Evidence map›Paper›PMID 27253069›Full record

ArticleeLife2016

A mitofusin-dependent docking ring complex triggers mitochondrial fusion in vitro.

Tobias Brandt, Laetitia Cavellini, Werner Kühlbrandt, Mickaël M Cohen

Abstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing 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

70 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Mfn2-dependent fusion pathway of PE-enriched micron-sized vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Mechanisms of SNARE proteins in membrane fusion.Nature reviews. Molecular cell biology · 2024
    Review
  15. Review
  16. Article
  17. HIF-1 signaling: an emerging mechanism for mitochondrial dynamics.Journal of physiology and biochemistry · 2023
    Review
  18. Article
  19. Article
  20. Article

10 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

4 authors.

Tobias BrandtMax Planck Institute of Biophysics, Frankfurt, Germany.
Laetitia CavelliniLaboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, Sorbonne Universités, Paris, France.
Werner KühlbrandtMax Planck Institute of Biophysics, Frankfurt, Germany.
Mickaël M CohenLaboratoire de Biologie Moléculaire et Cellulaire des Eucaryotes, Institut de Biologie Physico-Chimique, Sorbonne Universités, Paris, France.ORCID 0000-0002-1372-680X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fusion of mitochondrial outer membranes is crucial for proper organelle function and involves large GTPases called mitofusins. The discrete steps that allow mitochondria to attach to one another and merge their outer membranes are unknown. By combining an in vitro mitochondrial fusion assay with electron cryo-tomography (cryo-ET), we visualize the junction between attached mitochondria isolated from Saccharomyces cerevisiae and observe complexes that mediate this attachment. We find that cycles of GTP hydrolysis induce progressive formation of a docking ring structure around extended areas of contact. Further GTP hydrolysis triggers local outer membrane fusion at the periphery of the contact region. These findings unravel key features of mitofusin-dependent fusion of outer membranes and constitute an important advance in our understanding of how mitochondria connect and merge.

Indexed as

Membrane FusionGTP PhosphohydrolasesGuanosine TriphosphateIn Vitro TechniquesMitochondrial DynamicsMitochondrial MembranesMitochondrial Membrane Transport ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGTP PhosphohydrolasesGuanosine TriphosphateMitochondrial Membrane Transport ProteinsSaccharomyces cerevisiae Proteinsbiophysicscell biologycryo-EMdynamin-related-proteinsmembrane fusionmitochondriamitochondrial dynamicsmitofusinS. cerevisiaestructural biology

Identifiers

PMID27253069
PMCPMC4929004

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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.