JBC Ideal method for primary cell transfection

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Originally published In Press as doi:10.1074/jbc.M010211200 on March 26, 2001

J. Biol. Chem., Vol. 276, Issue 23, 20005-20010, June 8, 2001
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Ca2+/Calmodulin-dependent Protein Kinase IV Stimulates Nuclear Factor-kappa B Transactivation via Phosphorylation of the p65 Subunit*

Moon Kyoo JangDagger , Young Hwa GooDagger , Young Chang Sohn, Yun Sung Kim, Soo-Kyung Lee§, Heonjoong Kang, JaeHun Cheong, and Jae Woon Lee||

From the Center for Ligand and Transcription, Chonnam National University, Kwangju 500-757 and the  School of Earth and Environmental Sciences, Seoul National University, Seoul 151-742, Korea

Calmodulin-dependent protein kinase IV (CaMKIV) is a key mediator of Ca2+-induced gene expression. In this study, CaMKIV was found to directly associate with and phosphorylate the nuclear factor-kappa B (NFkappa B) component p65 both in vitro and in vivo. The phosphorylation of p65 by CaMKIV resulted in recruitment of transcription coactivator cAMP-response element-binding protein-binding protein and concomitant release of corepressor silencing mediator for retinoid and thyroid hormone receptors, as demonstrated by the glutathione S-transferase pull down and mammalian two hybrid assays. In addition, cotransfection of CaMKIV resulted in cytosolic translocation of the silencing mediator for retinoid and thyroid hormone receptors. Consistent with these results, cotransfected CaMKIV dramatically stimulated the NFkappa B transactivation in mammalian cells. From these results, NFkappa B is suggested to be a novel downstream effector molecule of CaMKIV.

* This work was exclusively supported by a grant from the National Creative Research Initiatives Program of the Korean Ministry of Science and Technology, Republic of Korea.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.

Dagger Contributed equally.

§ Present address: Salk Inst., San Diego, CA 92185.

|| To whom correspondence should be addressed. Tel.: 82-62-530-0910; Fax: 82-62-530-0772; E-mail: jlee@chonnam.chonnam.ac.kr.

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


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