TY - JOUR
T1 - Identification of myosin II as a binding protein to the PH domain of protein kinase B
AU - Tanaka, Motonari
AU - Konishi, Hiroaki
AU - Touhara, Kazushige
AU - Sakane, Fumio
AU - Hirata, Masato
AU - Ono, Yoshitaka
AU - Kikkawa, Ushio
N1 - Funding Information:
We thank Dr. Y. Nishizuka for discussions, Dr. T. Inazu for the GST-fusion protein expression plasmid of the PH domain of pleck-strin, and Ms. Y. Kimura for secretarial assistance. This study was supported in part by research grants from the Scientific Research Funds of the Ministry of Education, Science, Sports, and Culture of Japan; the Suntory Institute for Bioorganic Research; and the Charitable Trust Osaka Cancer Researcher Fund.
PY - 1999/2/5
Y1 - 1999/2/5
N2 - 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.
AB - 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.
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U2 - 10.1006/bbrc.1999.0162
DO - 10.1006/bbrc.1999.0162
M3 - Article
C2 - 10082674
AN - SCOPUS:0033525161
SN - 0006-291X
VL - 255
SP - 169
EP - 174
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -