Evidence map›Paper›PMID 32391792›Full record

ArticleeLife2020

A conserved and regulated mechanism drives endosomal Rab transition.

Lars Langemeyer, Ann-Christin Borchers, Eric Herrmann, Nadia Füllbrunn, Yaping Han, Angela Perz, Kathrin Auffarth, Daniel Kümmel, Christian Ungermann

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
5.9field-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

46 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Rethinking the Yeast Endomembrane System.Sub-cellular biochemistry · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. ESCRTing the RABs through conversion.Biochemical Society transactions · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Regulatory sites in the Mon1-Ccz1 complex control Rab5 to Rab7 transition and endosome maturation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

9 authors at 2 institutions in 1 country.

Lars LangemeyerUniversity of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Osnabrück, Germany.ORCID 0000-0002-4309-0910
Ann-Christin BorchersUniversity of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Osnabrück, Germany.
Eric HerrmannUniversity of Münster, Institute of Biochemistry, Münster, Germany.
Nadia FüllbrunnUniversity of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Osnabrück, Germany.
Yaping HanUniversity of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Osnabrück, Germany.
Angela PerzUniversity of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Osnabrück, Germany.
Kathrin AuffarthUniversity of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Osnabrück, Germany.
Daniel KümmelUniversity of Münster, Institute of Biochemistry, Münster, Germany.ORCID 0000-0003-3950-5914
Christian UngermannUniversity of Osnabrück, Department of Biology/Chemistry, Biochemistry section, Osnabrück, Germany.ORCID 0000-0003-4331-8695
Osnabrück University · DEUniversity of Münster · DE

Funding

Deutsche Forschungsgemeinschaft SFB 944
6 · The paper itself

Abstract

Endosomes and lysosomes harbor Rab5 and Rab7 on their surface as key proteins involved in their identity, biogenesis, and fusion. Rab activation requires a guanine nucleotide exchange factor (GEF), which is Mon1-Ccz1 for Rab7. During endosome maturation, Rab5 is replaced by Rab7, though the underlying mechanism remains poorly understood. Here, we identify the molecular determinants for Rab conversion in vivo and in vitro, and reconstitute Rab7 activation with yeast and metazoan proteins. We show (i) that Mon1-Ccz1 is an effector of Rab5, (ii) that membrane-bound Rab5 is the key factor to directly promote Mon1-Ccz1 dependent Rab7 activation and Rab7-dependent membrane fusion, and (iii) that this process is regulated in yeast by the casein kinase Yck3, which phosphorylates Mon1 and blocks Rab5 binding. Our study thus uncovers the minimal feed-forward machinery of the endosomal Rab cascade and a novel regulatory mechanism controlling this pathway.

Indexed as

AnimalsCasein Kinase IDrosophilaDrosophila ProteinsEndosomesGuanine Nucleotide Exchange FactorsLiposomesMembrane FusionPhosphatidylinositol PhosphatesPhosphorylationProtein BindingProtein Prenylationrab5 GTP-Binding Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsCasein Kinase ICcz1 protein, S cerevisiaeDrosophila ProteinsGuanine Nucleotide Exchange FactorsLiposomesMon1 protein, S cerevisiaephosphatidylinositol 3-phosphatePhosphatidylinositol Phosphatesrab5 GTP-Binding Proteinsrab7 GTP-Binding Proteinsrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsYCK3 protein, S cerevisiaebiochemistrycell biologychemical biologyD. melanogasterendosomeGEFMon1-Ccz1Rab5Rab7Rab cascadeS. cerevisiae

Identifiers

PMID32391792
PMCPMC7239660
OpenAlexW3023459585

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.