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• W2146166352 abstract "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 domain within the PRLr that is activated by ligand-induced phosphorylation, an event coupled to HMGN2 binding. The association of the PRLr with HMGN2 enables Stat5a-responsive promoter binding, thus facilitating transcriptional activation and promoting anchorage-independent growth. We propose that HMGN2 serves as a critical regulatory factor in Stat5a-driven gene expression by facilitating the assembly of PRLr/Stat5a onto chromatin and that these events may serve to promote biological events that contribute to a tumorigenic phenotype. Our data imply that phosphorylation may be the molecular switch that activates a cell surface receptor transactivation domain, enabling it to tether chromatin-modifying factors, such as HMGN2, to target promoter regions in a sequence-specific manner." @default.
• W2146166352 created "2016-06-24" @default.
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• W2146166352 date "2011-09-01" @default.
• W2146166352 modified "2023-10-18" @default.
• W2146166352 title "HMGN2 Inducibly Binds a Novel Transactivation Domain in Nuclear PRLr to Coordinate Stat5a-Mediated Transcription" @default.
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• W2146166352 doi "https://doi.org/10.1210/me.2011-0106" @default.
• W2146166352 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5417234" @default.
• W2146166352 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21816901" @default.
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