Evidence map›Paper›PMID 36496453›Full record

ArticleNature communications2022

Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments.

Arthur A Melo, Thiemo Sprink, Jeffrey K Noel, Elena Vázquez-Sarandeses, Chris van Hoorn, Saif Mohd, Justus Loerke, Christian M T Spahn, Oliver Daumke

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  5. Structural and functional characterization of the brain-specific dynamin superfamily member RNF112.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  7. Review
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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 2 institutions in 1 country.

Arthur A MeloMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Structural Biology, Robert-Rössle-Straße 10, Berlin, Germany. arthur.melo@ucsf.edu.
Thiemo SprinkMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Structural Biology, Robert-Rössle-Straße 10, Berlin, Germany.
Jeffrey K NoelMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Structural Biology, Robert-Rössle-Straße 10, Berlin, Germany.
Elena Vázquez-SarandesesMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Structural Biology, Robert-Rössle-Straße 10, Berlin, Germany.
Chris van HoornMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Structural Biology, Robert-Rössle-Straße 10, Berlin, Germany.ORCID 0000-0002-1319-847X
Saif MohdMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Structural Biology, Robert-Rössle-Straße 10, Berlin, Germany.
Justus LoerkeInstitut für Medizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Berlin, Germany.ORCID 0000-0002-3424-8536
Christian M T SpahnInstitut für Medizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Berlin, Germany.
Oliver DaumkeMax-Delbrück-Center for Molecular Medicine in the Helmholtz Association, Structural Biology, Robert-Rössle-Straße 10, Berlin, Germany. oliver.daumke@mdc-berlin.de.ORCID 0000-0002-6190-1414
Max Delbrück Center · DECharité - Universitätsmedizin Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eps15-homology domain containing proteins (EHDs) are eukaryotic, dynamin-related ATPases involved in cellular membrane trafficking. They oligomerize on membranes into filaments that induce membrane tubulation. While EHD crystal structures in open and closed conformations were previously reported, little structural information is available for the membrane-bound oligomeric form. Consequently, mechanistic insights into the membrane remodeling mechanism have remained sparse. Here, by using cryo-electron tomography and subtomogram averaging, we determined structures of nucleotide-bound EHD4 filaments on membrane tubes of various diameters at an average resolution of 7.6 Å. Assembly of EHD4 is mediated via interfaces in the G-domain and the helical domain. The oligomerized EHD4 structure resembles the closed conformation, where the tips of the helical domains protrude into the membrane. The variation in filament geometry and tube radius suggests a spontaneous filament curvature of approximately 1/70 nm

Indexed as

DynaminsElectron Microscope TomographyAdenosine TriphosphatasesCell MembraneCryoelectron MicroscopyMembranesAdenosine TriphosphatasesDynamins

Identifiers

PMID36496453
PMCPMC9741607
OpenAlexW4311679687

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.