Evidence map›Paper›PMID 40643536›Full record

ReviewCells2025

Post-Translational Modification of p62: Roles and Regulations in Autophagy.

Shuai Xiao, Yeping Yu, Meng Liao, Dandan Song, Xiaozhen Xu, Lingli Tian, Rui Zhang, Hao Lyu, Dong Guo, Qi Zhang and 3 more

Abstract readReview
In one paragraph

Review in Cells, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Review
  2. Lipophagy and lipid droplets in neurodegeneration.Trends in pharmacological sciences · 2026
    Review
  3. Article
  4. Ethanolic Extract ofAntioxidants (Basel, Switzerland) · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. The Roles of SQSTM1/p62 in Selective Autophagy and Oncogenic Signaling.International journal of molecular sciences · 2026
    Review
  10. Article
  11. Programmed cell death in osteoarthritis.Apoptosis : an international journal on programmed cell death · 2026
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
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

13 authors.

Shuai XiaoNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.
Yeping YuNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.
Meng LiaoNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.
Dandan SongNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.
Xiaozhen XuNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.
Lingli TianNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.
Rui ZhangNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.
Hao LyuNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.
Dong GuoNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.
Qi ZhangNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.ORCID 0000-0003-3878-9441
Xing-Zhen ChenMembrane Protein Disease Research Group, Department of Physiology, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, AB T6G 2R3, Canada.
Cefan ZhouNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.ORCID 0000-0003-0680-3843
Jingfeng TangNational "111" Center for Cellular Regulation and Molecular Pharmaceutics, Hubei University of Technology, Wuhan 430068, China.ORCID 0000-0002-5524-4518

Funding

Doctoral Start-up Foundation of Hubei University of Technology XJ2022003901Hubei Natural Science Foundation of China 2024AFB218National Key R&D Program of China 2023YFC2507904National Natural Science Foundation of China 32070726National Natural Science Foundation of China 32270768National Natural Science Foundation of China 82273970National Natural Science Foundation of China 82370715Science and Technology Talent Program of Hubei 2024DJA037
6 · The paper itself

Abstract

Autophagy is a highly conserved cellular process that plays a crucial role in maintaining cellular homeostasis by degrading damaged organelles, misfolded proteins, and other cellular components. p62/SQSTM1 functions as a selective autophagy receptor by binding polyubiquitinated cargo through its UBA domain and linking it to microtubule-associated protein light chain 3 (LC3)-decorated autophagosomes. Moreover, p62 acts as a signaling hub and is essential in response to various stressors, including nutrient deprivation and oxidative stress. Post-translational modifications (PTMs) critically regulate p62's multifaceted roles, controlling p62's phase separation, cargo recruitment, signaling interactions, and autophagic degradation efficiency. The dysregulation of p62 PTMs is closely related to the occurrence and development of human diseases, particularly neurodegenerative disorders and certain cancers. This review summarizes the main PTM events of p62 discovered to date that influence the autophagy process, including phosphorylation, acetylation, ubiquitination, and S-acylation, as well as their known contributions to protein aggregation and disease. The PTMs of p62 dynamically regulate autophagy, protein aggregation, and cellular signaling, underscoring its importance as a potential therapeutic target and biomarker for these diseases.

Indexed as

AutophagyProtein Processing, Post-TranslationalSequestosome-1 ProteinAcetylationAnimalsHumansPhosphorylationSignal TransductionUbiquitinationSequestosome-1 ProteinSQSTM1 protein, humanautophagyoligomerizationp62post-translational modifications

Identifiers

PMID40643536
PMCPMC12249475

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.