Evidence map›Paper›PMID 28416634›Full record

ArticleMolecular and cellular biology2017

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

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular and cellular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.0field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed, 63 citations in OpenAlex.

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  14. AhR and Wnt/β-Catenin Signaling Pathways and Their Interplay.Current issues in molecular biology · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 3 countries.

Sandra Luecke-JohanssonDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden Sandra.Luecke@ki.se Katarina.Gradin@ki.se.
Michael GrallaDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.
Helene RundqvistDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.
Jolene Caifeng HoCancer Science Institute of Singapore, National University of Singapore, Singapore, Singapore.
Randall S JohnsonDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.
Katarina GradinDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden Sandra.Luecke@ki.se Katarina.Gradin@ki.se.
Lorenz PoellingerDepartment of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.
Karolinska Institutet · SENational University Cancer Institute, Singapore · SGUniversity of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AnimalsAryl Hydrocarbon Receptor Nuclear TranslocatorBreast NeoplasmsEstrogen Receptor alphaFemaleGene Expression Regulation, NeoplasticHumansMiceMice, SCIDReceptors, Aryl HydrocarbonSignal TransductionTranscriptional ActivationTranscription FactorsTumor Cells, CulturedUbiquitin-Protein LigasesXenograft Model Antitumor AssaysARNT protein, humanAryl Hydrocarbon Receptor Nuclear TranslocatorESR1 protein, humanEstrogen Receptor alphaReceptors, Aryl HydrocarbonTranscription FactorsUbiquitin-Protein Ligasesaryl hydrocarbon receptoraryl hydrocarbon receptor nuclear translocatoraryl hydrocarbon receptor repressorE3 ubiquitin ligasemolecular switchtranscription factor

Identifiers

PMID28416634
PMCPMC5472827
OpenAlexW2606250554

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.