Evidence map›Paper›PMID 29212658›Full record

ArticleThe Journal of cell biology2018

A new mitofusin topology places the redox-regulated C terminus in the mitochondrial intermembrane space.

Sevan Mattie, Jan Riemer, Jeremy G Wideman, Heidi M McBride

Abstract read
In one paragraph

Article in The Journal of cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
99citing 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

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

  1. Pooled it
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  12. The Essential Role of Mitochondrial Dynamics in Viral Infections.International journal of molecular sciences · 2025
    Review
  13. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  14. Review
  15. Mitochondrial Dynamics in Brain Cells During Normal and Pathological Aging.International journal of molecular sciences · 2024
    Review
  16. Review
  17. Review
  18. Article
  19. 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
  20. Review

39 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Sevan MattieMontreal Neurological Institute, McGill University, Montreal, Quebec, Canada.
Jan RiemerInstitut für Biochemie, University of Cologne, Köln, Germany.
Jeremy G WidemanBiosciences, University of Exeter, Exeter, England, UK jeremy.grant.wideman@gmail.com.ORCID 0000-0002-4426-9533
Heidi M McBrideMontreal Neurological Institute, McGill University, Montreal, Quebec, Canada heidi.mcbride@mcgill.ca.ORCID 0000-0003-4666-2280

Funding

CIHR
6 · The paper itself

Abstract

Mitochondrial fusion occurs in many eukaryotes, including animals, plants, and fungi. It is essential for cellular homeostasis, and yet the underlying mechanisms remain elusive. Comparative analyses and phylogenetic reconstructions revealed that fungal Fzo1 and animal Mitofusin proteins are highly diverged from one another and lack strong sequence similarity. Bioinformatic analysis showed that fungal Fzo1 proteins exhibit two predicted transmembrane domains, whereas metazoan Mitofusins contain only a single transmembrane domain. This prediction contradicts the current models, suggesting that both animal and fungal proteins share one topology. This newly predicted topology of Mfn1 and Mfn2 was demonstrated biochemically, confirming that the C-terminal, redox-sensitive cysteine residues reside within the intermembrane space (IMS). Functional experiments established that redox-mediated disulfide modifications within the IMS domain are key modulators of reversible Mfn oligomerization that drives fusion. Together, these results lead to a revised understanding of Mfns as single-spanning outer membrane proteins with an N

Indexed as

AnimalsComputational BiologyGTP PhosphohydrolasesHEK293 CellsHumansMembrane ProteinsMitochondriaMitochondrial DynamicsMitochondrial Membrane Transport ProteinsMitochondrial ProteinsOxidation-ReductionSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsFZO1 protein, S cerevisiaeGTP PhosphohydrolasesMembrane ProteinsMfn1 protein, humanMFN2 protein, humanMitochondrial Membrane Transport ProteinsMitochondrial ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID29212658
PMCPMC5800796

What OpenQuestion holds

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Registered trials

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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.