Evidence map›Paper›PMID 32304672›Full record

ReviewJournal of molecular and cellular cardiology2020

Mitofusins as mitochondrial anchors and tethers.

Gerald W Dorn

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular and cellular cardiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Nanomaterial-induced mitochondrial biogenesis enhances intercellular mitochondrial transfer efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. ER-tethered stress sensor CREBH regulates mitochondrial unfolded protein response to maintain energy homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

1 author at 1 institution in 1 country.

Gerald W DornDepartment of Internal Medicine, Washington University School of Medicine, St. Louis, MO, USA. Electronic address: gdorn@wustl.edu.
Washington University in St. Louis · US

Funding

THE MITOCHONDRIAL DYNAMISM/FITNESS/BIOGENESIS INTERACTOME IN CARDIAC DISEASER35HL135736 · NHLBI · WASHINGTON UNIVERSITY · PI DORN, GERALD W. · 2017 to 2023
$6.4M
MITOFUSIN AGONISTS TO TREAT NEURODEGENERATIVE DISEASER41NS113642 · NINDS · MITOCHONDRIA IN MOTION, INC. · PI DORN, GERALD W. · 2019 to 2021
$557k
Mitofusin agonists to prevent Charcot-Marie-Tooth disease 2AR41NS115184 · NINDS · MITOCHONDRIA IN MOTION, INC. · PI DORN, GERALD W. · 2019 to 2019
$254k
NHLBI NIH HHS R35 HL135736NINDS NIH HHS R41 NS113642NINDS NIH HHS R41 NS115184
6 · The paper itself

Abstract

Mitochondria have their own genomes and their own agendas. Like their primitive bacterial ancestors, mitochondria interact with their environment and organelle colleagues at their physical interfaces, the outer mitochondrial membrane. Among outer membrane proteins, mitofusins (MFN) are increasingly recognized for their roles as arbiters of mitochondria-mitochondria and mitochondria-reticular interactions. This review examines the roles of MFN1 and MFN2 in the heart and other organs as proteins that tether mitochondria to each other or to other organelles, and as mitochondrial anchoring proteins for various macromolecular complexes. The consequences of MFN-mediated tethering and anchoring on mitochondrial fusion, motility, mitophagy, and mitochondria-ER calcium cross-talk are reviewed. Pathophysiological implications are explored from the perspective of mitofusin common functioning as tethering and anchoring proteins, rather than as mediators of individual processes. Finally, some informed speculation is provided for why mouse MFN knockout studies show severe multi-system phenotypes whereas rare human diseases linked to MFN mutations are limited in scope.

Indexed as

AnimalsBiological TransportGTP PhosphohydrolasesHumansMitochondriaMitochondrial DynamicsMitochondrial Membrane Transport ProteinsProtein MultimerizationUbiquitinationUbiquitin-Protein LigasesGTP PhosphohydrolasesMitochondrial Membrane Transport Proteinsparkin proteinUbiquitin-Protein LigasesMetabolismMitochondrial dynamicsMitochondrial fusionMitochondrial transportMitophagy

Identifiers

PMID32304672
PMCPMC7275906
OpenAlexW3016858569

What OpenQuestion holds

Textmetadata
LicenceTDM
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.