Aryl hydrocarbon receptor nuclear translocator: Difference between revisions

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{{Infobox_gene}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The '''ARNT''' [[gene]] encodes the '''aryl hydrocarbon receptor nuclear translocator''' [[protein]] that forms a complex with ligand-bound [[aryl hydrocarbon receptor]] (AhR), and is required for receptor function. The encoded protein has also been identified as the beta subunit of a heterodimeric transcription factor, [[hypoxia-inducible factor]] 1 (HIF1). A t(1;12)(q21;p13) translocation, which results in a TEL-ARNT [[fusion protein]], is associated with [[leukemia|acute myeloblastic leukemia]]. Three alternatively spliced variants encoding different isoforms have been described for this gene.
{{GNF_Protein_box
 
| image = PBB_Protein_ARNT_image.jpg
The aryl hydrocarbon receptor (AhR) is involved in the induction of several [[enzyme]]s that participate in [[xenobiotic]] metabolism. The ligand-free, [[cytosolic]] form of the [[aryl hydrocarbon receptor]] is complexed to [[Hsp90|heat shock protein 90]]. Binding of ligand, which includes [[dioxins and dioxin-like compounds|dioxin]] and polycyclic [[aromatic hydrocarbon]]s, results in translocation of the ligand-binding subunit only to the nucleus. Induction of enzymes involved in xenobiotic metabolism occurs through binding of the ligand-bound AhR to xenobiotic responsive elements in the promoters of genes for these enzymes.
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1x0o.
 
| PDB = {{PDB2|1x0o}}, {{PDB2|2a24}}, {{PDB2|2b02}}
== Interactions ==
| Name = Aryl hydrocarbon receptor nuclear translocator
| HGNCid = 700
| Symbol = ARNT
| AltSymbols =; HIF-1beta; HIF1B; HIF1BETA; TANGO
| OMIM = 126110
| ECnumber = 
| Homologene = 1261
| MGIid = 88071
| GeneAtlas_image1 = PBB_GE_ARNT_218221_at_tn.png
| GeneAtlas_image2 = PBB_GE_ARNT_210828_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ARNT_218222_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005061 |text = aryl hydrocarbon receptor nuclear translocator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000060 |text = protein import into nucleus, translocation}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 405
    | Hs_Ensembl = ENSG00000143437
    | Hs_RefseqProtein = NP_001659
    | Hs_RefseqmRNA = NM_001668
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 149048810
    | Hs_GenLoc_end = 149115837
    | Hs_Uniprot = P27540
    | Mm_EntrezGene = 11863
    | Mm_Ensembl = ENSMUSG00000015522
    | Mm_RefseqmRNA = NM_001037737
    | Mm_RefseqProtein = NP_001032826
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 95519792
    | Mm_GenLoc_end = 95581692
    | Mm_Uniprot = Q3U7X2
  }}
}}


