ArticleMolecular endocrinology (Baltimore, Md.)2011
HMGN2 inducibly binds a novel transactivation domain in nuclear PRLr to coordinate Stat5a-mediated transcription.
Article in Molecular endocrinology (Baltimore, Md.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- HMGN2 accelerates the proliferation and cell cycle progression of glioblastoma by regulating CDC20 expression.Genes & diseases · 2025Article
- Deficiency of HMGN2 enhances antibacterial activity of macrophages by promoting H3 histone modification-mediated CD14/iNOS expression.Frontiers in immunology · 2025Article
- The growth hormone receptor interacts with transcriptional regulator HMGN1 upon GH-induced nuclear translocation.Journal of cell communication and signaling · 2023Article
- Serine residues 726 and 780 have nonredundant roles regulating STAT5a activity in luminal breast cancer.Scientific reports · 2021Article
- Exogenous HMGN2 inhibits the migration and invasion of osteosarcoma cell lines.Translational cancer research · 2020Article
- Increased expression of high-mobility group nucleosomal-binding domain 2 protein in various tumor cell lines.Oncology letters · 2018Article
- Histone H1 and Chromosomal Protein HMGN2 Regulate Prolactin-induced STAT5 Transcription Factor Recruitment and Function in Breast Cancer Cells.The Journal of biological chemistry · 2017Article
- HDAC6 Deacetylates HMGN2 to Regulate Stat5a Activity and Breast Cancer Growth.Molecular cancer research : MCR · 2016Article
- The modulation of MiR-155 and MiR-23a manipulates Klebsiella pneumoniae Adhesion on Human pulmonary Epithelial cells via Integrin α5β1 Signaling.Scientific reports · 2016Article
- The prolactin receptor transactivation domain is associated with steroid hormone receptor expression and malignant progression of breast cancer.The American journal of pathology · 2013Article
- Landscape of EGFR signaling network in human cancers: biology and therapeutic response in relation to receptor subcellular locations.Cancer letters · 2012Review
- The nucleosome binding protein HMGN1 interacts with PCNA and facilitates its binding to chromatin.Molecular and cellular biology · 2012Article
- Nuclear functions and subcellular trafficking mechanisms of the epidermal growth factor receptor family.Cell & bioscience · 2012Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.