ArticleMolecular and cellular biology2006
Nuclear compartmentalization of N-CoR and its interactions with steroid receptors.
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- Review
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- Mediator subunit MED1 modulates intranuclear dynamics of the thyroid hormone receptor.Journal of cellular biochemistry · 2020Article
- Negative Correlation between the Diffusion Coefficient and Transcriptional Activity of the Glucocorticoid Receptor.International journal of molecular sciences · 2017Article
- Mechanism of androgen receptor corepression by CKβBP2/CRIF1, a multifunctional transcription factor coregulator expressed in prostate cancer.Molecular and cellular endocrinology · 2014Article
- Ski-interacting protein (SKIP) interacts with androgen receptor in the nucleus and modulates androgen-dependent transcription.BMC biochemistry · 2013Article
- SMRTε, a corepressor variant, interacts with a restricted subset of nuclear receptors, including the retinoic acid receptors α and β.Molecular and cellular endocrinology · 2012Article
- The leukemia-associated fusion protein MN1-TEL blocks TEL-specific recognition sequences.PloS one · 2012Article
- Analysis of interdomain interactions of the androgen receptor.Methods in molecular biology (Clifton, N.J.) · 2011Article
- Glucocorticoid receptor cofactors as therapeutic targets.Current opinion in pharmacology · 2010Review
- Estrogen receptors recruit SMRT and N-CoR corepressors through newly recognized contacts between the corepressor N terminus and the receptor DNA binding domain.Molecular and cellular biology · 2010Article
- FOXO1 transrepresses peroxisome proliferator-activated receptor gamma transactivation, coordinating an insulin-induced feed-forward response in adipocytes.The Journal of biological chemistry · 2009Article
- Structural basis for nuclear receptor corepressor recruitment by antagonist-liganded androgen receptor.Molecular cancer therapeutics · 2008Article
- What goes on behind closed doors: physiological versus pharmacological steroid hormone actions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2008Review
- Differential modulation of glucocorticoid and progesterone receptor transactivation.Molecular and cellular endocrinology · 2008Article
- A repressive role for prohibitin in estrogen signaling.Molecular endocrinology (Baltimore, Md.) · 2008Article
- Antiinflammatory glucocorticoid receptor ligand with reduced side effects exhibits an altered protein-protein interaction profile.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Transcriptional repression by androgen receptor: roles in castration-resistant prostate cancer.Asian journal of andrologyReview
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The repression mechanisms by the nuclear receptor corepressor (N-CoR) of steroid hormone receptor (SHR)-mediated transactivation were examined. Yellow fluorescent protein (YFP)-N-CoR was distributed as intranuclear discrete dots, while coexpression of androgen receptor (AR), glucocorticoid receptor alpha, and estrogen receptor alpha ligand-dependently triggered redistribution of YFP-N-CoR. In fluorescence recovery after photobleaching analysis, mobility of the N-CoR was reduced by 5alpha-dihydrotestosterone (DHT)-bound AR. The middle region of N-CoR mostly contributed to the interaction with agonist-bound SHRs and the suppression of their transactivation function. N-CoR impaired the DHT-induced N-C interaction of AR, and the impaired interaction was dose-dependently recovered by coexpression of SRC-1 and CBP. N-CoR also impaired the intranuclear complete (distinct) focus formation of SHRs. Coexpression of SRC-1 or CBP released YFP-N-CoR or endogenous N-CoR from incomplete foci and simultaneously recovered complete foci of AR-green fluorescent protein. These results indicate that the relative ratio of coactivators and corepressors determines the conformational equilibrium between transcriptionally active and inactive SHRs in the presence of agonists. The intranuclear foci formed by agonist-bound SHRs were completely destroyed by actinomycin D and alpha-amanitin, indicating that the focus formation does not precede the transcriptional activation. The focus formation may reflect the accumulation of SHR/coactivator complexes released from the transcriptionally active sites and thus be a mirror of transcriptionally active complex formation.
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