Evidence map›Paper›PMID 31586112›Full record

ArticleScientific reports2019

TFEB activates Nrf2 by repressing its E3 ubiquitin ligase DCAF11 and promoting phosphorylation of p62.

Jee-Yun Park, Sunhyo Kim, Hee Young Sohn, Young Ho Koh, Chulman Jo

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 57 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

5 authors at 1 institution in 1 country.

Jee-Yun ParkDivision of Brain Diseases, Center for Biomedical Science, Korea National Institute of Health, 187 Osongsaengmyeong 2-ro, Osong-eup, Cheongju-si, Chungcheongbuk-do, 28159, Korea.
Sunhyo KimDivision of Brain Diseases, Center for Biomedical Science, Korea National Institute of Health, 187 Osongsaengmyeong 2-ro, Osong-eup, Cheongju-si, Chungcheongbuk-do, 28159, Korea.
Hee Young SohnDivision of Brain Diseases, Center for Biomedical Science, Korea National Institute of Health, 187 Osongsaengmyeong 2-ro, Osong-eup, Cheongju-si, Chungcheongbuk-do, 28159, Korea.
Young Ho KohDivision of Brain Diseases, Center for Biomedical Science, Korea National Institute of Health, 187 Osongsaengmyeong 2-ro, Osong-eup, Cheongju-si, Chungcheongbuk-do, 28159, Korea.
Chulman JoDivision of Brain Diseases, Center for Biomedical Science, Korea National Institute of Health, 187 Osongsaengmyeong 2-ro, Osong-eup, Cheongju-si, Chungcheongbuk-do, 28159, Korea. chulman67@gmail.com.
Korea National Institute of Health · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcriptional factor EB (TFEB) and nuclear factor E2-related factor 2 (Nrf2) play crucial roles in the biological response against cellular stressors; however, their relationship has not yet been investigated. Here, we constructed human neuroglioma cell lines stably expressing TFEB. The expression of Nrf2-response genes, including heme oxygenase (HO)-1, glutathione-s-transferase-mu1 (GSTM1), and p62, was induced in the cell line, independent of oxidative stress. Of note, the protein level of Nrf2 was significantly increased, and its ubiquitinated fraction was reduced in stable cells compared to that in the control cells. Among E3 ubiquitin ligases known to be involved in the ubiquitination of Nrf2, DDB1 and Cullin4 associated factor 11 (DCAF11) was down-regulated at both protein and mRNA levels in stable cells, indicating that the repression of DCAF11 by TFEB may be mainly involved in the stabilization of Nrf2. In addition, the level of phosphorylated p62 at S349 was highly increased in stable cells compared to that in control cells, which could allow it to interfere with the association of Keap1 and Nrf2, thus stabilizing Nrf2. We suggest for the first time that TFEB could activate Nrf2 by increasing its stability under conditions devoid of oxidative stress.

Indexed as

Basic Helix-Loop-Helix Leucine Zipper Transcription FactorsCell Line, TumorDown-RegulationHEK293 CellsHumansNF-E2-Related Factor 2PhosphorylationProtein StabilityRNA-Binding ProteinsUbiquitinationUbiquitin-Protein Ligase ComplexesBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsDDB1 and CUL4 associated factor 11, humanNFE2L2 protein, humanNF-E2-Related Factor 2P62 protein, humanRNA-Binding ProteinsTFEB protein, humanUbiquitin-Protein Ligase Complexes

Identifiers

PMID31586112
PMCPMC6778067
OpenAlexW2978903241

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.