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Molecular Pharmacology

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Research ArticleArticle

Aryl Hydrocarbon Receptor (AhR)/AhR Nuclear Translocator (ARNT) Activity Is Unaltered by Phosphorylation of a Periodicity/ARNT/Single-Minded (PAS)-Region Serine Residue

Steven L. Levine and Gary H. Perdew
Molecular Pharmacology March 2001, 59 (3) 557-566; DOI: https://doi.org/10.1124/mol.59.3.557
Steven L. Levine
Department of Veterinary Science and Center for Molecular Toxicology and Carcinogenesis, The Pennsylvania State University, University Park, Pennsylvania
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Gary H. Perdew
Department of Veterinary Science and Center for Molecular Toxicology and Carcinogenesis, The Pennsylvania State University, University Park, Pennsylvania
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Abstract

The aryl hydrocarbon nuclear translocator (ARNT) protein belongs to the family of basic helix-loop-helix (HLH)-periodicity/ARNT/single-minded [Per/ARNT/Sim (PAS)] transcription factors and regulates a range of cellular processes by either homodimerizing or heterodimerizing with other basic HLH-PAS proteins. To date, it has been shown that both the HLH and PAS domains are required for aryl hydrocarbon receptor (AhR) ARNT heterodimerization and that phosphorylation of ARNT is also required for this heterodimerization. Presently, regulation of ARNT with respect to phosphorylation is poorly understood. In an earlier study, murine ARNT was shown to be a phosphoprotein, to display charge heterogeneity, and to have a shift in its predominant isoforms after heterodimerization with the AhR. It was hypothesized that this shift may represent a change in ARNT phosphorylation status. Metabolic [32P]orthophosphate labeling of human ARNT-transfected COS-1 cells, in conjunction with phosphoamino acid analysis, Edman degradation, and phosphopeptide mapping, demonstrated that ARNT is predominantly phosphorylated on serine residues and that serine 348 (S348) in the PAS domain is phosphorylated. Alanine and glutamic acid substitutions were used to demonstrate that loss of phosphorylation at this site did not influence AhR-mediated xenobiotic response elements-driven or ARNT-mediated class B E-box–driven signaling. Additionally, the phosphorylation pattern of ARNT was unaltered after AhR heterodimerization. Although phosphorylation of S348 did not modulate AhR-ARNT or ARNT-ARNT signaling, phosphorylation of this PAS-region serine residue may be important in other ARNT-mediated gene expression systems.

Footnotes

    • Received August 9, 2000.
    • Accepted November 20, 2000.
  • Send reprint requests to: Dr. Gary H. Perdew, Center for Molecular Toxicology, Department of Veterinary Science, Pennsylvania State University, 226 Fenske Lab, University Park, PA 16802. E-mail:ghp2{at}psu.edu

  • This work was supported by the National Institute of Environmental Health Science Grants ES04869, ES09272, and ES05863.

  • The American Society for Pharmacology and Experimental Therapeutics
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Molecular Pharmacology: 59 (3)
Molecular Pharmacology
Vol. 59, Issue 3
1 Mar 2001
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Research ArticleArticle

Aryl Hydrocarbon Receptor (AhR)/AhR Nuclear Translocator (ARNT) Activity Is Unaltered by Phosphorylation of a Periodicity/ARNT/Single-Minded (PAS)-Region Serine Residue

Steven L. Levine and Gary H. Perdew
Molecular Pharmacology March 1, 2001, 59 (3) 557-566; DOI: https://doi.org/10.1124/mol.59.3.557

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Research ArticleArticle

Aryl Hydrocarbon Receptor (AhR)/AhR Nuclear Translocator (ARNT) Activity Is Unaltered by Phosphorylation of a Periodicity/ARNT/Single-Minded (PAS)-Region Serine Residue

Steven L. Levine and Gary H. Perdew
Molecular Pharmacology March 1, 2001, 59 (3) 557-566; DOI: https://doi.org/10.1124/mol.59.3.557
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