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
N1 - Funding Information:
We thank Drs. Shigekazu Nagata, Hiroaki Miki, Stuart L. Schreiber, Sibo Feng, Joan S. Brugge, Terukatsu Sasaki, Michiyuki Matsuda for providing materials, and Ms. Noriko Kameoka for preparation of the manuscript. This work was supported by grants from the Ministry of Education, Science and Culture of Japan (to T.K. and S.T.), and the Ministry of Health and Welfare of Japan (to S.T.).
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 -