-trisphosphate production, and apoptotic cell death, where the involvement of Btk activity has been demonstrated previously. Together, these results indicate the negative regulatory role of Sab in the B cell cytoplasmic tyrosine kinase pathway.

Original languageEnglish
Pages (from-to)6341-6346
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number11
DOIs
Publication statusPublished - May 25 1999

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src Homology Domains
Carrier Proteins
B-Cell Antigen Receptors
B-Lymphocytes
Protein-Tyrosine Kinases
Inositol 1,4,5-Trisphosphate
Agammaglobulinaemia tyrosine kinase
Tyrosine
Cell Death
Phosphorylation
Calcium

All Science Journal Classification (ASJC) codes

  • General

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Bruton's tyrosine kinase activity is negatively regulated by Sab, the Btk-SH3 domain-binding protein. / Yamadori, Tomoki; Baba, Yoshihiro; Matsushita, Masato; Hashimoto, Shoji; Kurosaki, Mari; Kurosaki, Tomohiro; Kishimoto, Tadamitsu; Tsukada, Satoshi.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 11, 25.05.1999, p. 6341-6346.

Research output: Contribution to journalArticle

Yamadori, Tomoki ; Baba, Yoshihiro ; Matsushita, Masato ; Hashimoto, Shoji ; Kurosaki, Mari ; Kurosaki, Tomohiro ; Kishimoto, Tadamitsu ; Tsukada, Satoshi. / Bruton's tyrosine kinase activity is negatively regulated by Sab, the Btk-SH3 domain-binding protein. In: Proceedings of the National Academy of Sciences of the United States of America. 1999 ; Vol. 96, No. 11. pp. 6341-6346.
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AU - Hashimoto, Shoji

AU - Kurosaki, Mari

AU - Kurosaki, Tomohiro

AU - Kishimoto, Tadamitsu

AU - Tsukada, Satoshi

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AB - Bruton's tyrosine kinase (Btk) is a cytoplasmic tyrosine kinase that is crucial for human and murine B cell development, and its deficiency causes human X-linked agammaglobulinemia and murine X-linked immunodeficiency. In this report, we describe the function of the Btk-binding protein Sab (SH3- domain binding protein that preferentially associates with Btk), which we reported previously as a newly identified Src homology 3 domain-binding protein. Sab was shown to inhibit the auto- and transphosphorylation activity of Btk, which prompted us to propose that Sab functions as a transregulator of Btk. Forced overexpression of Sab in B cells led to the reduction of B cell antigen receptor-induced tyrosine phosphorylation of Btk and significantly reduced both early and late B cell antigen receptor-mediated events, including calcium mobilization, inositol 1,4,5-trisphosphate production, and apoptotic cell death, where the involvement of Btk activity has been demonstrated previously. Together, these results indicate the negative regulatory role of Sab in the B cell cytoplasmic tyrosine kinase pathway.

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