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Molecular Endocrinology 11 (9): 1353-1364
Copyright © 1997 by The Endocrine Society

Multiple Prolactin (PRL) Receptor Cytoplasmic Residues and Stat1 Mediate PRL Signaling to the Interferon Regulatory Factor-1 Promoter

Yu-fen Wang, Kevin D. O’Neal and Li-yuan Yu-Lee

Department of Medicine (Y.-f.W., L.-y.Y.-L.) Department of Microbiology and Immunology (K.D.O., L.-y.Y.-L.) Department of Cell Biology (L.-y.Y.-L.) Baylor College of Medicine Houston, Texas 77030

The Nb2 PRL receptor (PRL-R) is known to mediate PRL signaling to the interferon (IFN) regulatory factor-1 (IRF-1) gene via the family of signal transducers and activators of transcription or Stats. To analyze the components of the PRL-R/Stat/IRF-1 signaling pathway, various PRL-R, Stat, and IRF-1-CAT reporter constructs were transiently cotransfected into COS cells. First, mutations in the IFN{gamma}-activated sequence (GAS), either multimerized or in the context of the 1.7-kb IRF-1 promoter, failed to mediate a PRL response, showing that the IRF-1 GAS is a target of PRL signaling. Next, pairwise alanine substitutions into conserved residues in the proline-rich motif or Box 1 region and two tyrosine mutations, Y308F and Y382F, in the PRL-R intracellular domain all impaired PRL signaling to multimerized GAS or to the 1.7-kb IRF-1 promoter. Furthermore, these PRL-R mutants mediated reduced Stat1 binding to the IRF-1 GAS. Transfection of Stat1 further enhanced PRL signaling to the IRF-1 promoter, suggesting that Stat1 is a positive mediator of PRL action. These studies show that both membrane proximal and distal residues of the PRL-R are involved in signaling to the IRF-1 gene. Further, Stat1 and the GAS element are important for PRL activation of the IRF-1 gene.




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