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Research Article

A Molecular Mechanism To Switch the Aryl Hydrocarbon Receptor from a Transcription Factor to an E3 Ubiquitin Ligase

Sandra Luecke-Johansson, Michael Gralla, Helene Rundqvist, Jolene Caifeng Ho, Randall S. Johnson, Katarina Gradin, Lorenz Poellinger
Sandra Luecke-Johansson
aDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden
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Michael Gralla
aDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden
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Helene Rundqvist
aDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden
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Jolene Caifeng Ho
cCancer Science Institute of Singapore, National University of Singapore, Singapore, Singapore
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Randall S. Johnson
aDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden
bDepartment of Physiology, Development and Neuroscience, University of Cambridge, Cambridge, United Kingdom
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Katarina Gradin
aDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden
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Lorenz Poellinger
aDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden
cCancer Science Institute of Singapore, National University of Singapore, Singapore, Singapore
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DOI: 10.1128/MCB.00630-16
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ABSTRACT

The aryl hydrocarbon receptor (AhR) is a ligand-activated transcription factor that is known as a mediator of toxic responses. Recently, it was shown that the AhR has dual functions. Besides being a transcription factor, it also possesses an intrinsic E3 ubiquitin ligase function that targets, e.g., the steroid receptors for proteasomal degradation. The aim of this study was to identify the molecular switch that determines whether the AhR acts as a transcription factor or an E3 ubiquitin ligase. To do this, we used the breast cancer cell line MCF7, which expresses a functional estrogen receptor alpha (ERα) signaling pathway. Our data suggest that aryl hydrocarbon receptor nuclear translocator (ARNT) plays an important role in the modulation of the dual functions of the AhR. ARNT knockdown dramatically impaired the transcriptional activation properties of the ligand-activated AhR but did not affect its E3 ubiquitin ligase function. The availability of ARNT itself is modulated by another basic helix-loop-helix (bHLH)–Per-ARNT-SIM (PAS) protein, the repressor of AhR function (AhRR). MCF7 cells overexpressing the AhRR showed lower ERα protein levels, reduced responsiveness to estradiol, and reduced growth rates. Importantly, when these cells were used to produce estrogen-dependent xenograft tumors in SCID mice, we also observed lower ERα protein levels and a reduced tumor mass, implying a tumor-suppressive-like function of the AhR in MCF7 xenograft tumors.

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A Molecular Mechanism To Switch the Aryl Hydrocarbon Receptor from a Transcription Factor to an E3 Ubiquitin Ligase
Sandra Luecke-Johansson, Michael Gralla, Helene Rundqvist, Jolene Caifeng Ho, Randall S. Johnson, Katarina Gradin, Lorenz Poellinger
Molecular and Cellular Biology Jun 2017, 37 (13) e00630-16; DOI: 10.1128/MCB.00630-16

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A Molecular Mechanism To Switch the Aryl Hydrocarbon Receptor from a Transcription Factor to an E3 Ubiquitin Ligase
Sandra Luecke-Johansson, Michael Gralla, Helene Rundqvist, Jolene Caifeng Ho, Randall S. Johnson, Katarina Gradin, Lorenz Poellinger
Molecular and Cellular Biology Jun 2017, 37 (13) e00630-16; DOI: 10.1128/MCB.00630-16
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KEYWORDS

aryl hydrocarbon receptor nuclear translocator
Breast Neoplasms
Estrogen Receptor alpha
Receptors, Aryl Hydrocarbon
transcription factors
Ubiquitin-Protein Ligases
aryl hydrocarbon receptor
molecular switch
E3 ubiquitin ligase
transcription factor
aryl hydrocarbon receptor nuclear translocator
aryl hydrocarbon receptor repressor

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