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 | |
| Publication status | Published - Apr 17 1998 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
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
}
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 -