The '''ARNT''' [[gene]] encodes the '''aryl hydrocarbon receptor nuclear translocator''' [[protein]] that forms a complex with ligand-bound [[aryl hydrocarbon receptor]] (AhR), and is required for receptor function. The encoded protein has also been identified as the beta subunit of a heterodimeric transcription factor, [[hypoxia-inducible factor]] 1 (HIF1). A t(1;12)(q21;p13) translocation, which results in a TEL-ARNT [[fusion protein]], is associated with [[leukemia|acute myeloblastic leukemia]]. Three alternatively spliced variants encoding different isoforms have been described for this gene.
Aryl hydrocarbon receptor nuclear translocator has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[AIP (gene)|AIP]],<ref name = pmid9111057>{{cite journal | vauthors = Carver LA, Bradfield CA | title = Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo | journal = J. Biol. Chem. | volume = 272 | issue = 17 | pages = 11452–6 | date = April 1997 | pmid = 9111057 | doi = 10.1074/jbc.272.17.11452 }}</ref><ref name = pmid11259606>{{cite journal | vauthors = Kazlauskas A, Sundström S, Poellinger L, Pongratz I | title = The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor | journal = Mol. Cell. Biol. | volume = 21 | issue = 7 | pages = 2594–607 | date = April 2001 | pmid = 11259606 | pmc = 86890 | doi = 10.1128/MCB.21.7.2594-2607.2001 }}</ref>
* [[Aryl hydrocarbon receptor|AHR]],<ref name = pmid7628454>{{cite journal | vauthors = Lindebro MC, Poellinger L, Whitelaw ML | title = Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex | journal = EMBO J. | volume = 14 | issue = 14 | pages = 3528–39 | date = July 1995 | pmid = 7628454 | pmc = 394421 | doi =  }}</ref><ref name = pmid8384309>{{cite journal | vauthors = Whitelaw M, Pongratz I, Wilhelmsson A, Gustafsson JA, Poellinger L | title = Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor | journal = Mol. Cell. Biol. | volume = 13 | issue = 4 | pages = 2504–14 | date = April 1993 | pmid = 8384309 | pmc = 359572 | doi =  }}</ref><ref name = pmid7488247>{{cite journal | vauthors = Yamaguchi Y, Kuo MT | title = Functional analysis of aryl hydrocarbon receptor nuclear translocator interactions with aryl hydrocarbon receptor in the yeast two-hybrid system | journal = Biochem. Pharmacol. | volume = 50 | issue = 8 | pages = 1295–302 | date = October 1995 | pmid = 7488247 | doi = 10.1016/0006-2952(95)02016-6 }}</ref><ref name = pmid9887096>{{cite journal | vauthors = Mimura J, Ema M, Sogawa K, Fujii-Kuriyama Y | title = Identification of a novel mechanism of regulation of Ah (dioxin) receptor function | journal = Genes Dev. | volume = 13 | issue = 1 | pages = 20–5 | date = January 1999 | pmid = 9887096 | pmc = 316371 | doi = 10.1101/gad.13.1.20 }}</ref>
* [[EPAS1]],<ref name = pmid9079689/>
* [[HIF1A]],<ref name = pmid9079689>{{cite journal | vauthors = Hogenesch JB, Chan WK, Jackiw VH, Brown RC, Gu YZ, Pray-Grant M, Perdew GH, Bradfield CA | title = Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway | journal = J. Biol. Chem. | volume = 272 | issue = 13 | pages = 8581–93 | date = March 1997 | pmid = 9079689 | doi = 10.1074/jbc.272.13.8581 }}</ref><ref name = pmid11782478>{{cite journal | vauthors = Woods SL, Whitelaw ML | title = Differential activities of murine single minded 1 (SIM1) and SIM2 on a hypoxic response element. Cross-talk between basic helix-loop-helix/per-Arnt-Sim homology transcription factors | journal = J. Biol. Chem. | volume = 277 | issue = 12 | pages = 10236–43 | date = March 2002 | pmid = 11782478 | doi = 10.1074/jbc.M110752200 }}</ref>
* [[Nuclear receptor coactivator 2|NCOA2]],<ref name = pmid12024042/><ref name = pmid12024042>{{cite journal | vauthors = Beischlag TV, Wang S, Rose DW, Torchia J, Reisz-Porszasz S, Muhammad K, Nelson WE, Probst MR, Rosenfeld MG, Hankinson O | title = Recruitment of the NCoA/SRC-1/p160 family of transcriptional coactivators by the aryl hydrocarbon receptor/aryl hydrocarbon receptor nuclear translocator complex | journal = Mol. Cell. Biol. | volume = 22 | issue = 12 | pages = 4319–33 | date = June 2002 | pmid = 12024042 | pmc = 133867 | doi = 10.1128/mcb.22.12.4319-4333.2002 }}</ref>
* [[SIM1]],<ref name = pmid11782478/><ref name = pmid9020169>{{cite journal | vauthors = Probst MR, Fan CM, Tessier-Lavigne M, Hankinson O | title = Two murine homologs of the Drosophila single-minded protein that interact with the mouse aryl hydrocarbon receptor nuclear translocator protein | journal = J. Biol. Chem. | volume = 272 | issue = 7 | pages = 4451–7 | date = February 1997 | pmid = 9020169 | doi = 10.1074/jbc.272.7.4451 }}</ref> and
* [[SIM2]].<ref name = pmid11782478/><ref name = pmid9020169/><ref name = pmid14701734>{{cite journal | vauthors = Ooe N, Saito K, Mikami N, Nakatuka I, Kaneko H | title = Identification of a novel basic helix-loop-helix-PAS factor, NXF, reveals a Sim2 competitive, positive regulatory role in dendritic-cytoskeleton modulator drebrin gene expression | journal = Mol. Cell. Biol. | volume = 24 | issue = 2 | pages = 608–16 | date = January 2004 | pmid = 14701734 | pmc = 343817 | doi = 10.1128/mcb.24.2.608-616.2004 }}</ref><ref name = pmid9271372>{{cite journal | vauthors = Moffett P, Reece M, Pelletier J | title = The murine Sim-2 gene product inhibits transcription by active repression and functional interference | journal = Mol. Cell. Biol. | volume = 17 | issue = 9 | pages = 4933–47 | date = September 1997 | pmid = 9271372 | pmc = 232345 | doi =  10.1128/mcb.17.9.4933}}</ref>
{{Div col end}}


