2. Academic Validation
  3. Identification and characterization of a novel SH3-domain binding protein, Sab, which preferentially associates with Bruton's tyrosine kinase (BtK)

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

  • Biochem Biophys Res Commun. 1998 Apr 17;245(2):337-43. doi: 10.1006/bbrc.1998.8420.
M Matsushita 1,  T Yamadori,  S Kato,  Y Takemoto,  J Inazawa,  Y Baba,  S Hashimoto,  S Sekine,  S Arai,  T Kunikata,  M Kurimoto,  T Kishimoto,  S Tsukada
Affiliations

Affiliation

  • 1 Department of Medicine III, Osaka University Medical School, Japan.
PMID: 9571151 DOI: 10.1006/bbrc.1998.8420
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.

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