Evidence map›Paper›PMID 36762703›Full record

ArticleThe EMBO journal2023

Shuffled ATG8 interacting motifs form an ancestral bridge between UFMylation and autophagy.

Lorenzo Picchianti, Víctor Sánchez de Medina Hernández, Ni Zhan, Nicholas At Irwin, Roan Groh, Madlen Stephani, Harald Hornegger, Rebecca Beveridge, Justyna Sawa-Makarska, Thomas Lendl and 8 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
9.7field-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

35 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Evaluating evidence for UFMylation client diversity.Nature reviews. Molecular cell biology · 2026
    Article
  5. The mechanistic basis and cellular functions of UFMylation.Nature reviews. Molecular cell biology · 2026
    Review
  6. Review
  7. Review
  8. Review
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  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
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  17. Proximity biotinylation at the host-bioRxiv : the preprint server for biology · 2025
    Article
  18. Article
  19. Article
  20. UFMylation promotes orthoflavivirus infectious particle production.bioRxiv : the preprint server for biology · 2025
    Article
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

18 authors at 6 institutions in 3 countries.

Lorenzo Picchianti *Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Víctor Sánchez de Medina Hernández *Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Ni Zhan *Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Nicholas At IrwinDepartment of Zoology, University of Oxford, Oxford, UK.
Roan GrohGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Madlen StephaniGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Harald HorneggerMax Perutz Labs, Medical University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.
Rebecca BeveridgeDepartment of Pure and Applied Chemistry, University of Strathclyde, Glasgow, UK.
Justyna Sawa-MakarskaMax Perutz Labs, Medical University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0002-9321-976X
Thomas LendlResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.
Nenad GrujicGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Christin NaumannDepartment of Molecular Signal Processing, Leibniz Institute of Plant Biochemistry, Halle (Saale), Germany.ORCID 0000-0001-6972-155X
Sascha MartensMax Perutz Labs, Medical University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0003-3786-8199
Thomas A RichardsDepartment of Zoology, University of Oxford, Oxford, UK.
Tim ClausenResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.
Silvia RamundoGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
G Elif KaragözMax Perutz Labs, Medical University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0002-3392-2250
Yasin DagdasGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0002-9502-355X
Gregor Mendel Institute of Molecular Plant Biology · ATMax Perutz Labs · ATResearch Institute of Molecular Pathology · ATUniversity of Oxford · GBLeibniz Institute of Plant Biochemistry · DEUniversity of Strathclyde · GB

Funding

Austrian Science Fund FWF W 1261Medical Research Council MR/T020970/1
6 · The paper itself

Abstract

UFMylation involves the covalent modification of substrate proteins with UFM1 (Ubiquitin-fold modifier 1) and is important for maintaining ER homeostasis. Stalled translation triggers the UFMylation of ER-bound ribosomes and activates C53-mediated autophagy to clear toxic polypeptides. C53 contains noncanonical shuffled ATG8-interacting motifs (sAIMs) that are essential for ATG8 interaction and autophagy initiation. However, the mechanistic basis of sAIM-mediated ATG8 interaction remains unknown. Here, we show that C53 and sAIMs are conserved across eukaryotes but secondarily lost in fungi and various algal lineages. Biochemical assays showed that the unicellular alga Chlamydomonas reinhardtii has a functional UFMylation pathway, refuting the assumption that UFMylation is linked to multicellularity. Comparative structural analyses revealed that both UFM1 and ATG8 bind sAIMs in C53, but in a distinct way. Conversion of sAIMs into canonical AIMs impaired binding of C53 to UFM1, while strengthening ATG8 binding. Increased ATG8 binding led to the autoactivation of the C53 pathway and sensitization of Arabidopsis thaliana to ER stress. Altogether, our findings reveal an ancestral role of sAIMs in UFMylation-dependent fine-tuning of C53-mediated autophagy activation.

Indexed as

PeptidesProteinsAutophagyAutophagy-Related Protein 8 FamilyRibosomesAutophagy-Related Protein 8 FamilyPeptidesProteinsER-phagyphylogenomicsribosome stallingselective autophagyUFMylation

Identifiers

PMID36762703
PMCPMC10183829
OpenAlexW4319825963

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.