Evidence map›Paper›PMID 32242037›Full record

ArticleScientific reports2020

Cell cycle-dependent localization of the proteasome to chromatin.

Yuki Kito, Masaki Matsumoto, Atsushi Hatano, Tomoyo Takami, Kiyotaka Oshikawa, Akinobu Matsumoto, Keiichi I Nakayama

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
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  7. Proteasome dynamics in response to metabolic changes.Frontiers in cell and developmental biology · 2025
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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

7 authors at 3 institutions in 1 country.

Yuki KitoDivision of Cell Biology and Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Masaki MatsumotoDivision of Proteomics, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan. masakim@med.niigata-u.ac.jp.
Atsushi HatanoYCI Laboratory for Trans-Omics, Young Chief Investigator Program, RIKEN Center for Integrative Medical Sciences, Kanagawa, Japan.
Tomoyo TakamiDepartment of Omics and Systems Biology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.
Kiyotaka OshikawaDepartment of Omics and Systems Biology, Niigata University Graduate School of Medical and Dental Sciences, Niigata, Japan.
Akinobu MatsumotoDivision of Cell Biology and Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Keiichi I NakayamaDivision of Cell Biology and Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan. nakayak1@bioreg.kyushu-u.ac.jp.
Kyushu University · JPNiigata University · JPRIKEN Center for Integrative Medical Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An integrative understanding of nuclear events including transcription in normal and cancer cells requires comprehensive and quantitative measurement of protein dynamics that underlie such events. However, the low abundance of most nuclear proteins hampers their detailed functional characterization. We have now comprehensively quantified the abundance of nuclear proteins with the use of proteomics approaches in both normal and transformed human diploid fibroblasts. We found that subunits of the 26S proteasome complex were markedly down-regulated in the nuclear fraction of the transformed cells compared with that of the wild-type cells. The intranuclear proteasome abundance appeared to be inversely related to the rate of cell cycle progression, with restraint of the cell cycle being associated with an increase in the amount of proteasome subunits in the nucleus, suggesting that the nuclear proteasome content is dependent on the cell cycle. Furthermore, chromatin enrichment for proteomics (ChEP) analysis revealed enrichment of the proteasome in the chromatin fraction of quiescent cells and its apparent dissociation from chromatin in transformed cells. Our results thus suggest that translocation of the nuclear proteasome to chromatin may play an important role in control of the cell cycle and oncogenesis through regulation of chromatin-associated transcription factors.

Indexed as

Cell CycleAnimalsChromatinDown-RegulationHumansMiceNIH 3T3 CellsProteasome Endopeptidase ComplexProtein TransportProteomeATP dependent 26S proteaseChromatinProteasome Endopeptidase ComplexProteome

Identifiers

PMID32242037
PMCPMC7118148
OpenAlexW3014479432

What OpenQuestion holds

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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.