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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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“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
In the citing paper
“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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Clustal W and Clustal X version 2.0
Larkin, M., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P., McWilliam, H., Valentin, F., Wallace, I. M., Wilm, A., López, R., et al. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btm404 · Cited by 28,598
Wang, G. L., Jiang, B. H., Rue, E. A., & Semenza, G. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5510 · Cited by 6,212
The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735 · cited 1×
“This domain contains proline residues that are rapidly hydroxylated by three prolyl hydroxylase enzymes (EGL9 homologs, Egln1–3) whose enzymatic activity requires normal oxygen levels (81).”
BackgroundActivation of vascular endothelial growth factor gene transcription by hypoxia-inducible factor 1
Forsythe, J. A., Jiang, B.-H., Iyer, N. V., Agani, F., Leung, S. W., Koos, R. D., & Semenza, G. L. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.9.4604 · Cited by 3,981
A gene atlas of the mouse and human protein-encoding transcriptomes
Su, A. I., Wiltshire, T., Batalov, S., Lapp, H., Ching, K. A., Block, D., Zhang, J., Soden, R., Hayakawa, M., Kreiman, G., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400782101 · Cited by 3,475
Self-citationSemenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617
Poland, A., & Knutson, J. C. (1982) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pa.22.040182.002505 · Cited by 2,515
Role of HIF-1α in hypoxia-mediated apoptosis, cell proliferation and tumour angiogenesis
Carmeliet, P., Dor, Y., Herbert, J.-M., Fukumura, D., Brusselmans, K., Dewerchin, M., Neeman, M., Bono, F., Abramovitch, R., Maxwell, P., et al. (1998) · Nature · doi:10.1038/28867 · Cited by 2,502
Cellular and developmental control of O 2 homeostasis by hypoxia-inducible factor 1α
Iyer, N. V., Kotch, L. E., Agani, F., Leung, S. W., Laughner, E., Wenger, R. H., Gassmann, M., Gearhart, J. D., Lawler, A. M., Yu, A. Y., et al. (1998) · Genes & Development · doi:10.1101/gad.12.2.149 · Cited by 2,476
Research works printed but not linked: 6
- Gu YZ, 1998, Gene Expr., 7, 205
- Page RD, 2002, Curr. Protoc. Bioinformatics Chapter, 6, 0
- 10.1379/1466-1268(2004)009<0004:COHSPA>2.0.CO;2 · DOI
- Yunokawa M, 2007, Oncol. Rep., 17, 871
- Pratt WB, 1996, EXS, 77, 79
- Perdew GH, 1996, Biochem. Mol. Biol. Int., 39, 589
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Shimizu, T., Huang, D., Fang, Y., Stráňava, M., Bartošová, M., Fojtíková, V., & Martínková, M. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00018 · Cited by 198
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Whitehead, A., Clark, B. W., Reid, N. M., Hahn, M. E., & Nacci, D. E. (2017) · Evolutionary Applications · doi:10.1111/eva.12470 · Cited by 168
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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
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
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 52
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 49
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
Interorgan rhythmicity as a feature of healthful metabolism
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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 53
The Aryl Hydrocarbon Receptor in Immunity: Tools and Potential
Esser, C. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3139-2_16 · Cited by 49
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 50
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
LIN-42, the Caenorhabditis elegans PERIOD homolog, Negatively Regulates MicroRNA Transcription
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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 50
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 45
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
Metadata
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 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
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