Evidence map›Paper›PMID 28051187›Full record

ArticleNature communications2017

Architecture and mechanism of the late endosomal Rab7-like Ypt7 guanine nucleotide exchange factor complex Mon1-Ccz1.

Stephan Kiontke, Lars Langemeyer, Anne Kuhlee, Saskia Schuback, Stefan Raunser, Christian Ungermann, Daniel Kümmel

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

55 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
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  8. ESCRTing the RABs through conversion.Biochemical Society transactions · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Structural basis for Rab6 activation by the Ric1-Rgp1 complex.bioRxiv : the preprint server for biology · 2024
    Article
  13. Article
  14. Article
  15. 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
  16. Cryo-EM structure of the Mon1-Ccz1-RMC1 complex reveals molecular basis of metazoan RAB7A activation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Structure of the metazoan Rab7 GEF complex Mon1-Ccz1-Bulli.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  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

7 authors at 2 institutions in 1 country.

Stephan KiontkeDivision of Structural Biology, Department of Biology/Chemistry, University of Osnabrück, Barbarastraße 13, Osnabrück 49076, Germany.
Lars LangemeyerBiochemistry Section, Department of Biology/Chemistry, University of Osnabrück, Barbarastraße 13, Osnabrück 49076, Germany.
Anne KuhleeDepartment of Structural Biochemistry, Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund 44227, Germany.
Saskia SchubackDivision of Structural Biology, Department of Biology/Chemistry, University of Osnabrück, Barbarastraße 13, Osnabrück 49076, Germany.
Stefan RaunserDepartment of Structural Biochemistry, Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund 44227, Germany.
Christian UngermannBiochemistry Section, Department of Biology/Chemistry, University of Osnabrück, Barbarastraße 13, Osnabrück 49076, Germany.ORCID 0000-0003-4331-8695
Daniel KümmelDivision of Structural Biology, Department of Biology/Chemistry, University of Osnabrück, Barbarastraße 13, Osnabrück 49076, Germany.
Osnabrück University · DEMax Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Mon1-Ccz1 complex (MC1) is the guanine nucleotide exchange factor (GEF) for the Rab GTPase Ypt7/Rab7 and is required for endosomal maturation and fusion at the vacuole/lysosome. Here we present the overall architecture of MC1 from Chaetomium thermophilum, and in combining biochemical studies and mutational analysis in yeast, we identify the domains required for catalytic activity, complex assembly and localization of MC1. The crystal structure of a catalytic MC1 core complex bound to Ypt7 provides mechanistic insight into its function. We pinpoint the determinants that allow for a discrimination of the Rab7-like Ypt7 over the Rab5-like Vps21, which are both located on the same membrane. MC1 shares structural similarities with the TRAPP complex, but employs a novel mechanism to promote nucleotide exchange that utilizes a conserved lysine residue of Ypt7, which is inserted upon MC1 binding into the nucleotide-binding pocket of Ypt7 and contributes to specificity.

Indexed as

ChaetomiumCrystallography, X-RayEndosomesFungal ProteinsGuanine Nucleotide Exchange FactorsLysosomesProtein BindingProtein DomainsProtein MultimerizationProtein Transportrab GTP-Binding ProteinsSubstrate SpecificityVacuolesVesicular Transport ProteinsFungal ProteinsGuanine Nucleotide Exchange Factorsrab GTP-Binding ProteinsVesicular Transport Proteins

Identifiers

PMID28051187
PMCPMC5216073
OpenAlexW2569789545

What OpenQuestion holds

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LicenceCC BY
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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.