Evidence map›Paper›PMID 36810259›Full record

ArticleCell & bioscience2023

Enhanced liquidity of p62 droplets mediated by Smurf1 links Nrf2 activation and autophagy.

Qin Xia, Yang Li, Wanting Xu, Chengwei Wu, Hanfei Zheng, Liqun Liu, Lei Dong

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

Article in Cell & bioscience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

20 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
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  6. The Roles of SQSTM1/p62 in Selective Autophagy and Oncogenic Signaling.International journal of molecular sciences · 2026
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  18. SMURF1/2 Are Novel Regulators of WNK1 Stability.Kinases and phosphatases · 2024
    Article
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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 1 institution in 1 country.

Qin Xia *School of Life Science, Beijing Institute of Technology, No. 5, South Street, Zhongguancun, Haidian District, Beijing, China.
Yang Li *School of Life Science, Beijing Institute of Technology, No. 5, South Street, Zhongguancun, Haidian District, Beijing, China.
Wanting XuSchool of Life Science, Beijing Institute of Technology, No. 5, South Street, Zhongguancun, Haidian District, Beijing, China.
Chengwei WuSchool of Life Science, Beijing Institute of Technology, No. 5, South Street, Zhongguancun, Haidian District, Beijing, China.
Hanfei ZhengSchool of Life Science, Beijing Institute of Technology, No. 5, South Street, Zhongguancun, Haidian District, Beijing, China.
Liqun LiuSchool of Life Science, Beijing Institute of Technology, No. 5, South Street, Zhongguancun, Haidian District, Beijing, China.
Lei DongSchool of Life Science, Beijing Institute of Technology, No. 5, South Street, Zhongguancun, Haidian District, Beijing, China. ldong@bit.edu.cn.ORCID http://orcid.org/0000-0001-7530-7427
Beijing Institute of Technology · CN

Funding

Beijing Institute of Technology Research Fund Program for Young Scholars XSQD-202110002National Natural Science Foundation of China 81870123National Natural Science Foundation of China U21A20200National Science Foundation for Young Scientists of China 81902545Natural Science Foundation of Beijing Municipality Z190018
6 · The paper itself

Abstract

backgroundMacro-autophagy/Autophagy is an evolutionarily well-conserved recycling process to maintain the balance through precise spatiotemporal regulation. However, the regulatory mechanisms of biomolecular condensates by the key adaptor protein p62 via liquid-liquid phase separation (LLPS) remain obscure.

resultsIn this study, we showed that E3 ligase Smurf1 enhanced Nrf2 activation and promoted autophagy by increasing p62 phase separation capability. Specifically, the Smurf1/p62 interaction improved the formation and material exchange of liquid droplets compared with p62 single puncta. Additionally, Smurf1 promoted the competitive binding of p62 with Keap1 to increase Nrf2 nuclear translocation in p62 Ser349 phosphorylation-dependent manner. Mechanistically, overexpressed Smurf1 increased the activation of mTORC1 (mechanistic target of rapamycin complex 1), in turn leading to p62 Ser349 phosphorylation. Nrf2 activation increased the mRNA levels of Smurf1, p62, and NBR1, further promoting the droplet liquidity to enhance oxidative stress response. Importantly, we showed that Smurf1 maintained cellular homeostasis by promoting cargo degradation through the p62/LC3 autophagic pathway.

conclusionsThese findings revealed the complex interconnected role among Smurf1, p62/Nrf2/NBR1, and p62/LC3 axis in determining Nrf2 activation and subsequent clearance of condensates through LLPS mechanism.

Indexed as

p62-liquid dropletsProtein homeostasisSmurf1

Identifiers

PMID36810259
PMCPMC9945626
OpenAlexW4321611906

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LicenceCC BY
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Registered trials

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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.