Mammalian Per-Arnt-Sim Proteins in Environmental Adaptation
Abstract
The Per-Arnt-Sim (PAS) domain is conserved across the kingdoms of life and found in an ever-growing list of proteins. This domain can bind to and sense endogenous or xenobiotic small molecules such as molecular oxygen, cellular metabolites, or polyaromatic hydrocarbons. Members of this family are often found in pathways that regulate responses to environmental change; in mammals these include the hypoxia, circadian, and dioxin response pathways. These pathways function in development and throughout life to regulate cellular, organ, and whole-organism adaptive responses. Remarkably, in the case of the clock, this adaptation includes anticipation of environmental change. In this review, we summarize the roles of PAS domain-containing proteins in mammals. We provide structural evidence that functionally classifies both known and unknown biological roles. Finally, we discuss the role of PAS proteins in anticipation of and adaptation to environmental change.
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Mice homozygous for AhrTer383 are a phenocopy of null mice for the DV endpoint and may help identify other ARNT-dependent signaling events mediated by partners such as HIFs.
“Finally, it is important to note that mice homozygous for this allele are a phenocopy of null mice for the DV endpoint and may be useful in identifying other ARNT dependent signaling events mediated by partners such as hypoxia inducible factors (HIFs) (Chan et al., 1999; Gradin et al., 1996; McIntosh et al., 2010).”
From Rodent Genetic Models of Ah Receptor Signaling (2021) · cites this paper as McIntosh et al., 2010
ARNT dimerizes with HIFs and is essential for hypoxia response, glucose metabolism, blood cell development, and angiogenesis.
“Notably, ARNT is now known to dimerize with HIFs, and through these interactions is essential in biological processes including the hypoxia response, glucose metabolism, blood cell development, and angiogenesis (Gradin et al., 1996; McIntosh et al., 2010).”
From Rodent Genetic Models of Ah Receptor Signaling (2021) · cites this paper as McIntosh et al., 2010
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Atomic force microscopy – looking at mechanosensors on the cell surface
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Cryo-EM structure of the cytosolic AhR complex.
Wen, Z., Zhang, Y., Zhang, B., Hang, Y., Xu, L., Chen, Y., Xie, Q., Zhao, Q., Zhang, L., Li, G., et al. (2023) · Structure · doi:10.1016/j.str.2022.12.013 · Cited by 51 · see citing works
Identification of oleoylethanolamide as an endogenous ligand for HIF-3α
Diao, X., Ye, F., Zhang, M., Ren, X., Tian, X., Lu, J., Sun, X., Hou, Z., Chen, X., Li, F., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30338-z · Cited by 51 · see citing works
Identification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR
Hao, N., Whitelaw, M. L., Shearwin, K. E., Dodd, I. B., & Chapman‐Smith, A. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq1336 · Cited by 51 · see citing works
Oyama, Y., Bartman, C. M., Bonney, S. K., Lee, J. S., Walker, L. A., Han, J., Borchers, C. H., Buttrick, P. M., Aherne, C. M., Clendenen, N., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.07.020 · Cited by 50 · see citing works
Circadian clock disruption in the mouse ovary in response to 2,3,7,8-tetrachlorodibenzo-p-dioxin
Tischkau, S. A., Jaeger, C., & Krager, S. L. (2010) · Toxicology Letters · doi:10.1016/j.toxlet.2010.12.013 · Cited by 49 · see citing works
Interorgan rhythmicity as a feature of healthful metabolism
Bass, J. T. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.01.009 · Cited by 49 · see citing works
Kynurenic Acid/AhR Signaling at the Junction of Inflammation and Cardiovascular Diseases
Grishanova, A. Y., & Perepechaeva, M. L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25136933 · Cited by 51 · see citing works
The Aryl Hydrocarbon Receptor in Immunity: Tools and Potential
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Wu, G., Lee, Y. Y., Gulla, E. M., Potter, A., Kitzmiller, J. A., Ruben, M. D., Salomonis, N., Whitsett, J. A., Francey, L. J., Hogenesch, J. B., et al. (2021) · eLife · doi:10.7554/elife.63003 · Cited by 48 · see citing works
Self-citationStructure of the class C orphan GPCR GPR158 in complex with RGS7-Gβ5
Jeong, E.-Y., Kim, Y., Jeong, J., & Cho, Y. (2021) · Nature Communications · doi:10.1038/s41467-021-27147-1 · Cited by 47 · see citing works
LIN-42, the Caenorhabditis elegans PERIOD homolog, Negatively Regulates MicroRNA Transcription
Perales, R., King, D., Aguirre-Chen, C., & Hammell, C. M. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004486 · Cited by 44 · see citing works
Aryl Hydrocarbon Receptor Mechanisms Affecting Chronic Kidney Disease
Curran, C. S., & Kopp, J. B. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.782199 · Cited by 46 · see citing works
CRY1‐CBS binding regulates circadian clock function and metabolism
Cal‐Kayitmazbatir, S., Kulkoyluoglu‐Cotul, E., Growe, J., Selby, C. P., Rhoades, S. D., Malik, D. M., Öner, H., Asimgil, H., Francey, L. J., Sancar, A., et al. (2020) · FEBS Journal · doi:10.1111/febs.15360 · Cited by 44 · see citing works
Self-citationAHR Ligands: Promiscuity in Binding and Diversity in Response
DeGroot, D., He, G., Fraccalvieri, D., Bonati, L., Pandini, A., & Denison, M. S. (2011) · The AH Receptor in Biology and Toxicology · doi:10.1002/9781118140574.ch4 · Cited by 43 · see citing works
- Authors
- McIntosh, B. E., Hogenesch, J. B., & Bradfield, C. A.
- Affiliations
- University of Wisconsin–Madison (US)
- University of Pennsylvania (US)
- Venue
- Annual Review of Physiology
- Publisher
- Annual Reviews
- Published
- 2010-03-17
- Volume
- 72
- Issue
- 1
- Pages
- 625-645
- ISSN
- 0066-4278 (ISSN-L)
- 1545-1585
- OpenAlex
- W2143654291
- Cited by
- 352
- References
- 233
- Citations by year
- 2026: 4 · 2025: 13 · 2024: 24 · 2023: 21 · 2022: 26 · 2021: 30 · 2020: 18 · 2019: 14 · 2018: 15 · 2017: 14 · 2016: 28 · 2015: 18 · 2014: 25 · 2013: 36 · 2012: 32
- FWCI
- 3.23
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Physiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Environmental Health Sciences (R37ES005703)
- Topics
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
- Keywords
- environmental adaptation, hypoxia response, circadian clock, metabolite sensing, polycyclic aromatic hydrocarbons, protein structure, mammalian physiology
- MeSH terms
- Adaptation, Physiological, Amino Acid Sequence, Animals, Hypoxia, Circadian Rhythm, Dioxins, Environment, Humans, Mammals, Terminology as Topic, Polycyclic Aromatic Hydrocarbons, Signal Transduction, Aryl Hydrocarbon Receptor Nuclear Translocator, Basic Helix-Loop-Helix Proteins, Basic Helix-Loop-Helix Transcription Factors, Period Circadian Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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