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Originally published In Press as doi:10.1074/jbc.M001970200 on April 6, 2000

J. Biol. Chem., Vol. 275, Issue 23, 17476-17480, June 9, 2000
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Identification of the Functional Domain in the Transcription Factor RTEF-1 That Mediates alpha 1-Adrenergic Signaling in Hypertrophied Cardiac Myocytes*

Takahisa UeyamaDagger , Chongxue Zhu, Yunuen M. Valenzuela§, Joseph G. Suzow, and Alexandre F. R. Stewart

From the Cardiovascular Institute, School of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania 15213

Cardiac myocytes respond to alpha 1-adrenergic receptor stimulation by a progressive hypertrophy accompanied by the activation of many fetal genes, including skeletal muscle alpha -actin. The skeletal muscle alpha -actin gene is activated by signaling through an MCAT element, the binding site of the transcription enhancer factor-1 (TEF-1) family of transcription factors. Previously, we showed that overexpression of the TEF-1-related factor (RTEF-1) increased the alpha 1-adrenergic response of the skeletal muscle alpha -actin promoter, whereas TEF-1 overexpression did not. Here, we identified the functional domains and specific sequences in RTEF-1 that mediate the alpha 1-adrenergic response. Chimeric TEF-1 and RTEF-1 expression constructs localized the region responsible for the alpha 1-adrenergic response to the carboxyl-terminal domain of RTEF-1. Site-directed mutagenesis was used to inactivate eight serine residues of RTEF-1, not present in TEF-1, that are putative targets of alpha 1-adrenergic-dependent kinases. Mutation of a single serine residue, Ser-322, reduced the alpha 1-adrenergic activation of RTEF-1 by 70% without affecting protein stability, suggesting that phosphorylation at this serine residue accounts for most of the alpha 1-adrenergic response. Thus, these results demonstrate that RTEF-1 is a direct target of alpha 1-adrenergic signaling in hypertrophied cardiac myocytes.

* 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 Supported by a postdoctoral fellowship of the Pennsylvania affiliate of the American Heart Association.

§ Supported by a minority undergraduate research supplement to National Institutes of Health Grant R29 HL57211.

Supported by a grant-in-aid from the American Heart Association and by National Institutes of Health Grant R29 HL57211. To whom correspondence should be addressed: Cardiovascular Inst., School of Medicine, University of Pittsburgh, BST 1704.3, 200 Lothrop St., Pittsburgh, PA 15213. Tel.: 412-383-9761; Fax: 412-383-8997; E-mail: stewartaf@msx.upmc.edu.

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