Evidence map›Paper›PMID 23275879›Full record

ArticleG3 (Bethesda, Md.)2012

A targeted in vivo RNAi screen reveals deubiquitinases as new regulators of Notch signaling.

Junzheng Zhang, Min Liu, Ying Su, Juan Du, Alan Jian Zhu

Open access · goldAbstract read
In one paragraph

Article in G3 (Bethesda, Md.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

28 citing papers in PubMed, 39 citations in OpenAlex.

  1. Targeting ubiquitination in disease and therapy.Signal transduction and targeted therapy · 2025
    Review
  2. Review
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  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
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  12. Decoding the PTM-switchboard of Notch.Biochimica et biophysica acta. Molecular cell research · 2019
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
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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

5 authors at 1 institution in 1 country.

Junzheng ZhangDepartment of Cell Biology, Lerner Research Institute, Cleveland Clinic, Cleveland, Ohio 44195, USA.
Min Liu
Ying Su
Juan Du
Alan Jian Zhu
Cleveland Clinic Lerner College of Medicine · US

Funding

Clinical and Translational Science Collaborative of ClevelandUL1TR000439 · NCATS · CASE WESTERN RESERVE UNIVERSITY · PI KONSTAN, MICHAEL W. · 2012 to 2016
$50.0M
Reversible phosphorylation in Hedgehog signalingR01GM085175 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI ZHU, ALAN · 2009 to 2013
$1.5M
NCATS NIH HHS UL1 TR000439NIGMS NIH HHS R01 GM085175NIGMS NIH HHS R01GM085175
6 · The paper itself

Abstract

Notch signaling is highly conserved in all metazoan animals and plays critical roles in cell fate specification, cell proliferation, apoptosis, and stem cell maintenance. Although core components of the Notch signaling cascade have been identified, many gaps in the understanding of the Notch signaling pathway remain to be filled. One form of posttranslational regulation, which is controlled by the ubiquitin-proteasome system, is known to modulate Notch signaling. The ubiquitination pathway is a highly coordinated process in which the ubiquitin moiety is either conjugated to or removed from target proteins by opposing E3 ubiquitin ligases and deubiquitinases (DUBs). Several E3 ubiquitin ligases have been implicated in ubiquitin conjugation to the receptors and the ligands of the Notch signaling cascade. In contrast, little is known about a direct role of DUBs in Notch signaling in vivo. Here, we report an in vivo RNA interference screen in Drosophila melanogaster targeting all 45 DUBs that we annotated in the fly genome. We show that at least four DUBs function specifically in the formation of the fly wing margin and/or the specification of the scutellar sensory organ precursors, two processes that are strictly dependent on the balanced Notch signaling activity. Furthermore, we provide genetic evidence suggesting that these DUBs are necessary to positively modulate Notch signaling activity. Our study reveals a conserved molecular mechanism by which protein deubiquitination process contributes to the complex posttranslational regulation of Notch signaling in vivo.

Indexed as

RNA InterferenceAnimalsAnimals, Genetically ModifiedDrosophila melanogasterDrosophila ProteinsEukaryotic Initiation Factor-3GenomePhenotypeReceptors, NotchSignal TransductionUbiquitin-Activating EnzymesUbiquitinationUbiquitin-Protein LigasesWings, AnimalDrosophila ProteinsEukaryotic Initiation Factor-3Receptors, NotchUbiquitin-Activating EnzymesUbiquitin-Protein LigasesdeubiquitinaseDrosophila melanogasterNotch signalingubiquitination

Identifiers

PMID23275879
PMCPMC3516478
OpenAlexW2030213092

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.