Characterization of the pleckstrin homology domain of Btk as an inositol polyphosphate and phosphoinositide binding domain

Toshio Kojima, Mitsunori Fukuda, Yutaka Watanabe, Fumiaki Hamazato, Katsuhiko Mikoshiba

研究成果: Article査読

74 被引用数 (Scopus)

抄録

We previously reported that the pleckstrin homology (PH) domain of Bruton's tyrosine kinase (Btk) binds Ins(1,3,4,5)P4 and that missense mutations in this domain which cause either human X-linked agammaglo-bulinemia (XLA) or murine X-Linked immunodeficiency (Xid) also dramatically reduce the Ins(1,3,4,5)P4 binding activity. In this paper, we describe the inositol phosphate binding specificity of the Btk PH domain and different inositol polyphosphate binding properties among the PH domains of Tec family kinases. Our results suggest that certain inositol phosphates and/or phosphoinositides are physiological ligands of some Tec family kinases and that Tec family members are differently regulated by inositol molecules.

本文言語English
ページ(範囲)333-339
ページ数7
ジャーナルBiochemical and biophysical research communications
236
2
DOI
出版ステータスPublished - 1997 7 18
外部発表はい

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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