Evidence map›Paper›PMID 29364559›Full record

ArticleTraffic (Copenhagen, Denmark)2018

A role for Mitochondrial Rho GTPase 1 (MIRO1) in motility and membrane dynamics of peroxisomes.

Inês G Castro, David M Richards, Jeremy Metz, Joseph L Costello, Josiah B Passmore, Tina A Schrader, Ana Gouveia, Daniela Ribeiro, Michael Schrader

Open access · hybridAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

58 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Peroxisome calcium uptake is dependent on ER-peroxisome membrane contact.Cellular and molecular life sciences : CMLS · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Mitochondrial and peroxisomal fission in cortical neurogenesis.The international journal of biochemistry & cell biology · 2025
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024
    Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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 2 institutions in 2 countries.

Inês G CastroBiosciences, University of Exeter, Exeter, UK.ORCID 0000-0003-4669-985X
David M RichardsLSI, University of Exeter, Exeter, UK.
Jeremy MetzBiosciences, University of Exeter, Exeter, UK.ORCID 0000-0002-8099-8776
Joseph L CostelloBiosciences, University of Exeter, Exeter, UK.ORCID 0000-0002-2867-1864
Josiah B PassmoreBiosciences, University of Exeter, Exeter, UK.ORCID 0000-0001-7791-3439
Tina A SchraderBiosciences, University of Exeter, Exeter, UK.
Ana GouveiaInstitute of Biomedicine, University of Aveiro, Aveiro, Portugal.
Daniela RibeiroInstitute of Biomedicine, University of Aveiro, Aveiro, Portugal.ORCID 0000-0003-3397-0460
Michael SchraderBiosciences, University of Exeter, Exeter, UK.ORCID 0000-0003-2146-0535
University of Exeter · GBUniversity of Aveiro · PT

Funding

Biotechnology and Biological Sciences Research Council BB/K006231/1Biotechnology and Biological Sciences Research Council BB/N01541X/1Medical Research Council MR/P022405/1Wellcome TrustWellcome Trust WT097835MFWellcome Trust WT105618MA
6 · The paper itself

Abstract

Peroxisomes are dynamic organelles which fulfil essential roles in lipid and ROS metabolism. Peroxisome movement and positioning allows interaction with other organelles and is crucial for their cellular function. In mammalian cells, such movement is microtubule-dependent and mediated by kinesin and dynein motors. The mechanisms of motor recruitment to peroxisomes are largely unknown, as well as the role this plays in peroxisome membrane dynamics and proliferation. Here, using a combination of microscopy, live-cell imaging analysis and mathematical modelling, we identify a role for Mitochondrial Rho GTPase 1 (MIRO1) as an adaptor for microtubule-dependent peroxisome motility in mammalian cells. We show that MIRO1 is targeted to peroxisomes and alters their distribution and motility. Using a peroxisome-targeted MIRO1 fusion protein, we demonstrate that MIRO1-mediated pulling forces contribute to peroxisome membrane elongation and proliferation in cellular models of peroxisome disease. Our findings reveal a molecular mechanism for establishing peroxisome-motor protein associations in mammalian cells and provide new insights into peroxisome membrane dynamics in health and disease.

Indexed as

AnimalsCells, CulturedChlorocebus aethiopsCOS CellsHumansIntracellular MembranesMiceMicrotubulesOrganelle BiogenesisPeroxisomesProtein Transportrho GTP-Binding ProteinsMiro-1 protein, mouserho GTP-Binding Proteinsmathematical modellingmembrane protrusionmicrotubuleMIRO1organelle motilityperoxisomeproliferation

Identifiers

PMID29364559
PMCPMC5888202
OpenAlexW2784417246

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.