Evidence map›Paper›PMID 36649906›Full record

ArticleThe Journal of biological chemistry2023

Targeting of the Mon1-Ccz1 Rab guanine nucleotide exchange factor to distinct organelles by a synergistic protein and lipid code.

Eric Herrmann, Lars Langemeyer, Kathrin Auffarth, Christian Ungermann, Daniel Kümmel

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
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  6. Article
  7. ESCRTing the RABs through conversion.Biochemical Society transactions · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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
  14. 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
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

5 authors at 2 institutions in 1 country.

Eric HerrmannInstitute of Biochemistry, University of Münster, Münster, Germany.
Lars LangemeyerDepartment of Biology/Chemistry, Osnabrück University, Osnabrück, Germany.
Kathrin AuffarthDepartment of Biology/Chemistry, Osnabrück University, Osnabrück, Germany.
Christian UngermannDepartment of Biology/Chemistry, Osnabrück University, Osnabrück, Germany; Center of Cellular Nanoanalytics (CellNanOs), Osnabrück University, Osnabrück, Germany.
Daniel KümmelInstitute of Biochemistry, University of Münster, Münster, Germany. Electronic address: daniel.kuemmel@wwu.de.
Osnabrück University · DEUniversity of Münster · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of the small GTPase Rab7 by its cognate guanine nucleotide exchange factor Mon1-Ccz1 (MC1) is a key step in the maturation of endosomes and autophagosomes. This process is tightly regulated and subject to precise spatiotemporal control of MC1 localization, but the mechanisms that underly MC1 localization have not been fully elucidated. We here identify and characterize an amphipathic helix in Ccz1, which is required for the function of Mon-Ccz1 in autophagy, but not endosomal maturation. Furthermore, our data show that the interaction of the Ccz1 amphipathic helix with lipid packing defects, binding of Mon1 basic patches to positively charged lipids, and association of MC1 with recruiter proteins collectively govern membrane recruitment of the complex in a synergistic and redundant manner. Membrane binding enhances MC1 activity predominantly by increasing enzyme and substrate concentration on the membrane, but interaction with recruiter proteins can further stimulate the guanine nucleotide exchange factor. Our data demonstrate that specific protein and lipid cues convey the differential targeting of MC1 to endosomes and autophagosomes. In conclusion, we reveal the molecular basis for how MC1 is adapted to recognize distinct target compartments by exploiting the unique biophysical properties of organelle membranes and thus provide a model for how the complex is regulated and activated independently in different functional contexts.

Indexed as

rab GTP-Binding ProteinsVesicular Transport ProteinsEndosomesGuanine Nucleotide Exchange FactorsLipidsProtein TransportGuanine Nucleotide Exchange FactorsLipidsrab GTP-Binding ProteinsVesicular Transport ProteinsautophagyendosomeGTPaseguanine nucleotide exchange factormembrane recruitment

Identifiers

PMID36649906
PMCPMC10124900
OpenAlexW4316193138

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.