Evidence map›Paper›PMID 26446846›Full record

ArticleMolecular biology of the cell2015

The mitochondrial fission receptor Mff selectively recruits oligomerized Drp1.

Raymond Liu, David C Chan

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

118 citing papers in PubMed, 184 citations in OpenAlex.

  1. Trial
  2. Rhynchophylline rewires DLAT lipoylationActa pharmaceutica Sinica. B · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. DRP1, fission and apoptosis.Cell death discovery · 2025
    Review
  15. Article
  16. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  17. Article
  18. Organelle abnormalities in Alzheimer's disease.Organelle (Tucson, Ariz.) · 2025
    Article
  19. Article
  20. Review

58 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

2 authors at 1 institution in 1 country.

Raymond LiuDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.
David C ChanDivision of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125 dchan@caltech.edu.
California Institute of Technology · US

Funding

Analysis of Drp 1 Receptors Important for Mitochondrial FissionR01GM110039 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CHAN, DAVID C · 2014 to 2017
$1.4M
NIGMS NIH HHS GM110039NIGMS NIH HHS R01 GM110039
6 · The paper itself

Abstract

Dynamin-related protein 1 (Drp1) is the GTP-hydrolyzing mechanoenzyme that catalyzes mitochondrial fission in the cell. Residing in the cytosol as dimers and tetramers, Drp1 is recruited by receptors on the mitochondrial outer membrane, where it further assembles into a helical ring that drives division via GTP-dependent constriction. The Drp1 receptor Mff is a major regulator of mitochondrial fission, and its overexpression results in increased fission. In contrast, the alternative Drp1 receptors MiD51 and MiD49 appear to recruit inactive forms of Drp1, because their overexpression inhibits fission. Using genetic and biochemical assays, we studied the interaction of Drp1 with Mff. We show that the insert B region of Drp1 inhibits Mff-Drp1 interactions, such that recombinant Drp1 mutants lacking insert B form a stable complex with Mff. Mff cannot bind to assembly-deficient mutants of Drp1, suggesting that Mff selectively interacts with higher-order complexes of Drp1. In contrast, the alternative Drp1 receptors MiD51 and MiD49 can recruit Drp1 dimers. Therefore Drp1 recruitment by Mff versus MiD51 and MiD49 may result in different outcomes because they recruit different subpopulations of Drp1 from the cytosol.

Indexed as

AnimalsCytosolDynaminsHydrolysisMembrane ProteinsMiceMitochondriaMitochondrial DynamicsMitochondrial MembranesMitochondrial ProteinsModels, MolecularPeptide Elongation FactorsProtein MultimerizationDnm1l protein, mouseDynaminsMembrane Proteinsmitochondrial fission factor, mouseMitochondrial ProteinsPeptide Elongation Factors

Identifiers

PMID26446846
PMCPMC4666140
OpenAlexW1914770541

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.