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Originally published In Press as doi:10.1074/jbc.M006819200 on August 7, 2000

J. Biol. Chem., Vol. 275, Issue 43, 33365-33372, October 27, 2000
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cAMP Response Element-binding Protein-binding Protein Mediates Thyrotropin-releasing Hormone Signaling on Thyrotropin Subunit Genes*

Koshi HashimotoDagger , Kerstin Zanger§, Anthony N. HollenbergDagger , Laurie E. Cohen§, Sally Radovick§, and Fredric E. WondisfordDagger

From the Dagger  Thyroid Unit, Division of Endocrinology, Beth Israel Deaconess Medical Center and § Children's Hospital, Harvard Medical School, Boston, Massachusetts 02215

Transcription of pituitary alpha -glycoprotein hormone subunit (alpha -GSU) and thyrotropin beta  subunit (TSH-beta ) genes is stimulated by thyrotropin-releasing hormone (TRH). Since cAMP response element-binding protein (CREB)-binding protein (CBP) integrates a number of cell signaling pathways, we investigated whether CBP is important for TRH stimulation of the TSH subunit genes. Cotransfection of E1A in GH3 cells completely blocked TRH stimulation of the TSH subunit genes, suggesting that CBP is a key factor for TRH signaling in the pituitary. CBP and Pit-1 acted synergistically in TRH stimulation of the TSH-beta promoter, and amino acids 1-450 of CBP were sufficient for the TRH effect. In contrast, on the human alpha -GSU promoter, CREB and P-Lim mediated TRH signaling. Intriguingly, CREB was phosphorylated upon TRH stimulation, leading to CBP recruitment to the alpha -GSU promoter. CBP also interacted with P-Lim in a TRH-dependent manner, suggesting that P-Lim is an important factor for non-cAMP response element-mediated TRH stimulation of this promoter. Distinct domains of CBP were required for TRH signaling by CREB and P-Lim on the alpha -GSU promoter, amino acids 450-700 and 1-450, respectively. Thus, the amino terminus of CBP plays a critical role in TRH signaling in the anterior pituitary via both Pit-1-dependent and -independent pathways, yielding differential regulation of pituitary gene products.

* This work was supported by grants from the National Institutes of Health (to L. E. C., S. R., and F. E. W.).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: Dept. of Medicine, Section of Endocrinology, University of Chicago, 5841 South Maryland Ave., Chicago, IL 60637. Tel.: 773-702-6217; Fax: 773-834-0486; E-mail: fwondisf@medicine.bsd.uchicago.edu.

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