Evidence map›Paper›PMID 39316746›Full record

ArticleAutophagy2024

PLK2-mediated phosphorylation of SQSTM1 S349 promotes aggregation of polyubiquitinated proteins upon proteasomal dysfunction.

Yun-Da Chen, Xiu-Ping Lin, Zi-Lun Ruan, Mi Li, Xue-Mei Yi, Xu Zhang, Shu Li, Hong-Bing Shu

Abstract read
In one paragraph

Article in Autophagy, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. 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

8 authors.

Yun-Da ChenDepartment of Infectious Diseases, Medical Research Institute, Zhongnan Hospital of Wuhan University, College of Life Sciences, Wuhan, China.
Xiu-Ping LinDepartment of Infectious Diseases, Medical Research Institute, Zhongnan Hospital of Wuhan University, College of Life Sciences, Wuhan, China.
Zi-Lun RuanDepartment of Infectious Diseases, Medical Research Institute, Zhongnan Hospital of Wuhan University, College of Life Sciences, Wuhan, China.
Mi LiDepartment of Infectious Diseases, Medical Research Institute, Zhongnan Hospital of Wuhan University, College of Life Sciences, Wuhan, China.
Xue-Mei YiDepartment of Infectious Diseases, Medical Research Institute, Zhongnan Hospital of Wuhan University, College of Life Sciences, Wuhan, China.
Xu ZhangDepartment of Infectious Diseases, Medical Research Institute, Zhongnan Hospital of Wuhan University, College of Life Sciences, Wuhan, China.
Shu LiDepartment of Infectious Diseases, Medical Research Institute, Zhongnan Hospital of Wuhan University, College of Life Sciences, Wuhan, China.
Hong-Bing ShuDepartment of Infectious Diseases, Medical Research Institute, Zhongnan Hospital of Wuhan University, College of Life Sciences, Wuhan, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dysregulation in protein homeostasis results in accumulation of protein aggregates, which are sequestered into dedicated insoluble compartments so-called inclusion bodies or aggresomes, where they are scavenged through different mechanisms to reduce proteotoxicity. The protein aggregates can be selectively scavenged by macroautophagy/autophagy called aggrephagy, which is mediated by the autophagic receptor SQSTM1. In this study, we have identified PLK2 as an important regulator of SQSTM1-mediated aggregation of polyubiquitinated proteins. PLK2 is upregulated following proteasome inhibition, and then associates with and phosphorylates SQSTM1 at S349. The phosphorylation of SQSTM1 S349 strengthens its binding to KEAP1, which is required for formation of large SQSTM1 aggregates/bodies upon proteasome inhibition. Our findings suggest that PLK2-mediated phosphorylation of SQSTM1 S349 represents a critical regulatory mechanism in SQSTM1-mediated aggregation of polyubiquitinated proteins.

Indexed as

Proteasome Endopeptidase ComplexProtein AggregatesProtein Serine-Threonine KinasesSequestosome-1 ProteinAutophagyHEK293 CellsHumansKelch-Like ECH-Associated Protein 1PhosphorylationProtein BindingUbiquitinated ProteinsUbiquitinationKEAP1 protein, humanKelch-Like ECH-Associated Protein 1Proteasome Endopeptidase ComplexProtein AggregatesProtein Serine-Threonine KinasesSequestosome-1 ProteinSQSTM1 protein, humanUbiquitinated ProteinsPhosphorylationPLK2polyubiquitinationproteasomeprotein aggregationSQSTM1/p62

Identifiers

PMID39316746
PMCPMC11423667

What Socratic holds

Textmetadata
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 Socratic graph.