Evidence map›Paper›PMID 25770210›Full record

ArticleThe Journal of biological chemistry2015

The mechanoenzymatic core of dynamin-related protein 1 comprises the minimal machinery required for membrane constriction.

Christopher A Francy, Frances J D Alvarez, Louie Zhou, Rajesh Ramachandran, Jason A Mears

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed, 1 pooled it
–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

77 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Conformational Rearrangement of Fission DSPs.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  6. Article
  7. Article
  8. The Structure of the Drp1 Lattice on Membrane.Journal of molecular biology · 2025
    Article
  9. Review
  10. DRP1, fission and apoptosis.Cell death discovery · 2025
    Review
  11. Article
  12. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Article

17 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

5 authors.

Christopher A FrancyFrom the Department of Pharmacology, Center for Mitochondrial Diseases, and Cleveland Center for Membrane and Structural Biology, and.
Frances J D AlvarezFrom the Department of Pharmacology, Center for Mitochondrial Diseases, and Cleveland Center for Membrane and Structural Biology, and.
Louie ZhouFrom the Department of Pharmacology, Center for Mitochondrial Diseases, and Cleveland Center for Membrane and Structural Biology, and.
Rajesh RamachandranCleveland Center for Membrane and Structural Biology, and the Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106.
Jason A MearsFrom the Department of Pharmacology, Center for Mitochondrial Diseases, and Cleveland Center for Membrane and Structural Biology, and jason.mears@case.edu.

Funding

PREDOCTORAL TRAINING PROGRAM IN MOLECULAR THERAPEUTICST32GM008803 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI MIEYAL, JOHN J, NIEMAN, MARVIN THOMAS · 2001 to 2023
$4.2M
NIGMS NIH HHS 2T32GM008803-11A1NIGMS NIH HHS T32 GM008803
6 · The paper itself

Abstract

Mitochondria are dynamic organelles that continually undergo cycles of fission and fusion. Dynamin-related protein 1 (Drp1), a large GTPase of the dynamin superfamily, is the main mediator of mitochondrial fission. Like prototypical dynamin, Drp1 is composed of a mechanochemical core consisting of the GTPase, middle, and GTPase effector domain regions. In place of the pleckstrin homology domain in dynamin, however, Drp1 contains an unstructured variable domain, whose function is not yet fully resolved. Here, using time-resolved EM and rigorous statistical analyses, we establish the ability of full-length Drp1 to constrict lipid bilayers through a GTP hydrolysis-dependent mechanism. We also show the variable domain limits premature Drp1 assembly in solution and promotes membrane curvature. Furthermore, the mechanochemical core of Drp1, absent of the variable domain, is sufficient to mediate GTP hydrolysis-dependent membrane constriction.

Indexed as

Mechanical PhenomenaBiomechanical PhenomenaCardiolipinsDynaminsGTP PhosphohydrolasesGuanosine TriphosphateHumansHydrolysisKineticsLipid BilayersLiposomesMicrotubule-Associated ProteinsMitochondrial DynamicsMitochondrial MembranesMitochondrial ProteinsModels, MolecularCardiolipinsDNM1L protein, humanDynaminsGTP PhosphohydrolasesGuanosine TriphosphateLipid BilayersLiposomesMicrotubule-Associated ProteinsMitochondrial ProteinsDynaminDynamin-related Protein 1Electron Microscopy (EM)GTPaseMitochondriaMitochondrial FissionProtein Conformational ChangesProtein Self-assembly

Identifiers

PMID25770210
PMCPMC4416870

What OpenQuestion holds

Textmetadata
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.