Evidence map›Paper›PMID 21927000›Full record

ArticleNature2011

Crystal structure of nucleotide-free dynamin.

Katja Faelber, York Posor, Song Gao, Martin Held, Yvette Roske, Dennis Schulze, Volker Haucke, Frank Noé, Oliver Daumke

Abstract read
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In one paragraph

Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 179 papers.

0numbers the graph read from it
0cells of the map it votes in
179citing papers in PubMed
–field-weighted citation impact
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

179 citing papers in PubMed.

  1. Article
  2. Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  3. Molecular machineries shaping the mitochondrial inner membrane.Nature reviews. Molecular cell biology · 2025
    Review
  4. Article
  5. Expanding the phenotypic spectrum of DNM1-related disorders: novel GTPase domain variants and their diverse neurological outcomes.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2025
    Article
  6. Article
  7. Article
  8. 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
  9. BIN1 reduction amelioratesProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  11. Article
  12. Article
  13. Dynamics of membrane tubulation coupled with fission by a two-component module.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

119 more citing papers are in PubMed but not listed here.

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.

Katja FaelberCrystallography, Max-Delbrück-Centrum for Molecular Medicine, Robert-Rössle-Strasse 10, 13125 Berlin, Germany. katja.faelber@mdc-berlin.de
York Posor
Song Gao
Martin Held
Yvette Roske
Dennis Schulze
Volker Haucke
Frank Noé
Oliver Daumke

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dynamin is a mechanochemical GTPase that oligomerizes around the neck of clathrin-coated pits and catalyses vesicle scission in a GTP-hydrolysis-dependent manner. The molecular details of oligomerization and the mechanism of the mechanochemical coupling are currently unknown. Here we present the crystal structure of human dynamin 1 in the nucleotide-free state with a four-domain architecture comprising the GTPase domain, the bundle signalling element, the stalk and the pleckstrin homology domain. Dynamin 1 oligomerized in the crystals via the stalks, which assemble in a criss-cross fashion. The stalks further interact via conserved surfaces with the pleckstrin homology domain and the bundle signalling element of the neighbouring dynamin molecule. This intricate domain interaction rationalizes a number of disease-related mutations in dynamin 2 and suggests a structural model for the mechanochemical coupling that reconciles previous models of dynamin function.

Indexed as

NucleotidesCrystallography, X-RayDynamin IDynamin IIGTP PhosphohydrolasesGuanosine TriphosphateHeLa CellsHumansHydrolysisModels, MolecularMolecular Dynamics SimulationProtein BindingProtein Structure, TertiarySignal TransductionTransferrinDynamin IDynamin IIGTP PhosphohydrolasesGuanosine TriphosphateNucleotidesTransferrin

Identifiers

PMID21927000

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.