ArticleMolecular and cellular biology2001
Ligand-dependent degradation of retinoid X receptors does not require transcriptional activity or coactivator interactions.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 55 citations in OpenAlex.
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- Surprising Features of Nuclear Receptor Interaction Networks Revealed by Live Cell Single Molecule Imaging.bioRxiv : the preprint server for biology · 2024Article
- Liver X receptors and liver physiology.Biochimica et biophysica acta. Molecular basis of disease · 2021Review
- Inflammation Triggers Liver X Receptor-Dependent Lipogenesis.Molecular and cellular biology · 2020Article
- Tributyltin chloride (TBT) induces RXRA down-regulation and lipid accumulation in human liver cells.PloS one · 2019Article
- Guggulsterone and bexarotene induce secretion of exosome-associated breast cancer resistance protein and reduce doxorubicin resistance in MDA-MB-231 cells.International journal of cancer · 2015Article
- Retinoid X receptor α overexpression alleviates mitochondrial dysfunction-induced insulin resistance through transcriptional regulation of insulin receptor substrate 1.Molecules and cells · 2015Article
- Differential regulation of gene expression by LXRs in response to macrophage cholesterol loading.Molecular endocrinology (Baltimore, Md.) · 2013Article
- The Ski protein negatively regulates Siah2-mediated HDAC3 degradation.Biochemical and biophysical research communications · 2010Article
- HACE1: A novel repressor of RAR transcriptional activity.Journal of cellular biochemistry · 2009Article
- Differential regulation of estrogen-inducible proteolysis and transcription by the estrogen receptor alpha N terminus.Molecular and cellular biology · 2005Article
- c-Jun N-terminal kinase contributes to aberrant retinoid signaling in lung cancer cells by phosphorylating and inducing proteasomal degradation of retinoic acid receptor alpha.Molecular and cellular biology · 2005Article
- Proteasomal inhibition enhances glucocorticoid receptor transactivation and alters its subnuclear trafficking.Molecular and cellular biology · 2002Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cells utilize ubiquitin-mediated proteolysis to regulate the activity of numerous proteins involved in signal transduction, cell cycle control, and transcriptional regulation. For a number of transcription factors, there appears to be a direct correlation between transcriptional activity and protein instability, suggesting that cells use targeted destruction as one method to down-regulate or attenuate gene expression. In this report we demonstrate that retinoid X receptors (RXRs) which function as versatile mediators of nuclear hormone-dependent gene expression are marked for destruction upon binding agonist ligands. Interestingly, when RXR serves as a heterodimeric partner for retinoic acid (RAR) or thyroid hormone (TR) receptors, binding of agonists by RAR or TR leads to degradation of both the transcriptionally active RAR or TR subunits as well as the transcriptionally inactive RXR subunit. Furthermore, using a series of mutants in the ligand-dependent activation domain (activation function 2), we demonstrate that agonist-stimulated degradation of RXR does not require corepressor release, coactivator binding, or transcriptional activity. Taken together, the data suggest a model for targeted destruction of transcription factors based on structural or conformational signals as opposed to functional coupling with gene transcription.
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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.