Evidence map›Paper›PMID 33562118›Full record

ArticleInternational journal of molecular sciences2021

The Aryl Hydrocarbon Receptor Undergoes Chaperone-Mediated Autophagy in Triple-Negative Breast Cancer Cells.

Jinyun Chen, Yujie Yang, Wade A Russu, William K Chan

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

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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

4 authors at 1 institution in 1 country.

Jinyun ChenDepartment of Pharmaceutics & Medicinal Chemistry, Thomas J. Long School of Pharmacy, University of the Pacific, Stockton, CA 95211, USA.
Yujie YangDepartment of Pharmaceutics & Medicinal Chemistry, Thomas J. Long School of Pharmacy, University of the Pacific, Stockton, CA 95211, USA.
Wade A RussuDepartment of Pharmaceutics & Medicinal Chemistry, Thomas J. Long School of Pharmacy, University of the Pacific, Stockton, CA 95211, USA.
William K ChanDepartment of Pharmaceutics & Medicinal Chemistry, Thomas J. Long School of Pharmacy, University of the Pacific, Stockton, CA 95211, USA.
University of the Pacific · US

Funding

Investigating the molecular mechanisms in controlling the aryl hydrocarbon receptor protein levelsR15ES023104 · NIEHS · UNIVERSITY OF THE PACIFIC-STOCKTON · PI CHAN, WILLIAM K · 2014 to 2019
$750k
NIEHS NIH HHS R15 ES023104NIH HHS 2R15ES023104
6 · The paper itself

Abstract

The aryl hydrocarbon receptor (AHR) is a ligand-activated signaling molecule expressed in many cell types, including triple-negative and non-triple-negative breast cancer cells. It affects breast cancer growth and crosstalk with estrogen receptor signaling. Normally, this receptor is degraded shortly after ligand activation via the 26S proteasome. Here, we report that AHR undergoes chaperone-mediated autophagy in MDA-MB-468 triple-negative breast cancer cells. This lysosomal degradation of AHR exhibits the following characteristics: (1) it is triggered by 6 amino-nicotinamide, starvation, and piperazinylpyrimidine compound Q18; (2) it is not observed in non-triple-negative breast cancer cells (MCF-7, T47D, and MDA-MB-361); (3) it can be inhibited by progesterone receptor B but not estrogen receptor alpha; (4) it can be reversed by chloroquine but not MG132; (5) it requires LAMP2A; and (6) it involves AHR-HSC70 and AHR-LAMP2A interactions. The NEKFF sequence localized at amino acid 558 of human AHR appears to be a KFERQ-like motif of chaperone-mediated autophagy, responsible for the LAMP2A-mediated AHR protein degradation.

Indexed as

ProteolysisAmino Acid SequenceBasic Helix-Loop-Helix ProteinsCell Line, TumorChaperone-Mediated AutophagyChloroquineCytochrome P-450 CYP1A1Estrogen Receptor alphaHumansLeupeptinsLysosomal-Associated Membrane Protein 2LysosomesMCF-7 CellsReceptors, Aryl HydrocarbonReceptors, ProgesteroneRNA InterferenceAHR protein, humanBasic Helix-Loop-Helix Proteinsbenzyloxycarbonylleucyl-leucyl-leucine aldehydeChloroquineCYP1A1 protein, humanCytochrome P-450 CYP1A1ESR1 protein, humanEstrogen Receptor alphaLAMP2 protein, humanLeupeptinsLysosomal-Associated Membrane Protein 2progesterone receptor BReceptors, Aryl HydrocarbonReceptors, Progesteronearyl hydrocarbon receptorchaperone-mediated autophagyCMA motifLAMP2Aprotein degradation

Identifiers

PMID33562118
PMCPMC7914569
OpenAlexW3128211453

What OpenQuestion holds

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LicenceCC BY
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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.