Evidence map›Paper›PMID 23417307›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

The CORVET complex promotes tethering and fusion of Rab5/Vps21-positive membranes.

Henning J kleine Balderhaar, Jens Lachmann, Erdal Yavavli, Cornelia Bröcker, Anna Lürick, Christian Ungermann

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

54 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
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  6. Article
  7. Article
  8. Unifying biology of neurodegeneration in lysosomal storage diseases.Journal of inherited metabolic disease · 2025
    Review
  9. Article
  10. Article
  11. Genome-Scale Screening ofJournal of fungi (Basel, Switzerland) · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Small molecules targeting endocytic uptake and recycling pathways.Frontiers in cell and developmental biology · 2023
    Review
  17. Review
  18. 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 at 1 institution in 1 country.

Henning J kleine BalderhaarDepartment of Biology/Chemistry, University of Osnabrück, 49076 Osnabrück, Germany.
Jens Lachmann
Erdal Yavavli
Cornelia Bröcker
Anna Lürick
Christian Ungermann
Osnabrück University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane fusion along the endocytic pathway occurs in a sequence of tethering, docking, and fusion. At endosomes and vacuoles, the CORVET (class C core vacuole/endosome tethering) and HOPS (homotypic fusion and vacuole protein sorting) tethering complexes require their organelle-specific Rabs for localization and function. Until now, despite the absence of experimental evidence, it has been assumed that CORVET is a membrane-tethering factor. To test this theory and understand the mechanistic analogies with the HOPS complex, we set up an in vitro system, and establish CORVET as a bona-fide tether for Vps21-positive endosome/vacuole membranes. Purified CORVET binds to SNAREs and Rab5/Vps21-GTP. We then demonstrate that purified CORVET can specifically tether Vps21-positive membranes. Tethering via CORVET is dose-dependent, stimulated by the GEF Vps9, and inhibited by Msb3, the Vps21-GAP. Moreover, CORVET supports fusion of isolated membranes containing Vps21. In agreement with its role as a tether, overexpressed CORVET drives Vps21, but not the HOPS-specific Ypt7 into contact sites between vacuoles, which likely represent vacuole-associated endosomes. We therefore conclude that CORVET is a tethering complex that promotes fusion of Rab5-positive membranes and thus facilitates receptor down-regulation and recycling at the late endosome.

Indexed as

EndocytosisEndosomesLysosomesMembrane FusionMultiprotein Complexesrab5 GTP-Binding Proteinsrab GTP-Binding ProteinsRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSNARE ProteinsVacuolesMultiprotein Complexesrab5 GTP-Binding Proteinsrab GTP-Binding ProteinsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSNARE ProteinsVPS21 protein, S cerevisiae

Identifiers

PMID23417307
PMCPMC3593874
OpenAlexW2138181980

What OpenQuestion holds

Textmetadata
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.