Evidence map›Paper›PMID 37288820›Full record

ArticleeLife2023

Autophagosome membrane expansion is mediated by the N-terminus and

Wenxin Zhang, Taki Nishimura, Deepanshi Gahlot, Chieko Saito, Colin Davis, Harold B J Jefferies, Anne Schreiber, Lipi Thukral, Sharon A Tooze

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
8.4field-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

30 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. The Human Autophagy Core Complexes.Annual review of biochemistry · 2026
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Ceramide and the membrane-fusion activity of LC3/GABARAP autophagy proteins.Cellular and molecular life sciences : CMLS · 2025
    Article
  12. Article
  13. Article
  14. mBio · 2025
    Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Autophagy3D: a comprehensive autophagy structure database.Database : the journal of biological databases and curation · 2024
    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

9 authors at 3 institutions in 3 countries.

Wenxin Zhang *Molecular Cell Biology of Autophagy Laboratory, The Francis Crick Institute, London, United Kingdom.ORCID 0000-0002-7657-4495
Taki Nishimura *Molecular Cell Biology of Autophagy Laboratory, The Francis Crick Institute, London, United Kingdom.ORCID 0000-0003-4019-5984
Deepanshi GahlotCSIR-Institute of Genomics and Integrative Biology, New Delhi, India.ORCID 0000-0002-2681-8818
Chieko SaitoDepartment of Biochemistry and Molecular Biology, Graduate School and Faculty of Medicine, The University of Tokyo, Tokyo, Japan.
Colin DavisCellular Degradation Systems Laboratory, The Francis Crick Institute, London, United Kingdom.
Harold B J JefferiesMolecular Cell Biology of Autophagy Laboratory, The Francis Crick Institute, London, United Kingdom.
Anne SchreiberCellular Degradation Systems Laboratory, The Francis Crick Institute, London, United Kingdom.
Lipi ThukralCSIR-Institute of Genomics and Integrative Biology, New Delhi, India.ORCID 0000-0002-1961-039X
Sharon A ToozeMolecular Cell Biology of Autophagy Laboratory, The Francis Crick Institute, London, United Kingdom.ORCID 0000-0002-2182-3116
The Francis Crick Institute · GBInstitute of Genomics and Integrative Biology · INThe University of Tokyo · JP

Funding

Cancer Research UK CC2064Cancer Research UK CC2134European Research Council FP7/2007-2013 788708Medical Research Council CC2064Medical Research Council CC2134Wellcome Trust CC2064Wellcome Trust CC2134
6 · The paper itself

Abstract

Autophagy is an essential catabolic pathway which sequesters and engulfs cytosolic substrates via autophagosomes, unique double-membraned structures. ATG8 proteins are ubiquitin-like proteins recruited to autophagosome membranes by lipidation at the C-terminus. ATG8s recruit substrates, such as p62, and play an important role in mediating autophagosome membrane expansion. However, the precise function of lipidated ATG8 in expansion remains obscure. Using a real-time in vitro lipidation assay, we revealed that the N-termini of lipidated human ATG8s (LC3B and GABARAP) are highly dynamic and interact with the membrane. Moreover, atomistic MD simulation and FRET assays indicate that N-termini of LC3B and GABARAP associate in

Indexed as

AutophagosomesMicrotubule-Associated ProteinsAutophagyAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsHumansAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsMicrotubule-Associated Proteinsatomistic MD simulationautophagosome sizeautophagybiochemistrycell biologychemical biologycis-membrane associationmembrane expansionnonereal-time lipidation assay

Identifiers

PMID37288820
PMCPMC10289813
OpenAlexW4379768271

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.