Identification and Characterization of a Novel SH3-Domain Binding Protein, Sab, Which Preferentially Associates with Bruton's Tyrosine Kinase (Btk)

Autor: 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
Zdroj: Biochemical and Biophysical Research Communications; April 1998, Vol. 245 Issue: 2 p337-343, 7p
Abstrakt: 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.
Databáze: Supplemental Index