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

Research output: Contribution to journalArticle

74 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)333-339
Number of pages7
JournalBiochemical and biophysical research communications
Volume236
Issue number2
DOIs
Publication statusPublished - 1997 Jul 18
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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