Evidence map›Paper›PMID 31285494›Full record

ArticleScientific reports2019

The mammalian CTLH complex is an E3 ubiquitin ligase that targets its subunit muskelin for degradation.

Matthew E R Maitland, Gabriel Onea, Christopher A Chiasson, Xu Wang, Jun Ma, Sarah E Moor, Kathryn R Barber, Gilles A Lajoie, Gary S Shaw, Caroline Schild-Poulter

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

50 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
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  4. Review
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  6. Article
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  9. Article
  10. GSK3β Regulates a Novel β-Catenin Degradation Pathway via the GID Complex in Wnt Signaling.Genes to cells : devoted to molecular & cellular mechanisms · 2025
    Article
  11. The many faces of the GID/CTLH E3 ligase complex.Biochemical Society transactions · 2025
    Review
  12. Article
  13. RANBP9 and RANBP10 cooperate in regulating non-small cell lung cancer proliferation.Journal of experimental & clinical cancer research : CR · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The hGIDLife science alliance · 2024
    Article
  20. 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

10 authors at 1 institution in 1 country.

Matthew E R MaitlandRobarts Research Institute, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, Ontario, Canada.
Gabriel OneaRobarts Research Institute, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, Ontario, Canada.
Christopher A ChiassonRobarts Research Institute, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, Ontario, Canada.
Xu WangRobarts Research Institute, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, Ontario, Canada.
Jun MaDepartment of Biochemistry, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, Ontario, Canada.
Sarah E MoorRobarts Research Institute, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, Ontario, Canada.
Kathryn R BarberDepartment of Biochemistry, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, Ontario, Canada.
Gilles A LajoieDepartment of Biochemistry, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, Ontario, Canada.
Gary S ShawDepartment of Biochemistry, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, Ontario, Canada.ORCID http://orcid.org/0000-0002-4685-9625
Caroline Schild-PoulterRobarts Research Institute, Schulich School of Medicine & Dentistry, The University of Western Ontario, London, Ontario, Canada. cschild-poulter@robarts.ca.
Western University · CA

Funding

CIHR MOP-14606
6 · The paper itself

Abstract

The multi-subunit C-terminal to LisH (CTLH) complex is the mammalian homologue of the yeast Gid E3 ubiquitin ligase complex. In this study, we investigated the human CTLH complex and characterized its E3 ligase activity. We confirm that the complex immunoprecipitated from human cells comprises RanBPM, ARMC8 α/β, muskelin, WDR26, GID4 and the RING domain proteins RMND5A and MAEA. We find that loss of expression of individual subunits compromises the stability of other complex members and that MAEA and RMND5A protein levels are interdependent. Using in vitro ubiquitination assays, we demonstrate that the CTLH complex has E3 ligase activity which is dependent on RMND5A and MAEA. We report that the complex can pair with UBE2D1, UBE2D2 and UBE2D3 E2 enzymes and that recombinant RMND5A mediates K48 and K63 poly-ubiquitin chains. Finally, we show a proteasome-dependent increase in the protein levels of CTLH complex member muskelin in RMND5A KO cells. Furthermore, muskelin ubiquitination is dependent on RMND5A, suggesting that it may be a target of the complex. Overall, we further the characterization of the CTLH complex as an E3 ubiquitin ligase complex in human cells and reveal a potential autoregulation mechanism.

Indexed as

AnimalsCarrier ProteinsCell LineCell Line, TumorCytoskeletal ProteinsHEK293 CellsHeLa CellsHumansMammalsProteasome Endopeptidase ComplexProtein DomainsProtein SubunitsProteolysisUbiquitinationUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesCarrier ProteinsCytoskeletal ProteinsProteasome Endopeptidase ComplexProtein SubunitsUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases

Identifiers

PMID31285494
PMCPMC6614414
OpenAlexW2960530550

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.