ArticleNucleic acids research2011
Identification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 56 citations in OpenAlex.
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- In Silico Exploration of AHR-HIF Pathway Interplay: Implications for Therapeutic Targeting in ccRCC.Genes · 2024Article
- TCDD-Induced Allosteric Perturbation of the AhR:ARNT Binding to DNA.International journal of molecular sciences · 2023Article
- NPAS4 regulates the transcriptional response of the suprachiasmatic nucleus to light and circadian behavior.Neuron · 2021Article
- Recent advances in the development of AHR antagonists in immuno-oncology.RSC medicinal chemistry · 2021Review
- Genome-wide identification of the GATA transcription factor family and their expression patterns under temperature and salt stress in Aspergillus oryzae.AMB Express · 2021Article
- Molecular characterisation of rare loss-of-function NPAS3 and NPAS4 variants identified in individuals with neurodevelopmental disorders.Scientific reports · 2021Article
- Modulation of HIF-2α PAS-B domain contributes to physiological responses.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Expression of the neuroprotective protein aryl hydrocarbon receptor nuclear translocator 2 correlates with neuronal stress and disability in models of multiple sclerosis.Journal of neuroinflammation · 2018Article
- Changes in chromatin state reveal ARNT2 at a node of a tumorigenic transcription factor signature driving glioblastoma cell aggressiveness.Acta neuropathologica · 2018Article
- Structural hierarchy controlling dimerization and target DNA recognition in the AHR transcriptional complex.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural modeling of the AhR:ARNT complex in the bHLH-PASA-PASB region elucidates the key determinants of dimerization.Molecular bioSystems · 2017Article
- Molecular modeling of the AhR structure and interactions can shed light on ligand-dependent activation and transformation mechanisms.Current opinion in toxicology · 2017Article
- Deciphering Dimerization Modes of PAS Domains: Computational and Experimental Analyses of the AhR:ARNT Complex Reveal New Insights Into the Mechanisms of AhR Transformation.PLoS computational biology · 2016Article
- A network model for angiogenesis in ovarian cancer.BMC bioinformatics · 2015Article
- Promoter activation by CII, a potent transcriptional activator from bacteriophage 186.The Journal of biological chemistry · 2014Article
- Differential suppression of the aryl hydrocarbon receptor nuclear translocator-dependent function by an aryl hydrocarbon receptor PAS-A-derived inhibitory molecule.Biochemical pharmacology · 2014Article
- Multi-PAS domain-mediated protein oligomerization of PpsR from Rhodobacter sphaeroides.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Aryl hydrocarbon receptor (AHR) in the cnidarian Nematostella vectensis: comparative expression, protein interactions, and ligand binding.Development genes and evolution · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The basic helix-loop-helix (bHLH).PAS dimeric transcription factors have crucial roles in development, stress response, oxygen homeostasis and neurogenesis. Their target gene specificity depends in part on partner protein choices, where dimerization with common partner Aryl hydrocarbon receptor nuclear translocator (Arnt) is an essential step towards forming active, DNA binding complexes. Using a new bacterial two-hybrid system that selects for loss of protein interactions, we have identified 22 amino acids in the N-terminal PAS domain of Arnt that are involved in heterodimerization with aryl hydrocarbon receptor (AhR). Of these, Arnt E163 and Arnt S190 were selective for the AhR/Arnt interaction, since mutations at these positions had little effect on Arnt dimerization with other bHLH.PAS partners, while substitution of Arnt D217 affected the interaction with both AhR and hypoxia inducible factor-1α but not with single minded 1 and 2 or neuronal PAS4. Arnt uses the same face of the N-terminal PAS domain for homo- and heterodimerization and mutational analysis of AhR demonstrated that the equivalent region is used by AhR when dimerizing with Arnt. These interfaces differ from the PAS β-scaffold surfaces used for dimerization between the C-terminal PAS domains of hypoxia inducible factor-2α and Arnt, commonly used for PAS domain interactions.
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