ArticleThe Journal of biological chemistry2009
Mechanisms underlying the control of progesterone receptor transcriptional activity by SUMOylation.
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 22 papers.
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Who cites it
22 citing papers in PubMed, 46 citations in OpenAlex.
- Review
- Split Decisions in Hormone Signaling: Distinct Roles for Progesterone Receptor Isoforms in Breast Cancer Biology.Endocrinology · 2025Review
- The transcriptional activity of progestins used in contraception and menopausal hormone therapy via progesterone receptor A is dependent on the density of the receptor.Biochemical and biophysical research communications · 2023Article
- Review
- Characterisation of progestins used in hormonal contraception and progesterone via the progesterone receptor.Biochemical and biophysical research communications · 2020Article
- FGFs/FGFRs-dependent signalling in regulation of steroid hormone receptors - implications for therapy of luminal breast cancer.Journal of experimental & clinical cancer research : CR · 2019Review
- SUMOylation Regulates Transcription by the Progesterone Receptor A Isoform in a Target Gene Selective Manner.Diseases (Basel, Switzerland) · 2018Article
- An Approach to Greater Specificity for Glucocorticoids.Frontiers in endocrinology · 2018Review
- The transcriptional repressor GATAD2B mediates progesterone receptor suppression of myometrial contractile gene expression.The Journal of biological chemistry · 2017Article
- Active FOXO1 Is a Key Determinant of Isoform-Specific Progesterone Receptor Transactivation and Senescence Programming.Molecular cancer research : MCR · 2016Article
- Progesterone action in breast, uterine, and ovarian cancers.Journal of molecular endocrinology · 2015Review
- Post-translational modifications of the progesterone receptors.The Journal of steroid biochemistry and molecular biology · 2014Review
- Lysine methylation of progesterone receptor at activation function 1 regulates both ligand-independent activity and ligand sensitivity of the receptor.The Journal of biological chemistry · 2014Article
- Progesterone receptor signaling in the initiation of pregnancy and preservation of a healthy uterus.The International journal of developmental biology · 2014Review
- Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding.The Journal of biological chemistry · 2013Article
- PIASγ enhanced SUMO-2 modification of Nurr1 activation-function-1 domain limits Nurr1 transcriptional synergy.PloS one · 2013Article
- Control of progesterone receptor transcriptional synergy by SUMOylation and deSUMOylation.BMC molecular biology · 2012Article
- Structural and functional analysis of domains of the progesterone receptor.Molecular and cellular endocrinology · 2012Review
- Differential and interactive effects of ligand-bound progesterone receptor A and B isoforms on tyrosine hydroxylase promoter activity.Journal of neuroendocrinology · 2011Article
- Progesterone: the ultimate endometrial tumor suppressor.Trends in endocrinology and metabolism: TEM · 2011Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Posttranslational modification by small ubiquitin-like modifier (SUMO) is a major regulator of transcription. We previously showed that progesterone receptors (PR) have a single consensus psiKXE SUMO-conjugation motif centered at Lys-388 in the N-terminal domain of PR-B and a homologous site of PR-A. SUMOylation of the PR is hormone-dependent and has a suppressive effect on transcription of an exogenous promoter. Here we show that repression of PR activity by SUMOylation at Lys-388 is uncoupled from phosphorylation, involves synergy between tandem progesterone response elements, and is associated with lowered ligand sensitivity and slowed ligand-dependent down-regulation. However, paradoxically, cellular overexpression of SUMO-1 increases PR transcriptional activity even if Lys-388 is mutated, suggesting that the receptors are activated indirectly by other SUMOylated proteins. One of these is the coactivator SRC-1, whose binding to PR and enhancement of agonist-dependent N-/C-terminal interactions is augmented by the presence of SUMO-1. Increased transcription due to SRC-1 is independent of PR SUMOylation based on assays with the Lys-388 mutants and the pure antiprogestin ZK98299, which blocks N-/C-terminal interactions. In summary, SUMOylation tightly regulates the transcriptional activity of PR by repressing the receptors directly while activating them indirectly through augmented SRC-1 coactivation.
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Registered trials
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.