Evidence map›Paper›PMID 37774021›Full record

ArticleScience advances2023

ULK1 forms distinct oligomeric states and nanoscopic structures during autophagy initiation.

Chiranjib Banerjee, Dushyant Mehra, Daihyun Song, Angel Mancebo, Ji-Man Park, Do-Hyung Kim, Elias M Puchner

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.3field-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, 21 citations in OpenAlex.

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  10. The human autophagy-initiating complexes ULK1C and PI3KC3-C1.The Journal of biological chemistry · 2025
    Review
  11. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Chiranjib BanerjeeSchool of Physics and Astronomy, University of Minnesota, Twin Cities, Minneapolis, MN, USA.ORCID 0000-0003-0544-0681
Dushyant MehraSchool of Physics and Astronomy, University of Minnesota, Twin Cities, Minneapolis, MN, USA.ORCID 0000-0003-2942-8599
Daihyun SongDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Twin Cities, Minneapolis, MN, USA.
Angel ManceboSchool of Physics and Astronomy, University of Minnesota, Twin Cities, Minneapolis, MN, USA.ORCID 0000-0002-8663-2812
Ji-Man ParkDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Twin Cities, Minneapolis, MN, USA.ORCID 0000-0002-3201-3506
Do-Hyung KimDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Twin Cities, Minneapolis, MN, USA.ORCID 0000-0002-2924-4370
Elias M PuchnerSchool of Physics and Astronomy, University of Minnesota, Twin Cities, Minneapolis, MN, USA.ORCID 0000-0002-7129-2309
University of Minnesota · US

Funding

Mechanisms of mTORC1 signaling to protein degradation pathwaysR35GM130353 · NIGMS · UNIVERSITY OF MINNESOTA · PI Do-Hyung Kim · 2019 to 2026
$4.2M
Developing Diffusion-Contrast Super-Resolution Microscopy to Study Protein Interactions at Extreme Concentration Ratios in Live CellsR21GM127965 · NIGMS · UNIVERSITY OF MINNESOTA · PI PUCHNER, GEORG ELIAS MICHAEL · 2018 to 2019
$283k
NIGMS NIH HHS R21 GM127965NIGMS NIH HHS R35 GM130353
6 · The paper itself

Abstract

Autophagy induction involves extensive molecular and membrane reorganization. Despite substantial progress, the mechanism underlying autophagy initiation remains poorly understood. Here, we used quantitative photoactivated localization microscopy with single-molecule sensitivity to analyze the nanoscopic distribution of endogenous ULK1, the kinase that triggers autophagy. Under amino acid starvation, ULK1 formed large clusters containing up to 161 molecules at the endoplasmic reticulum. Cross-correlation analysis revealed that ULK1 clusters engaging in autophagosome formation require 30 or more molecules. The ULK1 structures with more than the threshold number contained varying levels of Atg13, Atg14, Atg16, LC3B, GEC1, and WIPI2. We found that ULK1 activity is dispensable for the initial clustering of ULK1, but necessary for the subsequent expansion of the clusters, which involves interaction with Atg14, Atg16, and LC3B and relies on Vps34 activity. This quantitative analysis at the single-molecule level has provided unprecedented insights into the behavior of ULK1 during autophagy initiation.

Indexed as

AutophagyAmino AcidsAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsHumansIntracellular Signaling Peptides and ProteinsAmino AcidsAutophagy-Related Protein-1 HomologAutophagy-Related ProteinsIntracellular Signaling Peptides and ProteinsULK1 protein, human

Identifiers

PMID37774021
PMCPMC10541014
OpenAlexW4387164549

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.