Evidence map›Paper›PMID 30508698›Full record

ArticleRedox biology2019

Proteasome lid bridges mitochondrial stress with Cdc53/Cullin1 NEDDylation status.

L Bramasole, A Sinha, S Gurevich, M Radzinski, Y Klein, N Panat, E Gefen, T Rinaldi, D Jimenez-Morales, J Johnson and 5 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Redox biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Csn5 Depletion Reverses Mitochondrial Defects in GCN5-NullInternational journal of molecular sciences · 2025
    Article
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  7. Article
  8. Biomolecules · 2021
    Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

15 authors at 5 institutions in 3 countries.

L BramasoleDepartment of Human Biology, The Faculty of Natural Sciences, University of Haifa, Haifa 3190500, Israel; Department of Biology and Environment, The Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 3600600, Israel.
A SinhaDepartment of Biology and Environment, The Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 3600600, Israel.
S GurevichDepartment of Biology, Technion-Israel Institute of Technology, 3200000 Haifa, Israel.
M RadzinskiDepartment of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Safra Campus Givat Ram, The Hebrew University of Jerusalem, Jerusalem 9190400, Israel.
Y KleinDepartment of Biology and Environment, The Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 3600600, Israel.
N PanatDepartment of Biology and Environment, The Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 3600600, Israel.
E GefenDepartment of Biology and Environment, The Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 3600600, Israel.
T RinaldiDepartment of Biology and Biotechnology, University of Rome ''La Sapienza'', Rome 00185, Italy.
D Jimenez-MoralesQuantitative Biosciences Institute (QBI), University of California, San Francisco, San Francisco, CA, USA; Department of Cellular and Molecular Pharmacology, University of California San Francisco, San Francisco, CA, USA.
J JohnsonQuantitative Biosciences Institute (QBI), University of California, San Francisco, San Francisco, CA, USA; Department of Cellular and Molecular Pharmacology, University of California San Francisco, San Francisco, CA, USA.
N J KroganQuantitative Biosciences Institute (QBI), University of California, San Francisco, San Francisco, CA, USA; Department of Cellular and Molecular Pharmacology, University of California San Francisco, San Francisco, CA, USA.
N ReisDepartment of Biology, Technion-Israel Institute of Technology, 3200000 Haifa, Israel.
D ReichmannDepartment of Biological Chemistry, The Alexander Silberman Institute of Life Sciences, Safra Campus Givat Ram, The Hebrew University of Jerusalem, Jerusalem 9190400, Israel.
M H GlickmanDepartment of Biology, Technion-Israel Institute of Technology, 3200000 Haifa, Israel.
E PickDepartment of Human Biology, The Faculty of Natural Sciences, University of Haifa, Haifa 3190500, Israel; Department of Biology and Environment, The Faculty of Natural Sciences, University of Haifa at Oranim, Tivon 3600600, Israel. Electronic address: elahpic@research.haifa.ac.il.
University of Haifa · ILQB3 · USTechnion – Israel Institute of Technology · ILHebrew University of Jerusalem · ILSapienza University of Rome · IT

Funding

BIOBEHAVIORAL STUDIES OF NARCOTICS ABUSE IN HUMANSK05DA000064 · NIDA · MC LEAN HOSPITAL (BELMONT, MA) · PI MENDELSON, JACK H · 1985 to 2007
$911k
NIDA NIH HHS K05 DA000064
6 · The paper itself

Abstract

Cycles of Cdc53/Cullin1 rubylation (a.k.a NEDDylation) protect ubiquitin-E3 SCF (Skp1-Cullin1-F-box protein) complexes from self-destruction and play an important role in mediating the ubiquitination of key protein substrates involved in cell cycle progression, development, and survival. Cul1 rubylation is balanced by the COP9 signalosome (CSN), a multi-subunit derubylase that shows 1:1 paralogy to the 26S proteasome lid. The turnover of SCF substrates and their relevance to various diseases is well studied, yet, the extent by which environmental perturbations influence Cul1 rubylation/derubylation cycles per se is still unclear. In this study, we show that the level of cellular oxidation serves as a molecular switch, determining Cullin1 rubylation/derubylation ratio. We describe a mutant of the proteasome lid subunit, Rpn11 that exhibits accumulated levels of Cullin1-Rub1 conjugates, a characteristic phenotype of csn mutants. By dissecting between distinct phenotypes of rpn11 mutants, proteasome and mitochondria dysfunction, we were able to recognize the high reactive oxygen species (ROS) production during the transition of cells into mitochondrial respiration, as a checkpoint of Cullin1 rubylation in a reversible manner. Thus, the study adds the rubylation cascade to the list of cellular pathways regulated by redox homeostasis.

Indexed as

Stress, PhysiologicalCell RespirationCullin ProteinsMitochondriaModels, BiologicalProteasome Endopeptidase ComplexReactive Oxygen SpeciesUbiquitin-Activating EnzymesUbiquitinationCullin 1Cullin ProteinsProteasome Endopeptidase ComplexReactive Oxygen SpeciesUbiquitin-Activating Enzymes26S proteasomeMitochondriaNEDD8/Rub1Rpn11Thiol switchUbiquitin

Identifiers

PMID30508698
PMCPMC6279957
OpenAlexW2900487899

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.