The aryl hydrocarbon receptor (AhR) is involved in the induction of several [[enzyme]]s that participate in [[xenobiotic]] metabolism. The ligand-free, [[cytosolic]] form of the [[aryl hydrocarbon receptor]] is complexed to [[Hsp90|heat shock protein 90]]. Binding of ligand, which includes dioxin and polycyclic [[aromatic hydrocarbon]]s, results in translocation of the ligand-binding subunit only to the nucleus. Induction of enzymes involved in xenobiotic metabolism occurs through binding of the ligand-bound AhR to xenobiotic responsive elements in the promoters of genes for these enzymes.
== References ==
{{Reflist}}


==References==
== Further reading ==
{{reflist|2}}
{{Refbegin | 2}}
==Further reading==
* {{cite journal | vauthors = Haase VH | title = Hypoxia-inducible factors in the kidney. | journal = Am. J. Physiol. Renal Physiol. | volume = 291 | issue = 2 | pages = F271–81 | year = 2006 | pmid = 16554418 | doi = 10.1152/ajprenal.00071.2006 }}
{{refbegin | 2}}
* {{cite journal | vauthors = Reyes H, Reisz-Porszasz S, Hankinson O | title = Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor. | journal = Science | volume = 256 | issue = 5060 | pages = 1193–5 | year = 1992 | pmid = 1317062 | doi = 10.1126/science.256.5060.1193 }}
{{PBB_Further_reading
* {{cite journal | vauthors = Hoffman EC, Reyes H, Chu FF, Sander F, Conley LH, Brooks BA, Hankinson O | title = Cloning of a factor required for activity of the Ah (dioxin) receptor. | journal = Science | volume = 252 | issue = 5008 | pages = 954–8 | year = 1991 | pmid = 1852076 | doi = 10.1126/science.1852076 }}
| citations =
* {{cite journal | vauthors = Yamaguchi Y, Kuo MT | title = Functional analysis of aryl hydrocarbon receptor nuclear translocator interactions with aryl hydrocarbon receptor in the yeast two-hybrid system. | journal = Biochem. Pharmacol. | volume = 50 | issue = 8 | pages = 1295–302 | year = 1995 | pmid = 7488247 | doi = 10.1016/0006-2952(95)02016-6 }}
*{{cite journal | author=Haase VH |title=Hypoxia-inducible factors in the kidney. |journal=Am. J. Physiol. Renal Physiol. |volume=291 |issue= 2 |pages= F271-81 |year= 2006 |pmid= 16554418 |doi= 10.1152/ajprenal.00071.2006 }}
* {{cite journal | vauthors = Wang GL, Jiang BH, Rue EA, Semenza GL | title = Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 92 | issue = 12 | pages = 5510–4 | year = 1995 | pmid = 7539918 | pmc = 41725 | doi = 10.1073/pnas.92.12.5510 }}
*{{cite journal | author=Reyes H, Reisz-Porszasz S, Hankinson O |title=Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor. |journal=Science |volume=256 |issue= 5060 |pages= 1193-5 |year= 1992 |pmid= 1317062 |doi= }}
* {{cite journal | vauthors = Lindebro MC, Poellinger L, Whitelaw ML | title = Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex. | journal = EMBO J. | volume = 14 | issue = 14 | pages = 3528–39 | year = 1995 | pmid = 7628454 | pmc = 394421 | doi =  }}
*{{cite journal | author=Hoffman EC, Reyes H, Chu FF, ''et al.'' |title=Cloning of a factor required for activity of the Ah (dioxin) receptor. |journal=Science |volume=252 |issue= 5008 |pages= 954-8 |year= 1991 |pmid= 1852076 |doi= }}
* {{cite journal | vauthors = Abbott BD, Probst MR, Perdew GH | title = Immunohistochemical double-staining for Ah receptor and ARNT in human embryonic palatal shelves. | journal = Teratology | volume = 50 | issue = 5 | pages = 361–6 | year = 1995 | pmid = 7716743 | doi = 10.1002/tera.1420500507 }}
*{{cite journal | author=Yamaguchi Y, Kuo MT |title=Functional analysis of aryl hydrocarbon receptor nuclear translocator interactions with aryl hydrocarbon receptor in the yeast two-hybrid system. |journal=Biochem. Pharmacol. |volume=50 |issue= 8 |pages= 1295-302 |year= 1995 |pmid= 7488247 |doi= }}
* {{cite journal | vauthors = Reisz-Porszasz S, Probst MR, Fukunaga BN, Hankinson O | title = Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT). | journal = Mol. Cell. Biol. | volume = 14 | issue = 9 | pages = 6075–86 | year = 1994 | pmid = 8065341 | pmc = 359134 | doi = 10.1128/mcb.14.9.6075 }}
