Evidence map›Paper›PMID 40055333›Full record

ArticleNature communications2025

Copper is essential for cyclin B1-mediated CDK1 activation.

Jiaru Wang, Dian Yang, Hai-Fan Yu, Jing Jin, Yuzhe Nie, Sihua Zhang, Weiwei Ren, Zihan Ge, Zhuo Zhang, Xinghong Ma and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. [Molecular imaging and biology · 2026
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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

13 authors.

Jiaru Wang *Laboratory of Cell Biology, College of Life Science, Northeast Forestry University, Harbin, 150040, China.
Dian Yang *Laboratory of Cell Biology, College of Life Science, Northeast Forestry University, Harbin, 150040, China.
Hai-Fan Yu *Laboratory of Cell Biology, College of Life Science, Northeast Forestry University, Harbin, 150040, China.ORCID http://orcid.org/0000-0002-0418-8800
Jing JinLaboratory of Cell Biology, College of Life Science, Northeast Forestry University, Harbin, 150040, China.
Yuzhe NieLaboratory of Cell Biology, College of Life Science, Northeast Forestry University, Harbin, 150040, China.
Sihua ZhangLaboratory of Cell Biology, College of Life Science, Northeast Forestry University, Harbin, 150040, China.
Weiwei RenDevelopment Center of Plant Germplasm Resources, College of Life Sciences, Shanghai Normal University, Shanghai, 200234, China.
Zihan GeLaboratory of Cell Biology, College of Life Science, Northeast Forestry University, Harbin, 150040, China.
Zhuo ZhangLaboratory of Cell Biology, College of Life Science, Northeast Forestry University, Harbin, 150040, China.
Xinghong MaCollege of Life Science, Northeast Agricultural University, Harbin, 150030, China.
Shaojun DaiDevelopment Center of Plant Germplasm Resources, College of Life Sciences, Shanghai Normal University, Shanghai, 200234, China.
Guangchao SuiLaboratory of Cell Biology, College of Life Science, Northeast Forestry University, Harbin, 150040, China.ORCID http://orcid.org/0000-0002-8164-5585
Chun-Bo TengLaboratory of Cell Biology, College of Life Science, Northeast Forestry University, Harbin, 150040, China. chunboteng@nefu.edu.cn.ORCID http://orcid.org/0000-0001-9103-035X

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32072801National Natural Science Foundation of China (National Science Foundation of China) U22A20369
6 · The paper itself

Abstract

Cyclin-dependent kinase 1 (CDK1) is the pivotal kinase responsible for initiating cell division. Its activation is dependent on binding to regulatory cyclins, such as CCNB1. Our research demonstrates that copper binding to both CDK1 and CCNB1 is essential for activating CDK1 in cells. Mutations in the copper-binding amino acids of either CDK1 or CCNB1 do not disrupt their interaction but are unable to activate CDK1. We also reveal that CCNB1 facilitates the transfer of copper from ATOX1 to CDK1, consequently activating its kinase function. Disruption of copper transfer through the ATOX1-CCNB1-CDK1 pathway can impede CDK1 activation and halt cell cycle progression. In summary, our findings elucidate a mechanism through which copper promotes CDK1 activation and the G2/M transition in the cell cycle. These results could provide insight into the acquisition of proliferative properties associated with increased copper levels in cancer and offer targets for cancer therapy.

Indexed as

CDC2 Protein KinaseCopperCyclin B1Cell CycleCopper Transport ProteinsEnzyme ActivationHEK293 CellsHeLa CellsHumansProtein BindingCCNB1 protein, humanCDC2 Protein KinaseCDK1 protein, humanCopperCopper Transport ProteinsCyclin B1

Identifiers

PMID40055333
PMCPMC11889272

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.