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A L Ferry Department of Physiology, University of Kentucky College of Medicine, Lexington, Kentucky 40536, USA
Departments of Medicine and of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA

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D M Locasto Department of Physiology, University of Kentucky College of Medicine, Lexington, Kentucky 40536, USA
Departments of Medicine and of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA

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L B Meszaros Department of Physiology, University of Kentucky College of Medicine, Lexington, Kentucky 40536, USA
Departments of Medicine and of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA

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J C Bailey Department of Physiology, University of Kentucky College of Medicine, Lexington, Kentucky 40536, USA
Departments of Medicine and of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA

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M D Jonsen Department of Physiology, University of Kentucky College of Medicine, Lexington, Kentucky 40536, USA
Departments of Medicine and of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA

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K Brodsky Department of Physiology, University of Kentucky College of Medicine, Lexington, Kentucky 40536, USA
Departments of Medicine and of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA

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C J Hoon Department of Physiology, University of Kentucky College of Medicine, Lexington, Kentucky 40536, USA
Departments of Medicine and of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA

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A Gutierrez-Hartmann Department of Physiology, University of Kentucky College of Medicine, Lexington, Kentucky 40536, USA
Departments of Medicine and of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA

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S E Diamond Department of Physiology, University of Kentucky College of Medicine, Lexington, Kentucky 40536, USA
Departments of Medicine and of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center, Denver, Colorado 80262, USA

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Many transcription factors are expressed as multiple isoforms with distinct effects on the regulation of gene expression, and the functional consequences of structural differences between transcription factor isoforms may allow for precise control of gene expression. The pituitary transcription factor isoforms Pit-1 and Pit-1β differentially regulate anterior pituitary hormone gene expression. Pit-1 is required for the development of and appropriate hormone expression by anterior pituitary somatotrophs and lactotrophs. Pit-1β differs structurally from Pit-1 by the splice-insertion of the 26-residue β-domain in the trans-activation domain, and it differs functionally from Pit-1 in that it represses expression of the prolactin promoter in a cell-type specific manner. In order to identify signal and promoter context requirements for repression by Pit-1β, we examined its function in the presence of physiological regulatory signals as well as wild-type and mutant Pit-1-dependent target promoters. Here, we demonstrate that Pit-1β impairs recruitment of cAMP response element-binding protein (CREB)-binding protein to the promoters that it represses. In addition, we show that repression of target promoter activity, reduction in promoter histone acetylation, and decrease of CREB-binding protein recruitment all depend on promoter context. These findings provide a mechanism for promoter-specific repression by Pit-1β.

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