*{{cite journal | author=Wang GL, Jiang BH, Rue EA, Semenza GL |title=Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 12 |pages= 5510-4 |year= 1995 |pmid= 7539918 |doi= }}
* {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. | journal = Gene | volume = 138 | issue = 1-2 | pages = 171–4 | year = 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
*{{cite journal | author=Lindebro MC, Poellinger L, Whitelaw ML |title=Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex. |journal=EMBO J. |volume=14 |issue= 14 |pages= 3528-39 |year= 1995 |pmid= 7628454 |doi=  }}
* {{cite journal | vauthors = Johnson B, Brooks BA, Heinzmann C, Diep A, Mohandas T, Sparkes RS, Reyes H, Hoffman E, Lange E, Gatti RA | title = The Ah receptor nuclear translocator gene (ARNT) is located on q21 of human chromosome 1 and on mouse chromosome 3 near Cf-3. | journal = Genomics | volume = 17 | issue = 3 | pages = 592–8 | year = 1993 | pmid = 8244375 | doi = 10.1006/geno.1993.1377 }}
*{{cite journal | author=Abbott BD, Probst MR, Perdew GH |title=Immunohistochemical double-staining for Ah receptor and ARNT in human embryonic palatal shelves. |journal=Teratology |volume=50 |issue= 5 |pages= 361-6 |year= 1995 |pmid= 7716743 |doi= 10.1002/tera.1420500507 }}
* {{cite journal | vauthors = Whitelaw M, Pongratz I, Wilhelmsson A, Gustafsson JA, Poellinger L | title = Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor. | journal = Mol. Cell. Biol. | volume = 13 | issue = 4 | pages = 2504–14 | year = 1993 | pmid = 8384309 | pmc = 359572 | doi =  }}
*{{cite journal | author=Reisz-Porszasz S, Probst MR, Fukunaga BN, Hankinson O |title=Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT). |journal=Mol. Cell. Biol. |volume=14 |issue= 9 |pages= 6075-86 |year= 1994 |pmid= 8065341 |doi= }}
* {{cite journal | vauthors = Jiang BH, Rue E, Wang GL, Roe R, Semenza GL | title = Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1. | journal = J. Biol. Chem. | volume = 271 | issue = 30 | pages = 17771–8 | year = 1996 | pmid = 8663540 | doi = 10.1074/jbc.271.30.17771 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
* {{cite journal | vauthors = Rowlands JC, McEwan IJ, Gustafsson JA | title = Trans-activation by the human aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator proteins: direct interactions with basal transcription factors. | journal = Mol. Pharmacol. | volume = 50 | issue = 3 | pages = 538–48 | year = 1996 | pmid = 8794892 | doi =  }}
*{{cite journal | author=Johnson B, Brooks BA, Heinzmann C, ''et al.'' |title=The Ah receptor nuclear translocator gene (ARNT) is located on q21 of human chromosome 1 and on mouse chromosome 3 near Cf-3. |journal=Genomics |volume=17 |issue= 3 |pages= 592-8 |year= 1993 |pmid= 8244375 |doi= }}
* {{cite journal | vauthors = Ema M, Morita M, Ikawa S, Tanaka M, Matsuda Y, Gotoh O, Saijoh Y, Fujii H, Hamada H, Kikuchi Y, Fujii-Kuriyama Y | title = Two new members of the murine Sim gene family are transcriptional repressors and show different expression patterns during mouse embryogenesis. | journal = Mol. Cell. Biol. | volume = 16 | issue = 10 | pages = 5865–75 | year = 1996 | pmid = 8927054 | pmc = 231588 | doi =  }}
*{{cite journal | author=Whitelaw M, Pongratz I, Wilhelmsson A, ''et al.'' |title=Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor. |journal=Mol. Cell. Biol. |volume=13 |issue= 4 |pages= 2504-14 |year= 1993 |pmid= 8384309 |doi=  }}
* {{cite journal | vauthors = Swanson HI, ((Yang Jh)) | title = Mapping the protein/DNA contact sites of the Ah receptor and Ah receptor nuclear translocator. | journal = J. Biol. Chem. | volume = 271 | issue = 49 | pages = 31657–65 | year = 1997 | pmid = 8940186 | doi = 10.1074/jbc.271.49.31657 }}
