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Originally published In Press as doi:10.1074/jbc.C000838200 on January 31, 2001

J. Biol. Chem., Vol. 276, Issue 12, 8631-8634, March 23, 2001
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ACCELERATED PUBLICATION
BMK1 Mediates Growth Factor-induced Cell Proliferation through Direct Cellular Activation of Serum and Glucocorticoid-inducible Kinase*

Masaaki Hayashi, Richard I. Tapping, Ta-Hsiang Chao, Jeng-Fan Lo, Charles C. King, Young YangDagger , and Jiing-Dwan Lee§

From the Department of Immunology, The Scripps Research Institute, La Jolla, California 92037 and Dagger  the R. W. Johnson Pharmaceutical Research Institute, San Diego, California 92121

Activation of the mammalian mitogen-activated protein kinase known as BMK1 is required for growth factor-induced cell proliferation. To understand the mechanism by which BMK1 mediates this cellular response, this kinase was used as bait in a yeast two-hybrid-based library screening. Here, we report the identification of serum and glucocorticoid-inducible kinase (SGK) as a cellular protein that physically interacts with BMK1. During growth factor-induced cell stimulation, BMK1 activates SGK by phosphorylation at serine 78. This BMK1-mediated phosphorylation event is necessary for the activation of SGK and, more importantly, for cell proliferation induced by growth factors.


* This work was supported by Grant CA79871 from the National Institutes of Health and a grant from the American Heart Association. This publication was made possible by funds received from the Cancer Research Fund, under Interagency Agreement 97-12013 (University of California Contract 98-00924V) with the Department of Health Services, Cancer Research Program. Mention of trade name, proprietary product, or specific equipment does not constitute a guaranty or warranty by the Department of Health Services nor does it imply approval to the exclusion of other products. The views expressed herein represent those of the authors and do not necessarily represent the position of the State of California, Department of Health Services.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. E-mail: jdlee@scripps.edu.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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