Evidence map›Paper›PMID 32851973›Full record

ArticleeLife2020

A cross-kingdom conserved ER-phagy receptor maintains endoplasmic reticulum homeostasis during stress.

Madlen Stephani, Lorenzo Picchianti, Alexander Gajic, Rebecca Beveridge, Emilio Skarwan, Victor Sanchez de Medina Hernandez, Azadeh Mohseni, Marion Clavel, Yonglun Zeng, Christin Naumann and 19 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers.

0numbers the graph read from it
0cells of the map it votes in
134citing papers in PubMed
21.7field-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

134 citing papers in PubMed, 236 citations in OpenAlex.

  1. Review
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  4. Review
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  6. Article
  7. The mechanistic basis and cellular functions of UFMylation.Nature reviews. Molecular cell biology · 2026
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  12. CDK5RAP3 Regulates Testosterone Production in Mouse Leydig Cells.International journal of molecular sciences · 2026
    Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Identification of Bitter Peptides inFoods (Basel, Switzerland) · 2025
    Article
  20. Biomolecular condensation of ERC1 recruits ATG8 and NBR1 to drive autophagosome formation for plant heat tolerance.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article

74 more citing papers are in PubMed but not listed here.

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

29 authors at 7 institutions in 5 countries.

Madlen Stephani *Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0001-6614-833X
Lorenzo Picchianti *Gregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Alexander GajicGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Rebecca BeveridgeResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.
Emilio SkarwanGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Victor Sanchez de Medina HernandezGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Azadeh MohseniGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Marion ClavelGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Yonglun ZengSchool of Life Sciences, Centre for Cell and Developmental Biology and State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, School of Life Sciences, New Territories, Shatin, China.
Christin NaumannDepartment of Molecular Signal Processing, Leibniz Institute of Plant Biochemistry, Halle, Germany.
Mateusz MatuszkiewiczGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Eleonora TurcoDepartment of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.
Christian LoefkeGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Baiying LiSchool of Life Sciences, Centre for Cell and Developmental Biology and State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, School of Life Sciences, New Territories, Shatin, China.
Gerhard DürnbergerGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Michael SchutzbierGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Hsiao Tieh ChenGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Alibek AbdrakhmanovGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Adriana SavovaDepartment of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.
Khong-Sam ChiaGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Armin DjameiGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0002-8087-9566
Irene SchaffnerBOKU Core Facility Biomolecular & Cellular Analysis, University of Natural Resources and Life Sciences, Vienna, Austria.
Steffen AbelDepartment of Molecular Signal Processing, Leibniz Institute of Plant Biochemistry, Halle, Germany.
Liwen JiangSchool of Life Sciences, Centre for Cell and Developmental Biology and State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, School of Life Sciences, New Territories, Shatin, China.
Karl MechtlerGregor Mendel Institute (GMI), Austrian Academy of Sciences, Vienna BioCenter (VBC), Vienna, Austria.
Fumiyo IkedaDepartment of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.ORCID 0000-0003-0407-2768
Sascha MartensDepartment of Biochemistry and Cell Biology, Max Perutz Labs, University of Vienna, Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0003-3786-8199
Tim ClausenResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), Vienna, Austria.ORCID 0000-0003-1582-6924
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 · ATChinese University of Hong Kong · HKUniversity of Vienna · ATLeibniz Institute of Plant Biochemistry · DEResearch Institute of Molecular Pathology · ATBOKU University · ATInstitute of Molecular Biotechnology · AT

Funding

Austrian Science Fund FWF P 30401Austrian Science Fund FWF P 32355Austrian Science Fund FWF W 1261
6 · The paper itself

Abstract

Eukaryotes have evolved various quality control mechanisms to promote proteostasis in the endoplasmic reticulum (ER). Selective removal of certain ER domains via autophagy (termed as ER-phagy) has emerged as a major quality control mechanism. However, the degree to which ER-phagy is employed by other branches of ER-quality control remains largely elusive. Here, we identify a cytosolic protein, C53, that is specifically recruited to autophagosomes during ER-stress, in both plant and mammalian cells. C53 interacts with ATG8 via a distinct binding epitope, featuring a shuffled ATG8 interacting motif (sAIM). C53 senses proteotoxic stress in the ER lumen by forming a tripartite receptor complex with the ER-associated ufmylation ligase UFL1 and its membrane adaptor DDRGK1. The C53/UFL1/DDRGK1 receptor complex is activated by stalled ribosomes and induces the degradation of internal or passenger proteins in the ER. Consistently, the C53 receptor complex and ufmylation mutants are highly susceptible to ER stress. Thus, C53 forms an ancient quality control pathway that bridges selective autophagy with ribosome-associated quality control in the ER.

Indexed as

Adaptor Proteins, Signal TransducingArabidopsis ProteinsAutophagyAutophagy-Related Protein 8 FamilyCell Cycle ProteinsEndoplasmic ReticulumEndoplasmic Reticulum StressHomeostasisHumansMembrane ProteinsProteostasisTumor Suppressor ProteinsAdaptor Proteins, Signal TransducingArabidopsis ProteinsAutophagy-Related Protein 8 FamilyCDK5RAP3 protein, humanCell Cycle ProteinsDDRGK1 protein, humanMembrane ProteinsTumor Suppressor ProteinsA. thalianacargo receptorcell biologyer-phagyer-quality controlhumanmarchantia polymorphaplant biologyribosome stallingselective autophagyUFMylation

Identifiers

PMID32851973
PMCPMC7515635
OpenAlexW3080457712

What OpenQuestion holds

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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.