Evidence map›Paper›PMID 36215690›Full record

ArticleEMBO reports2022

Lipid and protein content profiling of isolated native autophagic vesicles.

Daniel Schmitt, Süleyman Bozkurt, Pascale Henning-Domres, Heike Huesmann, Stefan Eimer, Laura Bindila, Christian Behrends, Emily Boyle, Florian Wilfling, Georg Tascher and 3 more

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
6.1field-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

20 citing papers in PubMed, 40 citations in OpenAlex.

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  8. Ceramide and the membrane-fusion activity of LC3/GABARAP autophagy proteins.Cellular and molecular life sciences : CMLS · 2025
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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

13 authors at 4 institutions in 1 country.

Daniel SchmittThe Autophagy Lab, Institute of Pathobiochemistry, University Medical Center of the Johannes Gutenberg University, Mainz, Germany.
Süleyman BozkurtInstitute of Biochemistry II, Faculty of Medicine, Goethe University, Frankfurt am Main, Germany.ORCID 0000-0003-4965-3195
Pascale Henning-DomresThe Autophagy Lab, Institute of Pathobiochemistry, University Medical Center of the Johannes Gutenberg University, Mainz, Germany.
Heike HuesmannThe Autophagy Lab, Institute of Pathobiochemistry, University Medical Center of the Johannes Gutenberg University, Mainz, Germany.
Stefan EimerDepartment of Structural Cell Biology, Institute for Cell Biology and Neuroscience, Goethe University, Frankfurt am Main, Germany.
Laura BindilaClinical Lipidomics Unit, Institute of Physiological Chemistry, University Medical Center of the Johannes Gutenberg University, Mainz, Germany.
Christian BehrendsMunich Cluster for Systems Neurology (SyNergy), Ludwig-Maximilians-University, Munich, Germany.ORCID 0000-0002-9184-7607
Emily BoyleMechanisms of Cellular Quality Control, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.ORCID 0000-0001-8803-3939
Florian WilflingMechanisms of Cellular Quality Control, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.
Georg TascherInstitute of Biochemistry II, Faculty of Medicine, Goethe University, Frankfurt am Main, Germany.
Christian MünchInstitute of Biochemistry II, Faculty of Medicine, Goethe University, Frankfurt am Main, Germany.ORCID 0000-0003-3832-090X
Christian BehlThe Autophagy Lab, Institute of Pathobiochemistry, University Medical Center of the Johannes Gutenberg University, Mainz, Germany.
Andreas KernThe Autophagy Lab, Institute of Pathobiochemistry, University Medical Center of the Johannes Gutenberg University, Mainz, Germany.ORCID 0000-0003-0993-9818
Johannes Gutenberg University Mainz · DEGoethe University Frankfurt · DEMax Planck Institute of Biophysics · DEMunich Cluster for Systems Neurology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is responsible for clearance of an extensive portfolio of cargoes, which are sequestered into vesicles, called autophagosomes, and are delivered to lysosomes for degradation. The pathway is highly dynamic and responsive to several stress conditions. However, the phospholipid composition and protein contents of human autophagosomes under changing autophagy rates are elusive so far. Here, we introduce an antibody-based FACS-mediated approach for the isolation of native autophagic vesicles and ensured the quality of the preparations. Employing quantitative lipidomics, we analyze phospholipids present within human autophagic vesicles purified upon basal autophagy, starvation, and proteasome inhibition. Importantly, besides phosphoglycerides, we identify sphingomyelin within autophagic vesicles and show that the phospholipid composition is unaffected by the different conditions. Employing quantitative proteomics, we obtain cargo profiles of autophagic vesicles isolated upon the different treatment paradigms. Interestingly, starvation shows only subtle effects, while proteasome inhibition results in the enhanced presence of ubiquitin-proteasome pathway factors within autophagic vesicles. Thus, here we present a powerful method for the isolation of native autophagic vesicles, which enabled profound phospholipid and cargo analyses.

Indexed as

Proteasome Endopeptidase ComplexProteomicsAutophagyHumansPhospholipidsPhospholipidsProteasome Endopeptidase Complexautophagic vesiclesautophagycargo profilinglipid profilingvesicle isolation

Identifiers

PMID36215690
PMCPMC9724672
OpenAlexW4304141642

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.