Evidence map›Paper›PMID 32840906›Full record

ArticleThe EMBO journal2020

AP-3 vesicle uncoating occurs after HOPS-dependent vacuole tethering.

Jannis Schoppe, Muriel Mari, Erdal Yavavli, Kathrin Auffarth, Margarita Cabrera, Stefan Walter, Florian Fröhlich, Christian Ungermann

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

21 citing papers in PubMed, 39 citations in OpenAlex.

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  7. A structure-based mechanism for initiation of AP-3 coated vesicle formation.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

8 authors at 3 institutions in 3 countries.

Jannis SchoppeDepartment of Biology/Chemistry, Biochemistry Section, University of Osnabrück, Osnabrück, Germany.
Muriel MariDepartment of Biomedical Sciences of Cells and Systems, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands.
Erdal YavavliDepartment of Biology/Chemistry, Biochemistry Section, University of Osnabrück, Osnabrück, Germany.
Kathrin AuffarthDepartment of Biology/Chemistry, Biochemistry Section, University of Osnabrück, Osnabrück, Germany.
Margarita CabreraDepartament de Ciències Experimentals i de la Salut, Universitat Pompeu Farba, Barcelona, Spain.
Stefan WalterCenter of Cellular Nanoanalytic Osnabrück (CellNanOs), University of Osnabrück, Osnabrück, Germany.
Florian FröhlichCenter of Cellular Nanoanalytic Osnabrück (CellNanOs), University of Osnabrück, Osnabrück, Germany.ORCID 0000-0001-8307-2189
Christian UngermannDepartment of Biology/Chemistry, Biochemistry Section, University of Osnabrück, Osnabrück, Germany.ORCID 0000-0003-4331-8695
Osnabrück University · DEUniversitat Pompeu Fabra · ESUniversity Medical Center Groningen · NL

Funding

Deutsche Forschungsgemeinschaft (DFG) SFB 944 P11Deutsche Forschungsgemeinschaft (DFG) SFB 944 P20Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO) open program ALW.355
6 · The paper itself

Abstract

Heterotetrameric adapter (AP) complexes cooperate with the small GTPase Arf1 or lipids in cargo selection, vesicle formation, and budding at endomembranes in eukaryotic cells. While most AP complexes also require clathrin as the outer vesicle shell, formation of AP-3-coated vesicles involved in Golgi-to-vacuole transport in yeast has been postulated to depend on Vps41, a subunit of the vacuolar HOPS tethering complex. HOPS has also been identified as the tether of AP-3 vesicles on vacuoles. To unravel this conundrum of a dual Vps41 function, we anchored Vps41 stably to the mitochondrial outer membrane. By monitoring AP-3 recruitment, we now show that Vps41 can tether AP-3 vesicles to mitochondria, yet AP-3 vesicles can form in the absence of Vps41 or clathrin. By proximity labeling and mass spectrometry, we identify the Arf1 GTPase-activating protein (GAP) Age2 at the AP-3 coat and show that tethering, but not fusion at the vacuole can occur without complete uncoating. We conclude that AP-3 vesicles retain their coat after budding and that their complete uncoating occurs only after tethering at the vacuole.

Indexed as

ADP-Ribosylation FactorsBiological Transport, ActiveCasein Kinase ICytoplasmic VesiclesGene DeletionGolgi ApparatusGTPase-Activating ProteinsMass SpectrometryMembrane FusionMicroscopy, ElectronMitochondrial MembranesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesVesicular Transport ProteinsADP-Ribosylation FactorsAGE2 protein, S cerevisiaeCasein Kinase IGTPase-Activating ProteinsSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsVPS41 protein, S cerevisiaeYCK3 protein, S cerevisiaeAP-3Arf1 GAPHOPSvacuoleVps41

Identifiers

PMID32840906
PMCPMC7560216
OpenAlexW3081040921

What OpenQuestion holds

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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.