ArticleProceedings of the National Academy of Sciences of the United States of America2000
Hormone binding induces rapid proteasome-mediated degradation of thyroid hormone receptors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 144 citations in OpenAlex.
- Mechanisms for Mineralocorticoid-Driven Age-Related Hypertension: Potential Therapeutic Role of Mineralocorticoid Receptor Antagonists and Aldosterone Synthase Inhibitors.Circulation research · 2026Review
- Induced protein degradation for therapeutics: past, present, and future.The Journal of clinical investigation · 2024Review
- UBR5 forms ligand-dependent complexes on chromatin to regulate nuclear hormone receptor stability.Molecular cell · 2023Article
- Thyroid hormone receptor phosphorylation regulates acute fasting-induced suppression of the hypothalamic-pituitary-thyroid axis.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Thyroid Hormone Receptor β Inhibits Self-Renewal Capacity of Breast Cancer Stem Cells.Thyroid : official journal of the American Thyroid Association · 2020Article
- Acetylation modulates thyroid hormone receptor intracellular localization and intranuclear mobility.Molecular and cellular endocrinology · 2019Article
- Redox Regulation of Heme Oxygenase-2 and the Transcription Factor, Rev-Erb, Through Heme Regulatory Motifs.Antioxidants & redox signaling · 2018Review
- Methylcytosine dioxygenase TET3 interacts with thyroid hormone nuclear receptors and stabilizes their association to chromatin.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Changes in Hepatic TRβ Protein Expression, Lipogenic Gene Expression, and Long-Chain Acylcarnitine Levels During Chronic Hyperthyroidism and Triiodothyronine Withdrawal in a Mouse Model.Thyroid : official journal of the American Thyroid Association · 2017Article
- Impaired Repressor Function in SUMOylation-Defective Thyroid Hormone Receptor Isoforms.European thyroid journal · 2016Article
- Desensitization and Incomplete Recovery of Hepatic Target Genes After Chronic Thyroid Hormone Treatment and Withdrawal in Male Adult Mice.Endocrinology · 2016Article
- MuRF1 mono-ubiquitinates TRα to inhibit T3-induced cardiac hypertrophy in vivo.Journal of molecular endocrinology · 2016Article
- Ubiquitylation of nuclear receptors: new linkages and therapeutic implications.Journal of molecular endocrinology · 2015Review
- Thyroid Hormone Receptors Predict Prognosis in BRCA1 Associated Breast Cancer in Opposing Ways.PloS one · 2015Article
- Src-dependent phosphorylation at Y406 on the thyroid hormone receptor β confers the tumor suppressor activity.Oncotarget · 2014Article
- Expression of neddylation-related proteins in melanoma cell lines and the effect of neddylation on melanoma proliferation.Oncology letters · 2014Article
- Thyroid hormone receptors and cancer.Biochimica et biophysica acta · 2013Review
- Upregulation of SIRT1 by 17β-estradiol depends on ubiquitin-proteasome degradation of PPAR-γ mediated by NEDD4-1.Protein & cell · 2013Article
- ERα phosphorylation at Y537 by Src triggers E6-AP-ERα binding, ERα ubiquitylation, promoter occupancy, and target gene expression.Molecular endocrinology (Baltimore, Md.) · 2012Article
- Back to your heart: ubiquitin proteasome system-regulated signal transduction.Journal of molecular and cellular cardiology · 2012Review
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
The thyroid hormone 3,3',5-triiodo-l-thyronine (T3) is essential for growth, differentiation, and development. Its biological activities are mediated by T3 nuclear receptors (TRs). At present, how T3 regulates TR proteins and the resulting functional consequences are still unknown. Immunofluorescence analyses of endogenous TR in the growth hormone-producing GC cells showed that the T3-induced rapid degradation of TR was specifically blocked by lactacystin, a selective inhibitor of the ubiquitin-proteasome degradation pathway. Immunoblots demonstrated that the transfected TRbeta1 was ubiquitinated and that the ubiquitination was T3 independent. Studies with a series of truncated TRbeta1 showed that the hormone-binding domain was sufficient for the T3-induced rapid degradation of TRbeta1 by the proteasome degradation pathway. T3 also induced rapid degradation of TRbeta2 and TRalpha1. In contrast, the stability of the non-T3-binding TRalpha2 and naturally occurring TRbeta1 mutants that do not bind T3 was not affected by T3 treatment, indicating that hormone binding to receptor was essential for the degradation of the wild-type receptors. In the presence of proteasome protease inhibitors, the levels of both total and ubiquitinated TRbeta1 protein increased, yet T3-dependent transcriptional activation and the expression of the growth hormone gene were diminished, suggesting that proteasome-mediated degradation played a novel role in modulating transcriptional activation by TR. The present study reveals a role of T3 in modulating the functions of TR by regulating its receptor level via the ubiquitin-proteasome degradation pathway.
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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 Socratic graph.