Evidence map›Paper›PMID 37252361›Full record

ArticleACS central science2023

Semisynthetic LC3 Probes for Autophagy Pathways Reveal a Noncanonical LC3 Interacting Region Motif Crucial for the Enzymatic Activity of Human ATG3.

Jakob Farnung, Matthias Muhar, Jin Rui Liang, Kateryna A Tolmachova, Roger M Benoit, Jacob E Corn, Jeffrey W Bode

Open access · diamondAbstract read
In one paragraph

Article in ACS central science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

12 citing papers in PubMed, 14 citations in OpenAlex.

  1. The Human Autophagy Core Complexes.Annual review of biochemistry · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
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  9. Mechanistic insights into the interactions of TAX1BP1 with RB1CC1 and mammalian ATG8 family proteins.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
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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

7 authors at 2 institutions in 1 country.

Jakob FarnungLaboratory for Organic Chemistry, Department of Chemistry and Applied Biosciences ETH Zürich, CH-8093 Zürich, Switzerland.ORCID https://orcid.org/0000-0002-4619-3421
Matthias MuharInstitute of Molecular Health Sciences, Department of Biology ETH Zürich, CH-8093 Zürich, Switzerland.
Jin Rui LiangInstitute of Molecular Health Sciences, Department of Biology ETH Zürich, CH-8093 Zürich, Switzerland.
Kateryna A TolmachovaLaboratory for Organic Chemistry, Department of Chemistry and Applied Biosciences ETH Zürich, CH-8093 Zürich, Switzerland.
Roger M BenoitLaboratory of Nanoscale Biology, Division of Biology and Chemistry, Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.ORCID https://orcid.org/0000-0001-9420-7739
Jacob E CornInstitute of Molecular Health Sciences, Department of Biology ETH Zürich, CH-8093 Zürich, Switzerland.
Jeffrey W BodeLaboratory for Organic Chemistry, Department of Chemistry and Applied Biosciences ETH Zürich, CH-8093 Zürich, Switzerland.ORCID https://orcid.org/0000-0001-8394-8910
ETH Zurich · CHPaul Scherrer Institute · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Macroautophagy is one of two major degradation systems in eukaryotic cells. Regulation and control of autophagy are often achieved through the presence of short peptide sequences called LC3 interacting regions (LIR) in autophagy-involved proteins. Using a combination of new protein-derived activity-based probes prepared from recombinant LC3 proteins, along with protein modeling and X-ray crystallography of the ATG3-LIR peptide complex, we identified a noncanonical LIR motif in the human E2 enzyme responsible for LC3 lipidation, ATG3. The LIR motif is present in the flexible region of ATG3 and adopts an uncommon β-sheet structure binding to the backside of LC3. We show that the β-sheet conformation is crucial for its interaction with LC3 and used this insight to design synthetic macrocyclic peptide-binders to ATG3. CRISPR-enabled

Identifiers

PMID37252361
PMCPMC10214526
OpenAlexW4367179325

What OpenQuestion holds

Textmetadata
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.