Evidence map›Paper›PMID 30561335›Full record

ArticleeLife2018

The role of scaffold reshaping and disassembly in dynamin driven membrane fission.

Martina Pannuzzo, Zachary A McDargh, Markus Deserno

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Solvent-Mediated Dewetting Principles for Cell-Sized Liposome Formation.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  4. Article
  5. Article
  6. Nanoscale dynamics of Dynamin 1 helices reveals squeeze-twist deformation mode critical for membrane fission.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Modeling membrane reshaping driven by dynamic protein assemblies.Current opinion in structural biology · 2023
    Review
  14. Article
  15. Review
  16. Article
  17. Quantification and demonstration of the collective constriction-by-ratchet mechanism in the dynamin molecular motor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Martina PannuzzoDepartment of Physics, Carnegie Mellon University, Pittsburgh, United States.ORCID http://orcid.org/0000-0001-8629-0173
Zachary A McDarghDepartment of Physics, Carnegie Mellon University, Pittsburgh, United States.ORCID https://orcid.org/0000-0001-9022-5593
Markus DesernoDepartment of Physics, Carnegie Mellon University, Pittsburgh, United States.ORCID https://orcid.org/0000-0001-5692-1595
Carnegie Mellon University · US

Funding

Marie Curie Marie Sklodowska-Curie grant agreement no. 754490
6 · The paper itself

Abstract

The large GTPase dynamin catalyzes membrane fission in eukaryotic cells, but despite three decades of experimental work, competing and partially conflicting models persist regarding some of its most basic actions. Here we investigate the mechanical and functional consequences of dynamin scaffold shape changes and disassembly with the help of a geometrically and elastically realistic simulation model of helical dynamin-membrane complexes. Beyond changes of radius and pitch, we emphasize the crucial role of a third functional motion: an effective rotation of the filament around its longitudinal axis, which reflects alternate tilting of dynamin's PH binding domains and creates a membrane torque. We also show that helix elongation impedes fission, hemifission is reached via a small transient pore, and coat disassembly assists fission. Our results have several testable structural consequences and help to reconcile mutual conflicting aspects between the two main present models of dynamin fission-the two-stage and the constrictase model.

Indexed as

DynaminsEukaryotic CellsMembranesModels, BiologicalMolecular Dynamics SimulationProtein ConformationDynaminscell biologydynaminfissionhemifissionmembranemolecular biophysicsnonesimulationstructural biology

Identifiers

PMID30561335
PMCPMC6355196
OpenAlexW2903664357

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.