Evidence map›Paper›PMID 24790094›Full record

ArticleMolecular biology of the cell2014

A dimeric equilibrium intermediate nucleates Drp1 reassembly on mitochondrial membranes for fission.

Patrick J Macdonald, Natalia Stepanyants, Niharika Mehrotra, Jason A Mears, Xin Qi, Hiromi Sesaki, Rajesh Ramachandran

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed, 1 pooled it
7.1field-weighted citation impact, top 2% 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

112 citing papers in PubMed, 1 synthesis or guideline pooled it, 170 citations in OpenAlex.

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

52 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

7 authors at 2 institutions in 1 country.

Patrick J MacdonaldDepartment of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH 44106.
Natalia StepanyantsDepartment of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH 44106.
Niharika MehrotraDepartment of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH 44106.
Jason A MearsDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, OH 44106Center for Mitochondrial Diseases, Case Western Reserve University School of Medicine, Cleveland, OH 44106.
Xin QiDepartment of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH 44106Center for Mitochondrial Diseases, Case Western Reserve University School of Medicine, Cleveland, OH 44106.
Hiromi SesakiDepartment of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
Rajesh RamachandranDepartment of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH 44106 rxr275@case.edu.
University School · USJohns Hopkins University · US

Funding

Mitochondrial Fusion and DivisionR01GM089853 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SESAKI, HIROMI · 2010 to 2014
$2.1M
NIGMS NIH HHS GM089853NIGMS NIH HHS R01 GM089853
6 · The paper itself

Abstract

The GTPase dynamin-related protein 1 (Drp1) catalyzes mitochondrial division, but the mechanisms remain poorly understood. Much of what is attributed to Drp1's mechanism of action in mitochondrial membrane fission parallels that of prototypical dynamin in endocytic vesicle scission. Unlike the case for dynamin, however, no lipid target for Drp1 activation at the mitochondria has been identified. In addition, the oligomerization properties of Drp1 have not been well established. We show that the mitochondria-specific lipid cardiolipin is a potent stimulator of Drp1 GTPase activity, as well as of membrane tubulation. We establish further that under physiological conditions, Drp1 coexists as two morphologically distinct polymeric species, one nucleotide bound in solution and the other membrane associated, which equilibrate via a dimeric assembly intermediate. With two mutations, C300A and C505A, that shift Drp1 polymerization equilibria in opposite directions, we demonstrate that dimers, and not multimers, potentiate the reassembly and reorganization of Drp1 for mitochondrial membrane remodeling both in vitro and in vivo.

Indexed as

Mitochondrial DynamicsAnimalsCardiolipinsCells, CulturedDynaminsGTP PhosphohydrolasesHumansLiposomesMiceMicrotubule-Associated ProteinsMitochondriaMitochondrial MembranesMitochondrial ProteinsProtein MultimerizationProtein Structure, QuaternaryCardiolipinsDNM1L protein, humanDynaminsGTP PhosphohydrolasesLiposomesMicrotubule-Associated ProteinsMitochondrial Proteins

Identifiers

PMID24790094
PMCPMC4055269
OpenAlexW2109065242

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.