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Originally published In Press as doi:10.1074/jbc.M206210200 on July 29, 2002

J. Biol. Chem., Vol. 277, Issue 40, 36955-36961, October 4, 2002
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A-Kinase Anchoring Protein AKAP220 Binds to Glycogen Synthase Kinase-3beta (GSK-3beta ) and Mediates Protein Kinase A-dependent Inhibition of GSK-3beta *

Chie TanjiDagger §, Hideki YamamotoDagger , Noriaki Yorioka§, Nobuoki Kohno§, Kunimi Kikuchi, and Akira KikuchiDagger ||

From the Departments of Dagger  Biochemistry and § Molecular and Internal Medicine, Graduate School of Biomedical Sciences, Hiroshima University, 1-2-3, Kasumi, Minami-ku, Hiroshima 734-8551, Japan and the  Division of Biochemical Oncology and Immunology, Institute for Genetic Medicine, Hokkaido University, Kita-15, Nichi-7, Kita-ku, Sapporo 060-0815, Japan

Glycogen synthase kinase-3 (GSK-3) is regulated by various extracellular ligands and phosphorylates many substrates, thereby regulating cellular functions. Using yeast two-hybrid screening, we found that GSK-3beta binds to AKAP220, which is known to act as an A-kinase anchoring protein. GSK-3beta formed a complex with AKAP220 in intact cells at the endogenous level. Cyclic AMP-dependent protein kinase (PKA) and type 1 protein phosphatase (PP1) were also detected in this complex, suggesting that AKAP220, GSK-3beta , PKA, and PP1 form a quaternary complex. It has been reported that PKA phosphorylates GSK-3beta , thereby decreasing its activity. When COS cells were treated with dibutyryl cyclic AMP to activate PKA, the activity of GSK-3beta bound to AKAP220 decreased more markedly than the total GSK-3beta activity. Calyculin A, a protein phosphatase inhibitor, also inhibited the activity of GSK-3beta bound to AKAP220 more strongly than the total GSK-3beta activity. These results suggest that PKA and PP1 regulate the activity of GSK-3beta efficiently by forming a complex with AKAP220.

* This work was supported by grants-in-aid for scientific research (B) and for scientific research on priority areas (C) from the Ministry of Education, Science, and Culture, Japan and by grants from the Yamanouchi Foundation for Research on Metabolic Disorders.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Dept. of Biochemistry, Graduate School of Biomedical Sciences, Hiroshima University, 1-2-3, Kasumi, Minami-ku, Hiroshima 734-8551, Japan. Tel.: 81-82-257-5130; Fax: 81-82-257-5134; E-mail: akikuchi@hiroshima-u.ac.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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