Evidence map›Paper›PMID 37881948›Full record

ArticleAutophagy2024

ATG9 resides on a unique population of small vesicles in presynaptic nerve terminals.

Beyenech Binotti, Momchil Ninov, Andreia P Cepeda, Marcelo Ganzella, Ulf Matti, Dietmar Riedel, Henning Urlaub, Sivakumar Sambandan, Reinhard Jahn

Open access · greenAbstract read
In one paragraph

Article in Autophagy, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.8field-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

19 citing papers in PubMed, 28 citations in OpenAlex.

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  12. Turning garbage into gold: Autophagy in synaptic function.Current opinion in neurobiology · 2025
    Review
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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

9 authors at 5 institutions in 1 country.

Beyenech BinottiLaboratory of Neurobiology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Momchil NinovLaboratory of Neurobiology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Andreia P CepedaBioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Marcelo GanzellaLaboratory of Neurobiology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Ulf MattiAbberior Instruments GmbH, Göttingen, Germany.
Dietmar RiedelFacility for Transmission Electron Microscopy, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Henning UrlaubBioanalytics, Institute of Clinical Chemistry, University Medical Center Göttingen, Germany.
Sivakumar SambandanLaboratory of Neurobiology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.
Reinhard JahnLaboratory of Neurobiology, Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany.ORCID 0000-0003-1542-3498
Max Planck Institute for Multidisciplinary SciencesUniversitätsmedizin Göttingen · DEMax Planck Institute for Dynamics and Self-Organization · DESensoMotoric Instruments (Germany) · DEUniversity of Würzburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In neurons, autophagosome biogenesis occurs mainly in distal axons, followed by maturation during retrograde transport. Autophagosomal growth depends on the supply of membrane lipids which requires small vesicles containing ATG9, a lipid scramblase essential for macroautophagy/autophagy. Here, we show that ATG9-containing vesicles are enriched in synapses and resemble synaptic vesicles in size and density. The proteome of ATG9-containing vesicles immuno-isolated from nerve terminals showed conspicuously low levels of trafficking proteins except of the AP2-complex and some enzymes involved in endosomal phosphatidylinositol metabolism. Super resolution microscopy of nerve terminals and isolated vesicles revealed that ATG9-containing vesicles represent a distinct vesicle population with limited overlap not only with synaptic vesicles but also other membranes of the secretory pathway, uncovering a surprising heterogeneity in their membrane composition. Our results are compatible with the view that ATG9-containing vesicles function as lipid shuttles that scavenge membrane lipids from various intracellular membranes to support autophagosome biogenesis.

Indexed as

Autophagy-Related ProteinsPresynaptic TerminalsVesicular Transport ProteinsAnimalsAutophagyEndosomesMembrane ProteinsMiceSynaptic VesiclesAtg9A protein, mouseAutophagy-Related ProteinsMembrane ProteinsVesicular Transport ProteinsATG9autophagyRAB26synapsesynaptic vesiclesvesicle proteome

Identifiers

PMID37881948
PMCPMC11062364
OpenAlexW4387948662

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.