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Originally published In Press as doi:10.1074/jbc.M002560200 on September 11, 2000

J. Biol. Chem., Vol. 275, Issue 48, 38032-38039, December 1, 2000
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Thyroxine Promotes Association of Mitogen-activated Protein Kinase and Nuclear Thyroid Hormone Receptor (TR) and Causes Serine Phosphorylation of TR*

Paul J. DavisDagger §, Ai ShihDagger , Hung-Yun LinDagger , Leon J. Martino§, and Faith B. DavisDagger §

From the Dagger  Samuel S. Stratton Veterans Affairs Medical Center and the § Molecular and Cellular Medicine Program, Department of Medicine and the Center for Cell Biology and Cancer Research, Albany Medical College, Albany, New York 12208

Activated nongenomically by L-thyroxine (T4), mitogen-activated protein kinase (MAPK) complexed in 10-20 min with endogenous nuclear thyroid hormone receptor (TRbeta 1 or TR) in nuclear fractions of 293T cells, resulting in serine phosphorylation of TR. Treatment of cells with the MAPK kinase inhibitor, PD 98059, prevented both T4-induced nuclear MAPK-TR co-immunoprecipitation and serine phosphorylation of TR. T4 treatment caused dissociation of TR and SMRT (silencing mediator of retinoid and thyroid hormone receptor), an effect also inhibited by PD 98059 and presumptively a result of association of nuclear MAPK with TR. Transfection into CV-1 cells of TR gene constructs in which one or both zinc fingers in the TR DNA-binding domain were replaced with those from the glucocorticoid receptor localized the site of TR phosphorylation by T4-activated MAPK to a serine in the second zinc finger of the TR DNA-binding domain. In an in vitro cell- and hormone-free system, purified activated MAPK phosphorylated recombinant human TRbeta 1 (). Thus, T4 activates MAPK and causes MAPK-mediated serine phosphorylation of TRbeta 1 and dissociation of TR and the co-repressor SMRT.

* This work was supported in part by funds from the Office of Research Development, Medical Research Service, Department of Veterans Affairs (to P. J. D.) and by a grant from the Candace King Weir Foundation.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 all correspondence should be addressed: Dept. of Medicine, MC-16, Albany Medical College, Albany, NY 12208. Tel.: 518-262-6138; Fax: 518-262-5008; E-mail: pjdavis@albany.net.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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