Evidence map›Paper›PMID 32123008›Full record

ArticleMolecular and cellular biology2020

NRF3-POMP-20S Proteasome Assembly Axis Promotes Cancer Development via Ubiquitin-Independent Proteolysis of p53 and Retinoblastoma Protein.

Tsuyoshi Waku, Nanami Nakamura, Misaki Koji, Hidenori Watanabe, Hiroki Katoh, Chika Tatsumi, Natsuko Tamura, Atsushi Hatanaka, Shuuhei Hirose, Hiroyuki Katayama and 7 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular and cellular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Review
  3. NFE2L1/Nrf1 forms a coactivator complex post-peptide:Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. New insight into the CNC-bZIP member, NFE2L3, in human diseases.Frontiers in cell and developmental biology · 2024
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
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  18. Review
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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

17 authors at 5 institutions in 1 country.

Tsuyoshi WakuLaboratory for Genetic Code, Department of Medical Life Systems, Faculty of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Nanami Nakamura *Laboratory for Genetic Code, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Misaki Koji *Laboratory for Genetic Code, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Hidenori WatanabeLaboratory for Genetic Code, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Hiroki KatohLaboratory for Genetic Code, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Chika TatsumiLaboratory for Genetic Code, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Natsuko TamuraLaboratory for Genetic Code, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Atsushi HatanakaLaboratory for Genetic Code, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Shuuhei HiroseLaboratory for Genetic Code, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Hiroyuki KatayamaLaboratory for Genetic Code, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Misato TaniLaboratory for Genetic Code, Graduate School of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Yuki KuboLaboratory for Genetic Code, Department of Medical Life Systems, Faculty of Life and Medical Sciences, Doshisha University, Kyoto, Japan.
Jun HamazakiLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Takao HamakuboDepartment of Protein-Protein Interaction Research, Institute for Advanced Medical Sciences, Nippon Medical School, Kanagawa, Japan.
Akira WatanabeDepartment of Life Science Frontiers, Center for iPS Cell Research and Application, Kyoto University, Kyoto, Japan.
Shigeo MurataLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Akira KobayashiLaboratory for Genetic Code, Department of Medical Life Systems, Faculty of Life and Medical Sciences, Doshisha University, Kyoto, Japan akobayas@mail.doshisha.ac.jp.
Doshisha University · JPThe University of Tokyo · JPJapan Society for the Promotion of Science · JPKyoto University · JPNippon Medical School · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteasomes are essential protease complexes that maintain cellular homeostasis, and aberrant proteasomal activity supports cancer development. The regulatory mechanisms and biological function of the ubiquitin-26S proteasome have been studied extensively, while those of the ubiquitin-independent 20S proteasome system remain obscure. Here, we show that the cap 'n' collar (CNC) family transcription factor NRF3 specifically enhances 20S proteasome assembly in cancer cells and that 20S proteasomes contribute to colorectal cancer development through ubiquitin-independent proteolysis of the tumor suppressor p53 and retinoblastoma (Rb) proteins. The

Indexed as

Basic-Leucine Zipper Transcription FactorsHCT116 CellsHeLa CellsHumansMolecular ChaperonesNeoplasmsProteasome Endopeptidase ComplexProteolysisRetinoblastoma ProteinTumor Suppressor Protein p53UbiquitinBasic-Leucine Zipper Transcription FactorsMolecular ChaperonesNFE2L3 protein, humanProteasome Endopeptidase Complexproteasome maturation proteinRetinoblastoma ProteinTP53 protein, humanTumor Suppressor Protein p53Ubiquitin20S proteasome assemblycancer developmentcolorectal cancerNFE2L3NRF3p53POMPRbretinoblastomaTP53ubiquitin-independent proteolysis

Identifiers

PMID32123008
PMCPMC7189095
OpenAlexW3007256515

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.