Evidence map›Paper›PMID 25793641›Full record

ArticlePloS one2015

RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early embryonic forebrain development.

Thorsten Pfirrmann, Pablo Villavicencio-Lorini, Abinash K Subudhi, Ruth Menssen, Dieter H Wolf, Thomas Hollemann

Abstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
–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

24 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Guideline
  2. Article
  3. The many faces of the GID/CTLH E3 ligase complex.Biochemical Society transactions · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Structural and Functional Insights into GID/CTLH E3 Ligase Complexes.International journal of molecular sciences · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Recognition of nonproline N-terminal residues by the Pro/N-degron pathway.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Gid10 as an alternative N-recognin of the Pro/N-degron pathway.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. 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

6 authors.

Thorsten PfirrmannMartin-Luther University Halle-Wittenberg, Institute of Physiological Chemistry, Halle, Germany.
Pablo Villavicencio-LoriniMartin Luther University Halle-Wittenberg, Institute of Human Genetics, Halle, Germany.
Abinash K SubudhiMartin-Luther University Halle-Wittenberg, Institute of Physiological Chemistry, Halle, Germany.
Ruth MenssenUniversity of Stuttgart, Institute of Biochemistry, Pfaffenwaldring 55, 70569 Stuttgart, Germany.
Dieter H WolfUniversity of Stuttgart, Institute of Biochemistry, Pfaffenwaldring 55, 70569 Stuttgart, Germany.
Thomas HollemannMartin-Luther University Halle-Wittenberg, Institute of Physiological Chemistry, Halle, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Saccharomyces cerevisiae the Gid-complex functions as an ubiquitin-ligase complex that regulates the metabolic switch between glycolysis and gluconeogenesis. In higher organisms six conserved Gid proteins form the CTLH protein-complex with unknown function. Here we show that Rmnd5, the Gid2 orthologue from Xenopus laevis, is an ubiquitin-ligase embedded in a high molecular weight complex. Expression of rmnd5 is strongest in neuronal ectoderm, prospective brain, eyes and ciliated cells of the skin and its suppression results in malformations of the fore- and midbrain. We therefore suggest that Xenopus laevis Rmnd5, as a subunit of the CTLH complex, is a ubiquitin-ligase targeting an unknown factor for polyubiquitination and subsequent proteasomal degradation for proper fore- and midbrain development.

Indexed as

Embryonic DevelopmentAmino Acid SequenceAnimalsCarrier ProteinsGene Expression Regulation, DevelopmentalHumansMolecular Sequence DataNeurogenesisPhylogenyProsencephalonSequence AlignmentUbiquitin-Protein LigasesXenopus laevisCarrier ProteinsRMND5A protein, humanUbiquitin-Protein Ligases

Identifiers

PMID25793641
PMCPMC4368662

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Registered trials

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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.