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Papers In Press, published online ahead of print March 26, 2001
Center for Ligand and Transcription, Chonnam National University, Kwangju 500-757
Corresponding Author: jlee{at}chonnam.chonnam.ac.kr
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-kappaB (NFkB) component p65 both in vitro and in vivo. The phosphorylation of p65 by CaMKIV resulted in recruitment of transcription coactivator CREB-binding protein and concomitant release of corepressor silencing mediator for retinoid and thyroid hormone receptors (SMRT), as demonstrated by the glutathione S-transferase pull down and mammalian two hybrid assays. In addition, cotransfection of CaMKIV resulted in cytosolic translocation of SMRT. Consistent with these results, cotransfected CaMKIV dramatically stimulated the NFkB transactivation in mammalian cells. From these results, NFkB is suggested to be a novel downstream effector molecule of CaMKIV.
J. Biol. Chem, 10.1074/jbc.M010211200
Submitted on November 9, 2000
Revised on March 26, 2001
Accepted on March 26, 2001
Ca2+/calmodulin-dependent protein kinase IV stimulates nuclear factor-
B transactivation via phosphorylation of the p65 subunit
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