*{{cite journal | author=Jiang BH, Rue E, Wang GL, ''et al.'' |title=Dimerization, DNA binding, and transactivation properties of hypoxia-inducible factor 1. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 17771-8 |year= 1996 |pmid= 8663540 |doi= }}
* {{cite journal | vauthors = Probst MR, Fan CM, Tessier-Lavigne M, Hankinson O | title = Two murine homologs of the Drosophila single-minded protein that interact with the mouse aryl hydrocarbon receptor nuclear translocator protein. | journal = J. Biol. Chem. | volume = 272 | issue = 7 | pages = 4451–7 | year = 1997 | pmid = 9020169 | doi = 10.1074/jbc.272.7.4451 }}
*{{cite journal | author=Rowlands JC, McEwan IJ, Gustafsson JA |title=Trans-activation by the human aryl hydrocarbon receptor and aryl hydrocarbon receptor nuclear translocator proteins: direct interactions with basal transcription factors. |journal=Mol. Pharmacol. |volume=50 |issue= 3 |pages= 538-48 |year= 1996 |pmid= 8794892 |doi=  }}
* {{cite journal | vauthors = Hogenesch JB, Chan WK, Jackiw VH, Brown RC, Gu YZ, Pray-Grant M, Perdew GH, Bradfield CA | title = Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway. | journal = J. Biol. Chem. | volume = 272 | issue = 13 | pages = 8581–93 | year = 1997 | pmid = 9079689 | doi = 10.1074/jbc.272.13.8581 }}
*{{cite journal | author=Ema M, Morita M, Ikawa S, ''et al.'' |title=Two new members of the murine Sim gene family are transcriptional repressors and show different expression patterns during mouse embryogenesis. |journal=Mol. Cell. Biol. |volume=16 |issue= 10 |pages= 5865-75 |year= 1996 |pmid= 8927054 |doi=  }}
* {{cite journal | vauthors = Carver LA, Bradfield CA | title = Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo. | journal = J. Biol. Chem. | volume = 272 | issue = 17 | pages = 11452–6 | year = 1997 | pmid = 9111057 | doi = 10.1074/jbc.272.17.11452 }}
*{{cite journal | author=Swanson HI, Yang J |title=Mapping the protein/DNA contact sites of the Ah receptor and Ah receptor nuclear translocator. |journal=J. Biol. Chem. |volume=271 |issue= 49 |pages= 31657-65 |year= 1997 |pmid= 8940186 |doi= }}
* {{cite journal | vauthors = Ema M, Taya S, Yokotani N, Sogawa K, Matsuda Y, Fujii-Kuriyama Y | title = A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 94 | issue = 9 | pages = 4273–8 | year = 1997 | pmid = 9113979 | pmc = 20712 | doi = 10.1073/pnas.94.9.4273 }}
*{{cite journal | author=Probst MR, Fan CM, Tessier-Lavigne M, Hankinson O |title=Two murine homologs of the Drosophila single-minded protein that interact with the mouse aryl hydrocarbon receptor nuclear translocator protein. |journal=J. Biol. Chem. |volume=272 |issue= 7 |pages= 4451-7 |year= 1997 |pmid= 9020169 |doi= }}
* {{cite journal | vauthors = Moffett P, Reece M, Pelletier J | title = The murine Sim-2 gene product inhibits transcription by active repression and functional interference. | journal = Mol. Cell. Biol. | volume = 17 | issue = 9 | pages = 4933–47 | year = 1997 | pmid = 9271372 | pmc = 232345 | doi =  10.1128/mcb.17.9.4933}}
*{{cite journal | author=Hogenesch JB, Chan WK, Jackiw VH, ''et al.'' |title=Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8581-93 |year= 1997 |pmid= 9079689 |doi= }}
{{Refend}}
*{{cite journal | author=Carver LA, Bradfield CA |title=Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 11452-6 |year= 1997 |pmid= 9111057 |doi= }}
*{{cite journal | author=Ema M, Taya S, Yokotani N, ''et al.'' |title=A novel bHLH-PAS factor with close sequence similarity to hypoxia-inducible factor 1alpha regulates the VEGF expression and is potentially involved in lung and vascular development. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 9 |pages= 4273-8 |year= 1997 |pmid= 9113979 |doi= }}
*{{cite journal | author=Moffett P, Reece M, Pelletier J |title=The murine Sim-2 gene product inhibits transcription by active repression and functional interference. |journal=Mol. Cell. Biol. |volume=17 |issue= 9 |pages= 4933-47 |year= 1997 |pmid= 9271372 |doi=  }}
}}
{{refend}}


