ArticleMolecular and cellular biology2001
The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor.
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 56 papers.
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Who cites it
56 citing papers in PubMed, 200 citations in OpenAlex.
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- Interaction patterns of methoprene-tolerant and germ cell-expressedFrontiers in molecular biosciences · 2023Article
- From Nucleus to Organs: Insights of Aryl Hydrocarbon Receptor Molecular Mechanisms.International journal of molecular sciences · 2022Review
- The aryl hydrocarbon receptor as a model PAS sensor.Toxicology reports · 2022Review
- Aryl hydrocarbon receptor: The master regulator of immune responses in allergic diseases.Frontiers in immunology · 2022Review
- Purification of an insect juvenile hormone receptor complex enables insights into its post-translational phosphorylation.The Journal of biological chemistry · 2021Article
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- Role of Heat Shock Proteins (HSP70 and HSP90) in Viral Infection.International journal of molecular sciences · 2021Review
- Aryl hydrocarbon receptor in mesenchymal stromal cells: new frontiers in AhR biology.The FEBS journal · 2021Review
- The Aryl Hydrocarbon Receptor Undergoes Chaperone-Mediated Autophagy in Triple-Negative Breast Cancer Cells.International journal of molecular sciences · 2021Article
- The Aryl Hydrocarbon Receptor as a Modulator of Anti-viral Immunity.Frontiers in immunology · 2021Review
- Regulation of Filaggrin, Loricrin, and Involucrin by IL-4, IL-13, IL-17A, IL-22, AHR, and NRF2: Pathogenic Implications in Atopic Dermatitis.International journal of molecular sciences · 2020Review
- Baicalein Inhibits Benzo[a]pyrene-Induced Toxic Response by Downregulating Src Phosphorylation and by Upregulating NRF2-HMOX1 System.Antioxidants (Basel, Switzerland) · 2020Article
- The Ah Receptor: Adaptive Metabolism, Ligand Diversity, and the Xenokine Model.Chemical research in toxicology · 2020Review
- New Insights Into Heat Shock Protein 90 in the Pathogenesis of Pulmonary Arterial Hypertension.Frontiers in physiology · 2020Review
- Expression and role of aryl hydrocarbon receptor inInternational journal of ophthalmology · 2020Article
- Chloracne and Hyperpigmentation Caused by Exposure to Hazardous Aryl Hydrocarbon Receptor Ligands.International journal of environmental research and public health · 2019Review
- Aryl Hydrocarbon Receptor in Atopic Dermatitis and Psoriasis.International journal of molecular sciences · 2019Review
- Xenobiotic Receptors and Their Mates in Atopic Dermatitis.International journal of molecular sciences · 2019Review
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
The molecular chaperone complex hsp90-p23 interacts with the dioxin receptor, a ligand-dependent basic helix-loop-helix (bHLH)/Per-Arnt-Sim domain transcription factor. Whereas biochemical and genetic evidence indicates that hsp90 is important for maintenance of a high-affinity ligand binding conformation of the dioxin receptor, the role of hsp90-associated proteins in regulation of the dioxin receptor function remains unclear. Here we demonstrate that the integrity of the hsp90 complex characterized by the presence of the hsp90-associated cochaperone p23 and additional cochaperone proteins is important for regulation of the intracellular localization of the dioxin receptor by two mechanisms. First, in the absence of ligand, the dioxin receptor-hsp90 complex was associated with the immunophilin-like protein XAP2 to mediate cytoplasmic retention of the dioxin receptor. Second, upon exposure to ligand, the p23-associated hsp90 complex mediated interaction of the dioxin receptor with the nuclear import receptor protein pendulin and subsequent nuclear translocation of the receptor. Interestingly, these two modes of regulation target two distinct functional domains of the dioxin receptor. Whereas the nuclear localization signal-containing and hsp90-interacting bHLH domain of the receptor regulates ligand-dependent nuclear import, the interaction of the p23-hsp90-XAP2 complex with the ligand binding domain of the dioxin receptor was essential to mediate cytoplasmic retention of the ligand-free receptor form. In conclusion, these data suggest a novel role of the hsp90 molecular chaperone complex in regulation of the intracellular localization of the dioxin receptor.
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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.