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J Biol Chem, Vol. 275, Issue 5, 3100-3106, February 4, 2000

The Pit-1 Homeodomain and beta -Domain Interact with Ets-1 and Modulate Synergistic Activation of the Rat Prolactin Promoter*

Andrew P. BradfordDagger §, Kelley S. Brodskypar , Scott E. Diamondpar , Laura C. Kuhn, Yingmiao Liu**, and Arthur Gutierrez-Hartmann§par **

From the Departments of Dagger  Obstetrics and Gynecology, § Biochemistry and Molecular Genetics, and par  Medicine, and ** Program in Molecular Biology, University of Colorado Health Sciences Center, Denver, Colorado 80262

Pit-1/GHF-1 is a pituitary-specific, POU homeodomain transcription factor required for development of somatotroph, lactotroph, and thyrotroph cell lineages and regulation of the temporal and spatial expression of the growth hormone, prolactin (PRL), and thyrotropin-beta genes. Synergistic interaction of Pit-1 with a member of the Ets family of transcription factors, Ets-1, has been shown to be an important mechanism regulating basal and Ras-induced lactotroph-specific rat (r) PRL promoter activity. Pit-1beta /GHF-2, an alternatively spliced isoform containing a 26-amino acid insert (beta -domain) within its transcription-activation domain, physically interacts with Ets-1 but fails to synergize. By using a series of Pit-1 internal-deletion constructs in a transient transfection protocol to reconstitute rPRL promoter activity in HeLa cells, we have determined that the functional and physical interaction of Pit-1 and Ets-1 is mediated via the POU homeodomain, which is common to both Pit-1 and Pit-1beta . Although the Pit-1 homeodomain is both necessary and sufficient for direct binding to Ets-1 in a DNA-independent manner, an additional interaction surface was mapped to the beta -domain, specific to the Pit-1beta isoform. Thus, the unique transcriptional properties of Pit-1 and Pit-1beta on the rPRL promoter may be due to the formation of functionally distinct complexes of these two Pit-1 isoforms with Ets-1.

* This work was supported by National Institutes of Health Grants DK 46868 (to A. G.-H.) and DK 53496 (to A. P. B.).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 Obstetrics and Gynecology, University of Colorado Health Sciences Center, 4200 East Ninth Ave., B-198, Denver, CO 80262. Tel.: 303-315-4146; Fax: 303-315-8889; E-mail: Andy.Bradford@uchsc.edu.

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