Evidence map›Paper›PMID 37943017›Full record

ArticleeLife2023

Multiple cullin-associated E3 ligases regulate cyclin D1 protein stability.

Ke Lu, Ming Zhang, Guizheng Wei, Guozhi Xiao, Liping Tong, Di Chen

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Induced proximity-based therapeutic modalities.Nature reviews. Drug discovery · 2026
    Review
  2. DDIT3 drives nucleus pulposus cell PANoptosis and intervertebral disc degeneration progression.Apoptosis : an international journal on programmed cell death · 2026
    Article
  3. Article
  4. Review
  5. Cul5bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Article
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

6 authors at 3 institutions in 2 countries.

Ke Lu *Research Center for Computer-aided Drug Discovery, Chinese Academy of Sciences, Shenzhen, China.ORCID 0000-0002-1641-4748
Ming Zhang *Department of Oncology, Johns Hopkins University, Baltimore, United States.
Guizheng WeiResearch Center for Computer-aided Drug Discovery, Chinese Academy of Sciences, Shenzhen, China.ORCID 0009-0006-0479-5076
Guozhi XiaoDepartment of Biochemistry, Southern University of Science and Technology, Shenzhen, China.ORCID 0000-0002-4269-2450
Liping TongResearch Center for Computer-aided Drug Discovery, Chinese Academy of Sciences, Shenzhen, China.
Di ChenResearch Center for Computer-aided Drug Discovery, Chinese Academy of Sciences, Shenzhen, China.ORCID 0000-0002-4258-3457
Chinese Academy of Sciences · CNJohns Hopkins University · USSouthern University of Science and Technology · CN

Funding

National Key Research and Development Program of China 2021YFB3800800National Natural Science Foundation of China 82030067National Natural Science Foundation of China 82161160342National Natural Science Foundation of China 82172397National Natural Science Foundation of China 82250710174
6 · The paper itself

Abstract

Cyclin D1 is a key regulator of cell cycle progression, which forms a complex with CDK4/6 to regulate G1/S transition during cell cycle progression. Cyclin D1 has been recognized as an oncogene since it was upregulated in several different types of cancers. It is known that the post-translational regulation of cyclin D1 is controlled by ubiquitination/proteasome degradation system in a phosphorylation-dependent manner. Several cullin-associated F-box E3 ligases have been shown to regulate cyclin D1 degradation; however, it is not known if additional cullin-associated E3 ligases participate in the regulation of cyclin D1 protein stability. In this study, we have screened an siRNA library containing siRNAs specific for 154 ligase subunits, including F-box, SOCS, BTB-containing proteins, and DDB proteins. We found that multiple cullin-associated E3 ligases regulate cyclin D1 activity, including Keap1, DDB2, and WSB2. We found that these E3 ligases interact with cyclin D1, regulate cyclin D1 ubiquitination and proteasome degradation in a phosphorylation-dependent manner. These E3 ligases also control cell cycle progression and cell proliferation through regulation of cyclin D1 protein stability. Our study provides novel insights into the regulatory mechanisms of cyclin D1 protein stability and function.

Indexed as

Cullin ProteinsF-Box ProteinsCyclin D1Kelch-Like ECH-Associated Protein 1NF-E2-Related Factor 2Proteasome Endopeptidase ComplexProtein StabilityUbiquitin-Protein LigasesCullin ProteinsCyclin D1F-Box ProteinsKelch-Like ECH-Associated Protein 1NF-E2-Related Factor 2Proteasome Endopeptidase ComplexUbiquitin-Protein Ligasescell biologycullin-associated E3 ligasecyclin D1DDB2humanKeap1Rbx1WSB2

Identifiers

PMID37943017
PMCPMC10651173
OpenAlexW4388526702

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.