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Science 17 May 1991:
Vol. 252. no. 5008, pp. 954 - 958
DOI: 10.1126/science.1852076
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Articles

Science, Vol 252, Issue 5008, 954-958
Copyright © 1991 by American Association for the Advancement of Science

articles

Cloning of a factor required for activity of the Ah (dioxin) receptor

EC Hoffman, H Reyes, FF Chu, F Sander, LH Conley, BA Brooks, and O Hankinson

Department of Pathology, University of California, Los Angeles 90024.

The aryl hydrocarbon (Ah) receptor binds various environmental pollutants, such as polycyclic aromatic hydrocarbons, heterocyclic amines, and polychlorinated aromatic compounds (dioxins, dibenzofurans, and biphenyls), and mediates the carcinogenic effects of these agents. The complementary DNA and part of the gene for an 87-kilodalton human protein that is necessary for Ah receptor function have been cloned. The protein is not the ligand-binding subunit of the receptor but is a factor that is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after binding ligand. The requirement for this factor distinguishes the Ah receptor from the glucocorticoid receptor, to which the Ah receptor has been presumed to be similar. Two portions of the 87-kilodalton protein share sequence similarities with two Drosophila proteins, Per and Sim. Another segment of the protein shows conformity to the consensus sequence for the basic helix-loop-helix motif found in proteins that bind DNA as homodimers or heterodimers.


