ArticleThe Journal of biological chemistry2009
A progesterone receptor co-activator (JDP2) mediates activity through interaction with residues in the carboxyl-terminal extension of the DNA binding domain.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- Article
- JDP2, a Novel Molecular Key in Heart Failure and Atrial Fibrillation?International journal of molecular sciences · 2021Review
- PRMT1 Is Critical for the Transcriptional Activity and the Stability of the Progesterone Receptor.iScience · 2020Article
- Dynamic transcriptome, accessible genome, and PGR cistrome profiles in the human myometrium.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Genotoxic stress-triggered β-catenin/JDP2/PRMT5 complex facilitates reestablishing glutathione homeostasis.Nature communications · 2019Article
- Jun Dimerization Protein 2 Activates Mc2r Transcriptional Activity: Role of Phosphorylation and SUMOylation.International journal of molecular sciences · 2017Article
- Identification and characterization of BATF3 as a context-specific coactivator of the glucocorticoid receptor.PloS one · 2017Article
- Review
- Hic-5 is a transcription coregulator that acts before and/or after glucocorticoid receptor genome occupancy in a gene-selective manner.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Minireview: dynamic structures of nuclear hormone receptors: new promises and challenges.Molecular endocrinology (Baltimore, Md.) · 2014Review
- Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding.The Journal of biological chemistry · 2013Article
- Variable steroid receptor responses: Intrinsically disordered AF1 is the key.Molecular and cellular endocrinology · 2013Review
- Binding of the N-terminal region of coactivator TIF2 to the intrinsically disordered AF1 domain of the glucocorticoid receptor is accompanied by conformational reorganizations.The Journal of biological chemistry · 2012Article
- Progesterone receptors, their isoforms and progesterone regulated transcription.Molecular and cellular endocrinology · 2012Review
- Allosteric modulators of steroid hormone receptors: structural dynamics and gene regulation.Endocrine reviews · 2012Review
- The road less traveled: new views of steroid receptor action from the path of dose-response curves.Molecular and cellular endocrinology · 2012Review
- Structural and functional analysis of domains of the progesterone receptor.Molecular and cellular endocrinology · 2012Review
- Roles of intrinsic disorder in protein-nucleic acid interactions.Molecular bioSystems · 2012Review
- Expanding the proteome: disordered and alternatively folded proteins.Quarterly reviews of biophysics · 2011Article
- Ligand binding domain mutations of the glucocorticoid receptor selectively modify the effects with, but not binding of, cofactors.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Progesterone receptor (PR) belongs to the nuclear receptor family of ligand-dependent transcription factors and mediates the major biological effects of progesterone. Transcriptional co-activators that are recruited by PR through the carboxyl-terminal ligand binding domain have been studied extensively. Much less is known about co-activators that interact with other regions of receptors. Jun dimerization protein 2 (JDP2) is a PR co-activator that enhances the transcriptional activity of the amino-terminal domain by increasing the alpha-helical content and stability of the intrinsically disordered amino-terminal domain. To gain insights into the mechanism of JDP2 co-activation of PR, the structural basis of JDP2-PR interaction was analyzed using NMR. The smallest regions of each protein needed for efficient protein interaction were used for NMR and included the basic region plus leucine zipper (bZIP) domain of JDP2 and the core zinc modules of the PR DNA binding domain plus the intrinsically disordered carboxyl-terminal extension (CTE) of the DNA binding domain. Chemical shift changes in PR upon titration with JDP2 revealed that most of the residues involved in binding of JDP2 reside within the CTE. The importance of the CTE for binding JDP2 was confirmed by peptide competition and mutational analyses. Point mutations within CTE sites identified by NMR and a CTE domain swapping experiment also confirmed the functional importance of JDP2 interaction with the CTE for enhancement of PR transcriptional activity. These studies provide insights into the role and functional importance of the CTE for co-activator interactions.
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