Evidence map›Paper›PMID 28536631›Full record

ReviewCellular & molecular biology letters2016

p62 links the autophagy pathway and the ubiqutin-proteasome system upon ubiquitinated protein degradation.

Wei Jing Liu, Lin Ye, Wei Fang Huang, Lin Jie Guo, Zi Gan Xu, Hong Luan Wu, Chen Yang, Hua Feng Liu

Open access · goldAbstract readReview
In one paragraph

Review in Cellular & molecular biology letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 542 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
542citing papers in PubMed, 1 pooled it
31.0field-weighted citation impact, top 1% 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

542 citing papers in PubMed, 1 synthesis or guideline pooled it, 915 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. The histone deacetylase family in health and disease.Signal transduction and targeted therapy · 2026
    Review
  7. Aporphine AlkaloidPharmaceuticals (Basel, Switzerland) · 2026
    Article
  8. Article
  9. Review
  10. Autophagy in MASLD: A Metabolic and Precision Medicine Perspective.Liver international : official journal of the International Association for the Study of the Liver · 2026
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

482 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

Wei Jing Liu *The Institute of Nephrology, Guangdong Medical University, Zhanjiang, Guangdong 524001 China.
Lin Ye *The Institute of Nephrology, Guangdong Medical University, Zhanjiang, Guangdong 524001 China.
Wei Fang HuangThe Institute of Nephrology, Guangdong Medical University, Zhanjiang, Guangdong 524001 China.
Lin Jie GuoThe Institute of Nephrology, Guangdong Medical University, Zhanjiang, Guangdong 524001 China.
Zi Gan XuThe Institute of Nephrology, Guangdong Medical University, Zhanjiang, Guangdong 524001 China.
Hong Luan WuThe Institute of Nephrology, Guangdong Medical University, Zhanjiang, Guangdong 524001 China.
Chen YangThe Institute of Nephrology, Guangdong Medical University, Zhanjiang, Guangdong 524001 China.
Hua Feng LiuThe Institute of Nephrology, Guangdong Medical University, Zhanjiang, Guangdong 524001 China.
Guangdong Medical College · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitin-proteasome system (UPS) and autophagy are two distinct and interacting proteolytic systems. They play critical roles in cell survival under normal conditions and during stress. An increasing body of evidence indicates that ubiquitinated cargoes are important markers of degradation. p62, a classical receptor of autophagy, is a multifunctional protein located throughout the cell and involved in many signal transduction pathways, including the Keap1-Nrf2 pathway. It is involved in the proteasomal degradation of ubiquitinated proteins. When the cellular p62 level is manipulated, the quantity and location pattern of ubiquitinated proteins change with a considerable impact on cell survival. Altered p62 levels can even lead to some diseases. The proteotoxic stress imposed by proteasome inhibition can activate autophagy through p62 phosphorylation. A deficiency in autophagy may compromise the ubiquitin-proteasome system, since overabundant p62 delays delivery of the proteasomal substrate to the proteasome despite proteasomal catalytic activity being unchanged. In addition, p62 and the proteasome can modulate the activity of HDAC6 deacetylase, thus influencing the autophagic degradation.

Indexed as

AutophagyProteasome Endopeptidase ComplexUbiquitinated ProteinsAnimalsHumansSequestosome-1 ProteinSignal TransductionProteasome Endopeptidase ComplexSequestosome-1 ProteinUbiquitinated ProteinsAggresomeAutophagyHistone deacetylase 6 (HDAC6)Keap1–Nrf2 pathwayMechanistic target of rapamycin complex 1 (mTORC1)p62p62 phosphorylationProteostasisUbiquitinated proteinUbiquitin–proteasome system (UPS)

Identifiers

PMID28536631
PMCPMC5415757
OpenAlexW2561943186

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.