Evidence map›Paper›PMID 20861518›Full record

ArticleMolecular & cellular proteomics : MCP2011

A novel strategy to isolate ubiquitin conjugates reveals wide role for ubiquitination during neural development.

Maribel Franco, Nicholas T Seyfried, Andrea H Brand, Junmin Peng, Ugo Mayor

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

48 citing papers in PubMed, 105 citations in OpenAlex.

  1. Review
  2. Review
  3. CXXC5 is a ubiquitinated protein and is degraded by the ubiquitin-proteasome pathway.Protein science : a publication of the Protein Society · 2025
    Article
  4. The Ubiquitin Tale: Current Strategies and Future Challenges.ACS pharmacology & translational science · 2024
    Review
  5. Article
  6. Proteomic approaches to study ubiquitinomics.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. The Ubiquitinated Axon: Local Control of Axon Development and Function by Ubiquitin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Review
  12. Article
  13. An Interaction Network of RNA-Binding Proteins Involved inMolecular & cellular proteomics : MCP · 2020
    Article
  14. Resolving the Complexity of Ubiquitin Networks.Frontiers in molecular biosciences · 2020
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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

5 authors at 3 institutions in 3 countries.

Maribel FrancoCIC Biogune, Bizkaia Teknologi Parkea, 48160 Derio, Spain.
Nicholas T Seyfried
Andrea H Brand
Junmin Peng
Ugo Mayor
Ikerbasque · ESCIC bioGUNE · ESEmory University · US

Funding

Analysis of Ubiquitinated ProteomeR21RR025822 · NCRR · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI PENG, JUNMIN · 2009 to 2010
$581k
Cancer Research UKNCRR NIH HHS R21 RR025822NCRR NIH HHS RR025822Wellcome TrustWellcome Trust 068055
6 · The paper itself

Abstract

Ubiquitination has essential roles in neuronal development and function. Ubiquitin proteomics studies on yeast and HeLa cells have proven very informative, but there still is a gap regarding neuronal tissue-specific ubiquitination. In an organism context, direct evidence for the ubiquitination of neuronal proteins is even scarcer. Here, we report a novel proteomics strategy based on the in vivo biotinylation of ubiquitin to isolate ubiquitin conjugates from the neurons of Drosophila melanogaster embryos. We confidently identified 48 neuronal ubiquitin substrates, none of which was yet known to be ubiquitinated. Earlier proteomics and biochemical studies in non-neuronal cell types had identified orthologs to some of those but not to others. The identification here of novel ubiquitin substrates, those with no known ubiquitinated ortholog, suggests that proteomics studies must be performed on neuronal cells to identify ubiquitination pathways not shared by other cell types. Importantly, several of those newly found neuronal ubiquitin substrates are key players in synaptogenesis. Mass spectrometry results were validated by Western blotting to confirm that those proteins are indeed ubiquitinated in the Drosophila embryonic nervous system and to elucidate whether they are mono- or polyubiquitinated. In addition to the ubiquitin substrates, we also identified the ubiquitin carriers that are active during synaptogenesis. Identifying endogenously ubiquitinated proteins in specific cell types, at specific developmental stages, and within the context of a living organism will allow understanding how the tissue-specific function of those proteins is regulated by the ubiquitin system.

Indexed as

UbiquitinationAnimalsBiotinylationCarrier ProteinsChromatography, LiquidDrosophila melanogasterDrosophila ProteinsMolecular WeightNerve Tissue ProteinsNervous SystemOrgan SpecificityProteomeRecombinant ProteinsUbiquitinUbiquitinated ProteinsCarrier ProteinsDrosophila ProteinsEps-15 protein, DrosophilaNerve Tissue ProteinsProteomeRecombinant ProteinsUbiquitinUbiquitinated Proteins

Identifiers

PMID20861518
PMCPMC3098581
OpenAlexW2154703935

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.