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

Masato Matsushita; Tomoki Yamadori; Seishi Kato; Yoshihiro Takemoto; Jouji Inazawa; Yoshihiro Baba; Shoji Hashimoto; Shingo Sekine; Shigeyuki Arai; Toshio Kunikata; Masashi Kurimoto; Tadamitsu Kishimoto; Satoshi Tsukada

doi:10.1006/bbrc.1998.8420

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

Masato Matsushita, Tomoki Yamadori, Seishi Kato, Yoshihiro Takemoto, Jouji Inazawa, Yoshihiro Baba, Shoji Hashimoto, Shingo Sekine, Shigeyuki Arai, Toshio Kunikata, Masashi Kurimoto, Tadamitsu Kishimoto, Satoshi Tsukada

Research output: Contribution to journal › Article › peer-review

41 Citations (Scopus)

Abstract

Protein interaction cloning method was used to identify a novel molecule, Sab, which binds to the SH3 domain of Bruton'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.

Original language	English
Pages (from-to)	337-343
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	245
Issue number	2
DOIs	https://doi.org/10.1006/bbrc.1998.8420
Publication status	Published - Apr 17 1998
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1006/bbrc.1998.8420

Fingerprint Dive into the research topics of 'Identification and characterization of a novel SH3-domain binding protein, Sab, which preferentially associates with Bruton's tyrosine kinase (Btk)'. Together they form a unique fingerprint.

Cite this

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. (1998). Identification and characterization of a novel SH3-domain binding protein, Sab, which preferentially associates with Bruton's tyrosine kinase (Btk). Biochemical and Biophysical Research Communications, 245(2), 337-343. https://doi.org/10.1006/bbrc.1998.8420

Identification and characterization of a novel SH3-domain binding protein, Sab, which preferentially associates with Bruton's tyrosine kinase (Btk). / Matsushita, Masato; Yamadori, Tomoki; Kato, Seishi; Takemoto, Yoshihiro; Inazawa, Jouji; Baba, Yoshihiro; Hashimoto, Shoji; Sekine, Shingo; Arai, Shigeyuki; Kunikata, Toshio; Kurimoto, Masashi; Kishimoto, Tadamitsu; Tsukada, Satoshi.

In: Biochemical and Biophysical Research Communications, Vol. 245, No. 2, 17.04.1998, p. 337-343.

Research output: Contribution to journal › Article › peer-review

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 1998, 'Identification and characterization of a novel SH3-domain binding protein, Sab, which preferentially associates with Bruton's tyrosine kinase (Btk)', Biochemical and Biophysical Research Communications, vol. 245, no. 2, pp. 337-343. https://doi.org/10.1006/bbrc.1998.8420

Matsushita, Masato ; Yamadori, Tomoki ; Kato, Seishi ; Takemoto, Yoshihiro ; Inazawa, Jouji ; Baba, Yoshihiro ; Hashimoto, Shoji ; Sekine, Shingo ; Arai, Shigeyuki ; Kunikata, Toshio ; Kurimoto, Masashi ; Kishimoto, Tadamitsu ; Tsukada, Satoshi. / Identification and characterization of a novel SH3-domain binding protein, Sab, which preferentially associates with Bruton's tyrosine kinase (Btk). In: Biochemical and Biophysical Research Communications. 1998 ; Vol. 245, No. 2. pp. 337-343.

@article{bf487b250f47409390fce3051360a0dd,

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

abstract = "Protein interaction cloning method was used to identify a novel molecule, Sab, which binds to the SH3 domain of Bruton'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.",

author = "Masato Matsushita and Tomoki Yamadori and Seishi Kato and Yoshihiro Takemoto and Jouji Inazawa and Yoshihiro Baba and Shoji Hashimoto and Shingo Sekine and Shigeyuki Arai and Toshio Kunikata and Masashi Kurimoto and Tadamitsu Kishimoto and Satoshi Tsukada",

year = "1998",

month = apr,

day = "17",

doi = "10.1006/bbrc.1998.8420",

language = "English",

volume = "245",

pages = "337--343",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

T1 - Identification and characterization of a novel SH3-domain binding protein, Sab, which preferentially associates with Bruton's tyrosine kinase (Btk)

AU - Matsushita, Masato

AU - Yamadori, Tomoki

AU - Kato, Seishi

AU - Takemoto, Yoshihiro

AU - Inazawa, Jouji

AU - Baba, Yoshihiro

AU - Hashimoto, Shoji

AU - Sekine, Shingo

AU - Arai, Shigeyuki

AU - Kunikata, Toshio

AU - Kurimoto, Masashi

AU - Kishimoto, Tadamitsu

AU - Tsukada, Satoshi

PY - 1998/4/17

Y1 - 1998/4/17

N2 - Protein interaction cloning method was used to identify a novel molecule, Sab, which binds to the SH3 domain of Bruton'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.

AB - Protein interaction cloning method was used to identify a novel molecule, Sab, which binds to the SH3 domain of Bruton'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.

UR - http://www.scopus.com/inward/record.url?scp=0032540094&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032540094&partnerID=8YFLogxK

U2 - 10.1006/bbrc.1998.8420

DO - 10.1006/bbrc.1998.8420

M3 - Article

C2 - 9571151

AN - SCOPUS:0032540094

VL - 245

SP - 337

EP - 343

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -