Evidence map›Paper›PMID 38057304›Full record

ArticleNature communications2023

Atg18 oligomer organization in assembled tubes and on lipid membrane scaffolds.

Daniel Mann, Simon A Fromm, Antonio Martinez-Sanchez, Navin Gopaldass, Ramona Choy, Andreas Mayer, Carsten Sachse

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. 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 4 institutions in 3 countries.

Daniel Mann *Ernst-Ruska Centre 3/Structural Biology, Forschungszentrum Jülich, Wilhelm-Johnen-Straße, Jülich, Germany.ORCID 0000-0002-9106-9358
Simon A Fromm *Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.ORCID 0000-0002-2094-1911
Antonio Martinez-SanchezDepartment of Information and Communications Engineering, Faculty of Computers Sciences, University of Murcia, Murcia, Spain.ORCID 0000-0002-5865-2138
Navin GopaldassDepartment of Biochemistry, University of Lausanne, Epalinges, Switzerland.
Ramona ChoyErnst-Ruska Centre 3/Structural Biology, Forschungszentrum Jülich, Wilhelm-Johnen-Straße, Jülich, Germany.
Andreas MayerDepartment of Biochemistry, University of Lausanne, Epalinges, Switzerland.ORCID 0000-0001-6131-313X
Carsten SachseErnst-Ruska Centre 3/Structural Biology, Forschungszentrum Jülich, Wilhelm-Johnen-Straße, Jülich, Germany. c.sachse@fz-juelich.de.ORCID 0000-0002-1168-5143
Forschungszentrum Jülich · DEUniversity of Lausanne · CHEuropean Molecular Biology Laboratory · DEUniversidad de Murcia · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy-related protein 18 (Atg18) participates in the elongation of early autophagosomal structures in concert with Atg2 and Atg9 complexes. How Atg18 contributes to the structural coordination of Atg2 and Atg9 at the isolation membrane remains to be understood. Here, we determined the cryo-EM structures of Atg18 organized in helical tubes, Atg18 oligomers in solution as well as on lipid membrane scaffolds. The helical assembly is composed of Atg18 tetramers forming a lozenge cylindrical lattice with remarkable structural similarity to the COPII outer coat. When reconstituted with lipid membranes, using subtomogram averaging we determined tilted Atg18 dimer structures bridging two juxtaposed lipid membranes spaced apart by 80 Å. Moreover, lipid reconstitution experiments further delineate the contributions of Atg18's FRRG motif and the amphipathic helical extension in membrane interaction. The observed structural plasticity of Atg18's oligomeric organization and membrane binding properties provide a molecular framework for the positioning of downstream components of the autophagy machinery.

Indexed as

Saccharomyces cerevisiae ProteinsAutophagyAutophagy-Related ProteinsLipidsMembrane ProteinsMembranesAutophagy-Related ProteinsLipidsMembrane ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID38057304
PMCPMC10700546
OpenAlexW4389370581

What OpenQuestion holds

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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.