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J. Biol. Chem. 277, 31963-31971
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R. H. WENGER (2002)
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J. Biol. Chem. 277, 23821-23827
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Recruitment of Dioxin Receptor to Active Transcription Sites.
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Mol. Biol. Cell 13, 2001-2015
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Regulatory Interactions among Three Members of the Vertebrate Aryl Hydrocarbon Receptor Family: AHR Repressor, AHR1, and AHR2.
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J. Biol. Chem. 277, 6949-6959
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Expression of AhR and ARNT mRNA in Cultured Human Endometrial Explants Exposed to TCDD.
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X.-D. Lei, B. Chapman, and O. Hankinson (2001)
Mol. Pharmacol. 60, 388-393
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Phosphatidylinositol 3-Kinase Signaling Controls Levels of Hypoxia-inducible Factor 1.
B.-H. Jiang, G. Jiang, J. Z. Zheng, Z. Lu, T. Hunter, and P. K. Vogt (2001)
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Y. Takahashi, S. Takahashi, Y. Shiga, T. Yoshimi, and T. Miura (2000)
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G. Elizondo, P. Fernandez-Salguero, M. S. Sheikh, G.-Y. Kim, A. J. Fornace, K. S. Lee, and F. J. Gonzalez (2000)
Mol. Pharmacol. 57, 1056-1063
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G. L. Semenza (2000)
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E. Gothie, D. E. Richard, E. Berra, G. Pages, and J. Pouyssegur (2000)
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M. T. Chin, K. Maemura, S. Fukumoto, M. K. Jain, M. D. Layne, M. Watanabe, C.-M. Hsieh, and M.-E. Lee (2000)
J. Biol. Chem. 275, 6381-6387
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Aromatic Hydrocarbon Receptor Interaction with the Retinoblastoma Protein Potentiates Repression of E2F-dependent Transcription and Cell Cycle Arrest.
A. Puga, S. J. Barnes, T. P. Dalton, C.-y. Chang, E. S. Knudsen, and M. A. Maier (2000)
J. Biol. Chem. 275, 2943-2950
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Mammalian oxygen sensing, signalling and gene regulation.
R. Wenger (2000)
J. Exp. Biol. 203, 1253-1263
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Degradation of the Basic Helix-Loop-Helix/Per-ARNT-Sim Homology Domain Dioxin Receptor Via the Ubiquitin/Proteasome Pathway.
B. J. Roberts and M. L. Whitelaw (1999)
J. Biol. Chem. 274, 36351-36356
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Hypoxia Upregulates Activity and Expression of the Glucose Transporter GLUT1 in Alveolar Epithelial Cells.
A. Ouiddir, C. Planès, I. Fernandes, A. VanHesse, and C. Clerici (1999)
Am. J. Respir. Cell Mol. Biol. 21, 710-718
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Similarity of the C. elegans Developmental Timing Protein LIN-42 to Circadian Rhythm Proteins.
M. Jeon, H. F. Gardner, E. A. Miller, J. Deshler, and A. E. Rougvie (1999)
Science 286, 1141-1146
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Generation of a Dominant-negative Mutant of Endothelial PAS Domain Protein 1 by Deletion of a Potent C-terminal Transactivation Domain.
K. Maemura, C.-M. Hsieh, M. K. Jain, S. Fukumoto, M. D. Layne, Y. Liu, S. Kourembanas, S.-F. Yet, M. A. Perrella, and M.-E. Lee (1999)
J. Biol. Chem. 274, 31565-31570
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Regulation of the Erythropoietin Gene.
B. L. Ebert and H. F. Bunn (1999)
Blood 94, 1864-1877
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Multiple Roles of Ligand in Transforming the Dioxin Receptor to an Active Basic Helix-Loop-Helix/PAS Transcription Factor Complex with the Nuclear Protein Arnt.
M. J. Lees and M. L. Whitelaw (1999)
Mol. Cell. Biol. 19, 5811-5822
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PAS Domains: Internal Sensors of Oxygen, Redox Potential, and Light.
B. L. Taylor and I. B. Zhulin (1999)
Microbiol. Mol. Biol. Rev. 63, 479-506
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Repression of Dioxin Signal Transduction in Fibroblasts. IDENTIFICATION OF A PUTATIVE REPRESSOR ASSOCIATED WITH Arnt.
K. Gradin, R. Toftgard, L. Poellinger, and A. Berghard (1999)
J. Biol. Chem. 274, 13511-13518
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Evidence That the Co-chaperone p23 Regulates Ligand Responsiveness of the Dioxin (Aryl Hydrocarbon) Receptor.
A. Kazlauskas, L. Poellinger, and I. Pongratz (1999)
J. Biol. Chem. 274, 13519-13524
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D Chilov, G Camenisch, I Kvietikova, U Ziegler, M Gassmann, and R. Wenger (1999)
J. Cell Sci. 112, 1203-1212
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Ah Receptor and NF-kappa B Interactions, a Potential Mechanism for Dioxin Toxicity.
Y. Tian, S. Ke, Michael. S. Denison, A. B. Rabson, and M. A. Gallo (1999)
J. Biol. Chem. 274, 510-515
   Abstract »    Full Text »    PDF »
General applicability of chicken egg yolk antibodies: the performance of IgY immunoglobulins raised against the hypoxia-inducible factor 1{alpha}.
G. Camenisch, M. Tini, D. Chilov, I. Kvietikova, V. Srinivas, J. Caro, P. Spielmann, R. H. Wenger, and M. Gassmann (1999)
FASEB J 13, 81-88
   Abstract »    Full Text »
Identification of a novel mechanism of regulation of Ah (dioxin) receptor function.
J. Mimura, M. Ema, K. Sogawa, and Y. Fujii-Kuriyama (1999)
Genes & Dev. 13, 20-25
   Abstract »    Full Text »
Lipopolysaccharide Activation of Murine Splenocytes and Splenic B Cells Increased the Expression of Aryl Hydrocarbon Receptor and Aryl Hydrocarbon Receptor Nuclear Translocator.
R. S. Marcus, M. P. Holsapple, and N. E. Kaminski (1998)
J. Pharmacol. Exp. Ther. 287, 1113-1118
   Abstract »    Full Text »
The Aryl Hydrocarbon Receptor Interacts with Transcription Factor IIB.
H. I. Swanson and J.-H. Yang (1998)
Mol. Pharmacol. 54, 671-677
   Abstract »    Full Text »
Temporal, spatial, and oxygen-regulated expression of hypoxia-inducible factor-1 in the lung.
A. Y. Yu, M. G. Frid, L. A. Shimoda, C. M. Wiener, K. Stenmark, and G. L. Semenza (1998)
Am J Physiol Lung Cell Mol Physiol 275, L818-L826
   Abstract »    Full Text »    PDF »
Structure and Expression of the Mouse AhR Nuclear Translocator (mArnt) Gene.
F. Wang, J.-x. Gao, J. Mimura, A. Kobayashi, K. Sogawa, and Y. Fujii-Kuriyama (1998)
J. Biol. Chem. 273, 24867-24873
   Abstract »    Full Text »    PDF »
Mechanisms of Ligand-Induced Aryl Hydrocarbon Receptor-Mediated Biochemical and Toxic Responses.
C. L. Wilson and S. Safe (1998)
Toxicol Pathol 26, 657-671
   Abstract »    PDF »
A Direct Interaction between the Aryl Hydrocarbon Receptor and Retinoblastoma Protein. LINKING DIOXIN SIGNALING TO THE CELL CYCLE.
N.-L. Ge and C. J. Elferink (1998)
J. Biol. Chem. 273, 22708-22713
   Abstract »    Full Text »    PDF »
Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway.
L. E. Huang, J. Gu, M. Schau, and H. F. Bunn (1998)
PNAS 95, 7987-7992
   Abstract »    Full Text »    PDF »
Role of the PAS Domain in Regulation of Dimerization and DNA Binding Specificity of the Dioxin Receptor.
I. Pongratz, C. Antonsson, M. L. Whitelaw, and L. Poellinger (1998)
Mol. Cell. Biol. 18, 4079-4088
   Abstract »    Full Text »    PDF »
Photoactive yellow protein: A structural prototype for the three-dimensional fold of the PAS domain superfamily.
J.-L. Pellequer, K. A. Wager-Smith, S. A. Kay, and E. D. Getzoff (1998)
PNAS 95, 5884-5890
   Abstract »    Full Text »    PDF »
The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors.
J. B. Hogenesch, Y.-Z. Gu, S. Jain, and C. A. Bradfield (1998)
PNAS 95, 5474-5479
   Abstract »    Full Text »    PDF »
Insect juvenile hormone resistance gene homology with the bHLH-PAS family of transcriptional regulators.
M. Ashok, C. Turner, and T. G. Wilson (1998)
PNAS 95, 2761-2766
   Abstract »    Full Text »    PDF »
Caenorhabditis elegans orthologs of the aryl hydrocarbon receptor and its heterodimerization partner the aryl hydrocarbon receptor nuclear translocator.
J. A. Powell-Coffman, C. A. Bradfield, and W. B. Wood (1998)
PNAS 95, 2844-2849
   Abstract »    Full Text »    PDF »
Control of cell lineage-specific development and transcription by bHLH-PAS proteins.
S. T. Crews (1998)
Genes & Dev. 12, 607-620
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