Evidence map›Paper›PMID 31894645›Full record

ArticleEMBO reports2020

Peroxisomal fission is modulated by the mitochondrial Rho-GTPases, Miro1 and Miro2.

Christian Covill-Cooke, Viktoriya S Toncheva, James Drew, Nicol Birsa, Guillermo López-Doménech, Josef T Kittler

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
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  6. The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024
    Review
  7. Article
  8. Review
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  18. Article
  19. Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Christian Covill-CookeNeuroscience, Physiology and Pharmacology Department, University College London, London, UK.ORCID 0000-0002-4479-8734
Viktoriya S TonchevaNeuroscience, Physiology and Pharmacology Department, University College London, London, UK.ORCID 0000-0002-8526-080X
James DrewNeuroscience, Physiology and Pharmacology Department, University College London, London, UK.ORCID 0000-0002-2864-7987
Nicol BirsaNeuroscience, Physiology and Pharmacology Department, University College London, London, UK.ORCID 0000-0002-8271-540X
Guillermo López-DoménechNeuroscience, Physiology and Pharmacology Department, University College London, London, UK.ORCID 0000-0002-3114-2082
Josef T KittlerNeuroscience, Physiology and Pharmacology Department, University College London, London, UK.ORCID 0000-0002-3437-9456
University College London · GB

Funding

EC|H2020|H2020 Priority Excellent Science|H2020 European Research Council (ERC) 282430Medical Research Council 1368635Medical Research Council 1477260Medical Research Council 2180679UK Research and Innovation|Medical Research Council (MRC) 1368635
6 · The paper itself

Abstract

Peroxisomes are essential for a number of cellular functions, including reactive oxygen species metabolism, fatty acid β-oxidation and lipid synthesis. To ensure optimal functionality, peroxisomal size, shape and number must be dynamically maintained; however, many aspects of how this is regulated remain poorly characterised. Here, we show that the localisation of Miro1 and Miro2-outer mitochondrial membrane proteins essential for mitochondrial trafficking-to peroxisomes is not required for basal peroxisomal distribution and long-range trafficking, but rather for the maintenance of peroxisomal size and morphology through peroxisomal fission. Mechanistically, this is achieved by Miro negatively regulating Drp1-dependent fission, a function that is shared with the mitochondria. We further find that the peroxisomal localisation of Miro is regulated by its first GTPase domain and is mediated by an interaction through its transmembrane domain with the peroxisomal-membrane protein chaperone, Pex19. Our work highlights a shared regulatory role of Miro in maintaining the morphology of both peroxisomes and mitochondria, supporting a crosstalk between peroxisomal and mitochondrial biology.

Indexed as

Mitochondrial Proteinsrho GTP-Binding ProteinsAnimalsMiceMitochondriaMitochondrial MembranesPeroxisomesMitochondrial Proteinsrho GTP-Binding ProteinsFis1oscillatoryRhot1Rhot2tail-anchored

Identifiers

PMID31894645
PMCPMC7001505
OpenAlexW2998249717

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.