Evidence map›Paper›PMID 37115157›Full record

ArticleThe Journal of cell biology2023

Quantitative analysis of autophagy reveals the role of ATG9 and ATG2 in autophagosome formation.

David G Broadbent, Carlo Barnaba, Gloria I Perez, Jens C Schmidt

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
16.7field-weighted citation impact, top 1% 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

64 citing papers in PubMed, 78 citations in OpenAlex.

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  7. The Human Autophagy Core Complexes.Annual review of biochemistry · 2026
    Review
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  10. Role of N-glycosylation as a determinant of ATG9A conformations and activity.Protein science : a publication of the Protein Society · 2026
    Article
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4 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

David G Broadbent *Institute for Quantitative Health Science and Engineering, Michigan State University , East Lansing, MI, USA.ORCID 0000-0002-0940-1068
Carlo Barnaba *Institute for Quantitative Health Science and Engineering, Michigan State University , East Lansing, MI, USA.ORCID 0000-0003-2170-9695
Gloria I PerezInstitute for Quantitative Health Science and Engineering, Michigan State University , East Lansing, MI, USA.ORCID 0000-0002-0391-1358
Jens C SchmidtInstitute for Quantitative Health Science and Engineering, Michigan State University , East Lansing, MI, USA.ORCID 0000-0001-9061-7853
Michigan State University · US

Funding

Single-molecule Analysis of the DNA Damage Response in Living CellsDP2GM142307 · NIGMS · MICHIGAN STATE UNIVERSITY · PI SCHMIDT, JENS CHRISTOPHER · 2020 to 2020
$2.1M
NIGMS NIH HHS DP2 GM142307NIH HHS DP2 GM142307
6 · The paper itself

Abstract

Autophagy is a catabolic pathway required for the recycling of cytoplasmic materials. To define the mechanisms underlying autophagy it is critical to quantitatively characterize the dynamic behavior of autophagy factors in living cells. Using a panel of cell lines expressing HaloTagged autophagy factors from their endogenous loci, we analyzed the abundance, single-molecule dynamics, and autophagosome association kinetics of autophagy proteins involved in autophagosome biogenesis. We demonstrate that autophagosome formation is inefficient and ATG2-mediated tethering to donor membranes is a key commitment step in autophagosome formation. Furthermore, our observations support the model that phagophores are initiated by the accumulation of autophagy factors on mobile ATG9 vesicles, and that the ULK1 complex and PI3-kinase form a positive feedback loop required for autophagosome formation. Finally, we demonstrate that the duration of autophagosome biogenesis is ∼110 s. In total, our work provides quantitative insight into autophagosome biogenesis and establishes an experimental framework to analyze autophagy in human cells.

Indexed as

AutophagosomesAutophagy-Related ProteinsMembrane ProteinsAutophagyHumansMacroautophagyVesicular Transport ProteinsATG2A protein, humanATG9A protein, humanAutophagy-Related ProteinsMembrane ProteinsVesicular Transport Proteins

Identifiers

PMID37115157
PMCPMC10148237
OpenAlexW4367312761

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.