Article
HMGN2 inducibly binds a novel transactivation domain in nuclear PRLr to coordinate Stat5a-mediated transcription.
Molecular endocrinology (Baltimore, Md.) - 1 Sept 2011
Fiorillo Alyson A, Medler Terry R, Feeney Yvonne B, Liu Yi, Tommerdahl Kalie L, Clevenger Charles V
Abstract excerpt
The direct actions of transmembrane receptors within the nucleus remain enigmatic. In this report, we demonstrate that the prolactin receptor (PRLr) localizes to the nucleus where it functions as a coactivator through its interactions with the latent transcription factor signal transducer and activator of transcription 5a (Stat5a) and the high-mobility group N2 protein (HMGN2). We identify a novel transactivation...
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