{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T05:07:33Z","timestamp":1789016853213,"version":"build-2803163510"},"reference-count":154,"publisher":"MDPI AG","issue":"9","license":[{"start":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T00:00:00Z","timestamp":1788825600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100007446","name":"King Khalid University","doi-asserted-by":"crossref","award":["RGP1\/64\/47"],"award-info":[{"award-number":["RGP1\/64\/47"]}],"id":[{"id":"10.13039\/501100007446","id-type":"DOI","asserted-by":"crossref"}]},{"award":["RGP1\/64\/47"],"award-info":[{"award-number":["RGP1\/64\/47"]}],"id":[{"id":"https:\/\/ror.org\/052kwzs30","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmaceuticals"],"abstract":"<jats:p>The aryl hydrocarbon receptor (AHR) and the vitamin D receptor (VDR) were long regarded as independent transcription factors governing distinct physiology\u2014xenobiotic sensing and calcium\u2013vitamin D homeostasis, respectively. AHR, a basic helix\u2013loop\u2013helix\/PAS protein, heterodimerizes with ARNT and binds xenobiotic response elements (XREs) to drive cytochrome P450 genes such as CYP1A1; VDR, a nuclear receptor activated by 1,25-dihydroxyvitamin D3, heterodimerizes with RXR and binds vitamin D response elements (VDREs). Although their genes reside on separate chromosomes (AHR, Chr 7; VDR, Chr 12), an integrated view recognizes the two pathways as extensively cross-regulatory. This review synthesizes the molecular, immunological, and tissue-level evidence for VDR\u2013AHR interplay. At the molecular level, the receptors cooperate at composite promoter architectures\u2014most notably an everted-repeat VDRE positioned adjacent to an XRE in the CYP1A1 promoter\u2014while AHR ligands reciprocally enhance CYP24A1-mediated catabolism of active vitamin D. Tryptophan metabolism provides a bidirectional hub: kynurenine and the UVB photoproduct FICZ serve as endogenous AHR ligands whose balance, modulated by VDR, shapes signaling output. The tumor suppressor p53 functions as a shared upstream regulator coupling genotoxic stress to both receptors, with convergence on the CDKN1A (p21) checkpoint. Functionally, AHR and VDR converge on the regulatory T cell (Treg)\/Th17 axis to influence immune tolerance: sustained AHR activation by TCDD favors Foxp3+ Treg differentiation, transient FICZ-driven activation promotes Th17 responses, and VDR reinforces the tolerogenic arm while independently repressing IL-17. The receptors further cooperate in maintaining intestinal epithelial barrier integrity and NF-\u03baB restraint, with parallel impairment in inflammatory bowel disease, and are co-activated in skin by solar UVB, which simultaneously generates vitamin D3 and the AHR ligand FICZ within keratinocytes. In cancer, VDR acts as a tumor suppressor, AHR exhibits context-dependent pro- and anti-tumor roles, and a three-way AHR\u2013VDR\u2013p53 interaction\u2014inverted by mutant p53\u2014forms a critical regulatory node. Throughout, the direction and magnitude of cross-talk prove highly dependent on cell type, ligand identity and kinetics, and species\u2014distinctions often underappreciated in the literature. Clarifying these context-specific determinants is essential for translating AHR\u2013VDR cross-regulation into rational therapies in autoimmunity, mucosal inflammation, dermatology, and oncology.<\/jats:p>","DOI":"10.3390\/ph19091416","type":"journal-article","created":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T08:10:22Z","timestamp":1788855022000},"page":"1416","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Cooperation or Conflict? Molecular and Physiological Cross-Talk Between the Aryl Hydrocarbon and Vitamin D Receptors"],"prefix":"10.3390","volume":"19","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1551-1132","authenticated-orcid":false,"given":"Mohammed A.","family":"Alqahtani","sequence":"first","affiliation":[{"name":"Department of Pharmacology, College of Pharmacy, King Khalid University, P.O. Box 960, Abha 61421, Saudi Arabia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,9,8]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"954","DOI":"10.1126\/science.1852076","article-title":"Cloning of a factor required for activity of the Ah (dioxin) receptor","volume":"252","author":"Hoffman","year":"1991","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1146\/annurev.pharmtox.43.100901.135828","article-title":"Activation of the aryl hydrocarbon receptor by structurally diverse exogenous and endogenous chemicals","volume":"43","author":"Denison","year":"2003","journal-title":"Annu. Rev. Pharmacol. 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