==External links==
== External links ==
* {{MeshName|Aryl+Hydrocarbon+Receptor+Nuclear+Translocator}}
* {{MeshName|Aryl+Hydrocarbon+Receptor+Nuclear+Translocator}}
{{PDB Gallery|geneid=405}}
{{Transcription factors|g1}}


{{NLM content}}
{{NLM content}}
{{protein-stub}}
 
{{Transcription factors}}
[[Category:Transcription factors]]
[[Category:Transcription factors]]
[[Category:PAS-domain-containing proteins]]
[[Category:Oncogenes]]

Revision as of 17:38, 5 December 2017

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Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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The ARNT gene encodes the aryl hydrocarbon receptor nuclear translocator protein that forms a complex with ligand-bound aryl hydrocarbon receptor (AhR), and is required for receptor function. The encoded protein has also been identified as the beta subunit of a heterodimeric transcription factor, hypoxia-inducible factor 1 (HIF1). A t(1;12)(q21;p13) translocation, which results in a TEL-ARNT fusion protein, is associated with acute myeloblastic leukemia. Three alternatively spliced variants encoding different isoforms have been described for this gene.

The aryl hydrocarbon receptor (AhR) is involved in the induction of several enzymes that participate in xenobiotic metabolism. The ligand-free, cytosolic form of the aryl hydrocarbon receptor is complexed to heat shock protein 90. Binding of ligand, which includes dioxin and polycyclic aromatic hydrocarbons, results in translocation of the ligand-binding subunit only to the nucleus. Induction of enzymes involved in xenobiotic metabolism occurs through binding of the ligand-bound AhR to xenobiotic responsive elements in the promoters of genes for these enzymes.

