Evidence map›Paper›PMID 32620754›Full record

ArticleNature communications2020

Super-assembly of ER-phagy receptor Atg40 induces local ER remodeling at contacts with forming autophagosomal membranes.

Keisuke Mochida, Akinori Yamasaki, Kazuaki Matoba, Hiromi Kirisako, Nobuo N Noda, Hitoshi Nakatogawa

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

44 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
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  3. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
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  8. Different ER-plasma membrane tethers play opposing roles in autophagy of the cortical ER.Proceedings of the National Academy of Sciences of the United States of America · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Keisuke Mochida *School of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Akinori Yamasaki *Institute of Microbial Chemistry (BIKAKEN), Tokyo, Japan.ORCID http://orcid.org/0000-0002-5820-5549
Kazuaki MatobaInstitute of Microbial Chemistry (BIKAKEN), Tokyo, Japan.ORCID http://orcid.org/0000-0002-0588-3100
Hiromi KirisakoSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Nobuo N NodaInstitute of Microbial Chemistry (BIKAKEN), Tokyo, Japan. nn@bikaken.or.jp.ORCID http://orcid.org/0000-0002-6940-8069
Hitoshi NakatogawaSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan. hnakatogawa@bio.titech.ac.jp.ORCID http://orcid.org/0000-0002-5828-0741
Tokyo Institute of Technology · JPMicrobial Chemistry Research Foundation · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The endoplasmic reticulum (ER) is selectively degraded by autophagy (ER-phagy) through proteins called ER-phagy receptors. In Saccharomyces cerevisiae, Atg40 acts as an ER-phagy receptor to sequester ER fragments into autophagosomes by binding Atg8 on forming autophagosomal membranes. During ER-phagy, parts of the ER are morphologically rearranged, fragmented, and loaded into autophagosomes, but the mechanism remains poorly understood. Here we find that Atg40 molecules assemble in the ER membrane concurrently with autophagosome formation via multivalent interaction with Atg8. Atg8-mediated super-assembly of Atg40 generates highly-curved ER regions, depending on its reticulon-like domain, and supports packing of these regions into autophagosomes. Moreover, tight binding of Atg40 to Atg8 is achieved by a short helix C-terminal to the Atg8-family interacting motif, and this feature is also observed for mammalian ER-phagy receptors. Thus, this study significantly advances our understanding of the mechanisms of ER-phagy and also provides insights into organelle fragmentation in selective autophagy of other organelles.

Indexed as

AutophagyAmino Acid SequenceAutophagosomesAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsBinding SitesEndoplasmic ReticulumEndoplasmic Reticulum StressIntracellular MembranesLuminescent ProteinsMembrane ProteinsMicroscopy, FluorescenceMutationProtein BindingProtein DomainsReceptors, Cytoplasmic and NuclearAtg40 protein, S cerevisiaeATG8 protein, S cerevisiaeAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsLuminescent ProteinsMembrane ProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae Proteins

Identifiers

PMID32620754
PMCPMC7335187
OpenAlexW3039255571

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.