Evidence map›Paper›PMID 25600778›Full record

ArticleNature communications2015

The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates.

Daichi Morimoto, Erik Walinda, Harumi Fukada, Yu-Shin Sou, Shun Kageyama, Masaru Hoshino, Takashi Fujii, Hikaru Tsuchiya, Yasushi Saeki, Kyohei Arita and 7 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

45 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Article
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  4. An edge β-strand mutation turns ubiquitin into a pore-forming amyloid.Protein science : a publication of the Protein Society · 2026
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  8. Article
  9. Review
  10. Review
  11. Suppressing UBE2N ameliorates Alzheimer's disease pathology through the clearance of amyloid beta.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024
    Article
  12. Article
  13. P-NADs:Heliyon · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. TheActa biochimica et biophysica Sinica · 2023
    Article
  20. 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

17 authors at 6 institutions in 1 country.

Daichi MorimotoDepartment of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-Ku, Kyoto 615-8510, Japan.
Erik WalindaDepartment of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-Ku, Kyoto 615-8510, Japan.
Harumi FukadaGraduate School of Life and Environmental Sciences, Osaka Prefecture University, Naka-ku, Sakai, Osaka 599-8531, Japan.
Yu-Shin SouProtein Metabolism Project, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan.
Shun Kageyama1] Protein Metabolism Project, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan [2] Department of Biochemistry, School of Medicine, Niigata University, Chuo-ku, Niigata 951-8510, Japan.
Masaru HoshinoGraduate School of Pharmaceutical Sciences, Kyoto University, 46-29 Yoshida-Shimoadachi, Sakyo-ku, Kyoto 606-8501, Japan.
Takashi FujiiQuantitative Biology Center, RIKEN, 1-3 OLABB, Osaka University 6-2-3, Furuedai, Suita, Osaka 565-0874, Japan.
Hikaru TsuchiyaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan.
Yasushi SaekiLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan.
Kyohei AritaGraduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.
Mariko AriyoshiDepartment of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-Ku, Kyoto 615-8510, Japan.
Hidehito TochioDepartment of Biophysics, Graduate School of Science, Kyoto University, Oiwake-cho, Kitashirakawa, Sakyo-Ku, Kyoto 606-8502, Japan.
Kazuhiro IwaiGraduate School of Medicine, Kyoto University, Yoshida-Konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.
Keiichi Namba1] Quantitative Biology Center, RIKEN, 1-3 OLABB, Osaka University 6-2-3, Furuedai, Suita, Osaka 565-0874, Japan [2] Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan.
Masaaki Komatsu1] Protein Metabolism Project, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan [2] Department of Biochemistry, School of Medicine, Niigata University, Chuo-ku, Niigata 951-8510, Japan.
Keiji TanakaLaboratory of Protein Metabolism, Tokyo Metropolitan Institute of Medical Science, Setagaya-ku, Tokyo 156-8506, Japan.
Masahiro ShirakawaDepartment of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-Ku, Kyoto 615-8510, Japan.
Tokyo Metropolitan Institute of Medical Science · JPKyoto University · JPKyoto Katsura Hospital · JPOsaka University · JPOsaka Prefecture University · JPYokohama City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin is known to be one of the most soluble and stably folded intracellular proteins, but it is often found in inclusion bodies associated with various diseases including neurodegenerative disorders and cancer. To gain insight into this contradictory behaviour, we have examined the physicochemical properties of ubiquitin and its polymeric chains that lead to aggregate formation. We find that the folding stability of ubiquitin chains unexpectedly decreases with increasing chain length, resulting in the formation of amyloid-like fibrils. Furthermore, when expressed in cells, polyubiquitin chains covalently linked to EGFP also form aggregates depending on chain length. Notably, these aggregates are selectively degraded by autophagy. We propose a novel model in which the physical and chemical instability of polyubiquitin chains drives the formation of fibrils, which then serve as an initiation signal for autophagy.

Indexed as

AnimalsAutophagyCalorimetry, Differential ScanningCircular DichroismEscherichia coliImmunohistochemistryMiceMicroscopy, Electron, TransmissionPolyubiquitinSf9 CellsSpectrometry, FluorescenceUbiquitinPolyubiquitinUbiquitin

Identifiers

PMID25600778
PMCPMC4309437
OpenAlexW2064085066

What OpenQuestion holds

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Registered trials

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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.