Evidence map›Paper›PMID 29855490›Full record

ArticleScientific reports2018

Expression and Regulation of Deubiquitinase-Resistant, Unanchored Ubiquitin Chains in Drosophila.

Jessica R Blount, Kozeta Libohova, Gregory B Marsh, Joanna R Sutton, Sokol V Todi

Abstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Cells · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Unanchored Ubiquitin Chains, Revisited.Frontiers in cell and developmental biology · 2020
    Review
  11. Article
  12. Article
  13. 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

5 authors.

Jessica R BlountDepartment of Pharmacology, Wayne State University School of Medicine, Detroit, MI, USA.
Kozeta LibohovaDepartment of Pharmacology, Wayne State University School of Medicine, Detroit, MI, USA.
Gregory B MarshDepartment of Pharmacology, Wayne State University School of Medicine, Detroit, MI, USA.
Joanna R SuttonDepartment of Pharmacology, Wayne State University School of Medicine, Detroit, MI, USA.
Sokol V TodiDepartment of Pharmacology, Wayne State University School of Medicine, Detroit, MI, USA. stodi@wayne.edu.

Funding

Protection against Alzheimer's Disease proteins by novel ubiquitin processesR01NS086778 · NINDS · WAYNE STATE UNIVERSITY · PI Sokol Todi · 2014 to 2026
$4.9M
Mechanisms to suppress polyglutamine-dependent toxicity in Machado-Joseph DiseaseF31NS095575 · NINDS · WAYNE STATE UNIVERSITY · PI SUTTON, JOANNA · 2015 to 2017
$108k
NINDS NIH HHS F31 NS095575NINDS NIH HHS R01 NS086778
6 · The paper itself

Abstract

The modifier protein, ubiquitin (Ub) regulates various cellular pathways by controlling the fate of substrates to which it is conjugated. Ub moieties are also conjugated to each other, forming chains of various topologies. In cells, poly-Ub is attached to proteins and also exists in unanchored form. Accumulation of unanchored poly-Ub is thought to be harmful and quickly dispersed through dismantling by deubiquitinases (DUBs). We wondered whether disassembly by DUBs is necessary to control unanchored Ub chains in vivo. We generated Drosophila melanogaster lines that express Ub chains non-cleavable into mono-Ub by DUBs. These chains are rapidly modified with different linkages and represent various types of unanchored species. We found that unanchored poly-Ub is not devastating in Drosophila, under normal conditions or during stress. The DUB-resistant, free Ub chains are degraded by the proteasome, at least in part through the assistance of VCP and its cofactor, p47. Also, unanchored poly-Ub that cannot be cleaved by DUBs can be conjugated en bloc, in vivo. Our results indicate that unanchored poly-Ub species need not be intrinsically toxic; they can be controlled independently of DUB-based disassembly by being degraded, or through conjugation onto other proteins.

Indexed as

Amino Acid SequenceAnimalsDeubiquitinating EnzymesDrosophila melanogasterDrosophila ProteinsGene ExpressionHEK293 CellsHeLa CellsHumansPolyubiquitinTransgenesUbiquitinUbiquitinationDeubiquitinating EnzymesDrosophila ProteinsPolyubiquitinUbiquitin

Identifiers

PMID29855490
PMCPMC5981470

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.