Interactions

Aryl hydrocarbon receptor nuclear translocator has been shown to interact with:

References

  1. ↑ Carver LA, Bradfield CA (April 1997). "Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel immunophilin homolog in vivo". J. Biol. Chem. 272 (17): 11452–6. doi:10.1074/jbc.272.17.11452. PMID 9111057.
  2. ↑ Kazlauskas A, Sundström S, Poellinger L, Pongratz I (April 2001). "The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor". Mol. Cell. Biol. 21 (7): 2594–607. doi:10.1128/MCB.21.7.2594-2607.2001. PMC 86890. PMID 11259606.
  3. ↑ Lindebro MC, Poellinger L, Whitelaw ML (July 1995). "Protein-protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor-Arnt transcription factor complex". EMBO J. 14 (14): 3528–39. PMC 394421. PMID 7628454.
  4. ↑ Whitelaw M, Pongratz I, Wilhelmsson A, Gustafsson JA, Poellinger L (April 1993). "Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor". Mol. Cell. Biol. 13 (4): 2504–14. PMC 359572. PMID 8384309.
  5. ↑ Yamaguchi Y, Kuo MT (October 1995). "Functional analysis of aryl hydrocarbon receptor nuclear translocator interactions with aryl hydrocarbon receptor in the yeast two-hybrid system". Biochem. Pharmacol. 50 (8): 1295–302. doi:10.1016/0006-2952(95)02016-6. PMID 7488247.
  6. ↑ Mimura J, Ema M, Sogawa K, Fujii-Kuriyama Y (January 1999). "Identification of a novel mechanism of regulation of Ah (dioxin) receptor function". Genes Dev. 13 (1): 20–5. doi:10.1101/gad.13.1.20. PMC 316371. PMID 9887096.
  7. ↑ 7.0 7.1 Hogenesch JB, Chan WK, Jackiw VH, Brown RC, Gu YZ, Pray-Grant M, Perdew GH, Bradfield CA (March 1997). "Characterization of a subset of the basic-helix-loop-helix-PAS superfamily that interacts with components of the dioxin signaling pathway". J. Biol. Chem. 272 (13): 8581–93. doi:10.1074/jbc.272.13.8581. PMID 9079689.
  8. ↑ 8.0 8.1 8.2 Woods SL, Whitelaw ML (March 2002). "Differential activities of murine single minded 1 (SIM1) and SIM2 on a hypoxic response element. Cross-talk between basic helix-loop-helix/per-Arnt-Sim homology transcription factors". J. Biol. Chem. 277 (12): 10236–43. doi:10.1074/jbc.M110752200. PMID 11782478.
  9. ↑ 9.0 9.1 Beischlag TV, Wang S, Rose DW, Torchia J, Reisz-Porszasz S, Muhammad K, Nelson WE, Probst MR, Rosenfeld MG, Hankinson O (June 2002). "Recruitment of the NCoA/SRC-1/p160 family of transcriptional coactivators by the aryl hydrocarbon receptor/aryl hydrocarbon receptor nuclear translocator complex". Mol. Cell. Biol. 22 (12): 4319–33. doi:10.1128/mcb.22.12.4319-4333.2002. PMC 133867. PMID 12024042.
  10. ↑ 10.0 10.1 Probst MR, Fan CM, Tessier-Lavigne M, Hankinson O (February 1997). "Two murine homologs of the Drosophila single-minded protein that interact with the mouse aryl hydrocarbon receptor nuclear translocator protein". J. Biol. Chem. 272 (7): 4451–7. doi:10.1074/jbc.272.7.4451. PMID 9020169.
  11. ↑ Ooe N, Saito K, Mikami N, Nakatuka I, Kaneko H (January 2004). "Identification of a novel basic helix-loop-helix-PAS factor, NXF, reveals a Sim2 competitive, positive regulatory role in dendritic-cytoskeleton modulator drebrin gene expression". Mol. Cell. Biol. 24 (2): 608–16. doi:10.1128/mcb.24.2.608-616.2004. PMC 343817. PMID 14701734.
  12. ↑ Moffett P, Reece M, Pelletier J (September 1997). "The murine Sim-2 gene product inhibits transcription by active repression and functional interference". Mol. Cell. Biol. 17 (9): 4933–47. doi:10.1128/mcb.17.9.4933. PMC 232345. PMID 9271372.

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