Evidence map›Paper›PMID 21274005›Full record

ArticleEMBO reports2011

Inner-membrane proteins PMI/TMEM11 regulate mitochondrial morphogenesis independently of the DRP1/MFN fission/fusion pathways.

Thomas Rival, Marc Macchi, Laetitia Arnauné-Pelloquin, Mickael Poidevin, Frédéric Maillet, Fabrice Richard, Ahmed Fatmi, Pascale Belenguer, Julien Royet

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

24 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
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  4. Article
  5. Article
  6. Coordinating BNIP3/NIX-mediated mitophagy in space and time.Biochemical Society transactions · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Mitochondrial Morphofunction in Mammalian Cells.Antioxidants & redox signaling · 2019
    Review
  19. Review
  20. The ever-growing complexity of the mitochondrial fission machinery.Cellular and molecular life sciences : CMLS · 2018
    Review
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

9 authors at 4 institutions in 1 country.

Thomas RivalInstitut de Biologie du Développement de Marseille-Luminy, CNRS UMR 6216/Aix-Marseille Universités, F-13288 Marseille, France.
Marc Macchi
Laetitia Arnauné-Pelloquin
Mickael Poidevin
Frédéric Maillet
Fabrice Richard
Ahmed Fatmi
Pascale Belenguer
Julien Royet
Centre National de la Recherche Scientifique · FRInstitut de Biologie du Développement Marseille · FRAix-Marseille Université · FRCentre de Génétique Moléculaire · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria are highly dynamic organelles that can change in number and morphology during cell cycle, development or in response to extracellular stimuli. These morphological dynamics are controlled by a tight balance between two antagonistic pathways that promote fusion and fission. Genetic approaches have identified a cohort of conserved proteins that form the core of mitochondrial remodelling machineries. Mitofusins (MFNs) and OPA1 proteins are dynamin-related GTPases that are required for outer- and inner-mitochondrial membrane fusion respectively whereas dynamin-related protein 1 (DRP1) is the master regulator of mitochondrial fission. We demonstrate here that the Drosophila PMI gene and its human orthologue TMEM11 encode mitochondrial inner-membrane proteins that regulate mitochondrial morphogenesis. PMI-mutant cells contain a highly condensed mitochondrial network, suggesting that PMI has either a pro-fission or an anti-fusion function. Surprisingly, however, epistatic experiments indicate that PMI shapes the mitochondria through a mechanism that is independent of drp1 and mfn. This shows that mitochondrial networks can be shaped in higher eukaryotes by at least two separate pathways: one PMI-dependent and one DRP1/MFN-dependent.

Indexed as

AnimalsCarrier ProteinsCells, CulturedCytoskeletal ProteinsDrosophilaDrosophila ProteinsDynaminsGene Knockdown TechniquesGTP-Binding ProteinsGTP PhosphohydrolasesHumansMembrane ProteinsMembrane Transport ProteinsMicrotubule-Associated ProteinsMitochondriaMitochondrial MembranesCarrier ProteinsCytoskeletal ProteinsDNM1L protein, humanDrosophila ProteinsDRP1 protein, DrosophilaDynaminsGTP-Binding ProteinsGTP PhosphohydrolasesMembrane ProteinsMembrane Transport ProteinsMfn1 protein, humanMicrotubule-Associated ProteinsMitochondrial Membrane Transport ProteinsMitochondrial ProteinsOPA1 protein, Drosophilapeptidoglycan recognition proteinPMI protein, DrosophilaRNA, Small Interfering

Identifiers

PMID21274005
PMCPMC3059922
OpenAlexW2049474080

What OpenQuestion holds

Textmetadata
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.