Identification of myosin II as a binding protein to the PH domain of protein kinase B

Motonari Tanaka, Hiroaki Konishi, Kazushige Touhara, Fumio Sakane, Masato Hirata, Yoshitaka Ono, Ushio Kikkawa

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23 Citations (Scopus)

Abstract

Myosin II was identified as a binding protein to the pleckstrin homology (PH) domain of protein kinase B (PKB) in CHO cell extract by using the glutathione S-transferase-fusion protein as a probe. When myosin II purified from rabbit skeletal muscle was employed, myosin II was shown to bind almost exclusively to the PH domain of PKB among the PH domain fusion proteins examined. The purified myosin II bound to the PH domain of PKB with a K(d) value of 1.1 x 10-7 M. Studies with a series of truncated molecules indicated that the whole structure of the PH domain is required for the binding of myosin II, and the binding to the PH domain was inhibited by phosphatidylinositol 4,5-bisphosphate. These results suggest that myosin II is a specific binding protein to the PH domain of particular proteins including PKB.

Original languageEnglish
Pages (from-to)169-174
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume255
Issue number1
DOIs
Publication statusPublished - Feb 5 1999

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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