Evidence map›Paper›PMID 38057553›Full record

ArticleNature structural & molecular biology2024

Complete set of the Atg8-E1-E2-E3 conjugation machinery forms an interaction web that mediates membrane shaping.

Jahangir Md Alam, Tatsuro Maruyama, Daisuke Noshiro, Chika Kakuta, Tetsuya Kotani, Hitoshi Nakatogawa, Nobuo N Noda

Abstract read
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In one paragraph

Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

18 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. The role of autophagy in protozoan infections.Frontiers in cellular and infection microbiology · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Mechanisms of autophagosome formation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025
    Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Phosphatidylethanolamine.Trends in endocrinology and metabolism: TEM · 2024
    Article
  17. Article
  18. Review
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 3 institutions in 1 country.

Jahangir Md Alam *Institute of Microbial Chemistry (BIKAKEN), Tokyo, Japan.
Tatsuro Maruyama *Institute of Microbial Chemistry (BIKAKEN), Tokyo, Japan.
Daisuke NoshiroInstitute for Genetic Medicine, Hokkaido University, Sapporo, Japan.ORCID http://orcid.org/0000-0001-7024-2054
Chika KakutaCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.
Tetsuya KotaniCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.
Hitoshi NakatogawaCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.ORCID http://orcid.org/0000-0002-5828-0741
Nobuo N NodaInstitute of Microbial Chemistry (BIKAKEN), Tokyo, Japan. nn@igm.hokudai.ac.jp.ORCID http://orcid.org/0000-0002-6940-8069
Tokyo Institute of Technology · JPHokkaido University · JPMicrobial Chemistry Research Foundation · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Atg8, a ubiquitin-like protein, is conjugated with phosphatidylethanolamine (PE) via Atg7 (E1), Atg3 (E2) and Atg12-Atg5-Atg16 (E3) enzymatic cascade and mediates autophagy. However, its molecular roles in autophagosome formation are still unclear. Here we show that Saccharomyces cerevisiae Atg8-PE and E1-E2-E3 enzymes together construct a stable, mobile membrane scaffold. The complete scaffold formation induces an in-bud in prolate-shaped giant liposomes, transforming their morphology into one reminiscent of isolation membranes before sealing. In addition to their enzymatic roles in Atg8 lipidation, all three proteins contribute nonenzymatically to membrane scaffolding and shaping. Nuclear magnetic resonance analyses revealed that Atg8, E1, E2 and E3 together form an interaction web through multivalent weak interactions, where the intrinsically disordered regions in Atg3 play a central role. These data suggest that all six Atg proteins in the Atg8 conjugation machinery control membrane shaping during autophagosome formation.

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAutophagyAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsMembranesMicrotubule-Associated ProteinsUbiquitin-Conjugating EnzymesUbiquitinsAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsMicrotubule-Associated ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesUbiquitins

Identifiers

PMID38057553
OpenAlexW4389388777

What OpenQuestion holds

Textmetadata
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.