Evidence map›Paper›PMID 30459446›Full record

ArticleScientific reports2018

GBF1 and Arf1 interact with Miro and regulate mitochondrial positioning within cells.

Laurence Walch, Emilie Pellier, Weihua Leng, Goran Lakisic, Alexis Gautreau, Vincent Contremoulins, Jean-Marc Verbavatz, Catherine L Jackson

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. The AMPK Pathway: Molecular Rejuvenation of Metabolism and Mitochondria.Annual review of cell and developmental biology · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. The Arf family GTPases: Regulation of vesicle biogenesis and beyond.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Miro: A molecular switch at the center of mitochondrial regulation.Protein science : a publication of the Protein Society · 2020
    Review
  18. Article
  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

8 authors at 2 institutions in 2 countries.

Laurence WalchInstitut Jacques Monod, UMR7592 CNRS Université Paris-Diderot, Sorbonne Paris Cité, Paris, France.
Emilie PellierInstitut Jacques Monod, UMR7592 CNRS Université Paris-Diderot, Sorbonne Paris Cité, Paris, France.
Weihua LengMax Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.
Goran LakisicCNRS UMR7654, Ecole Polytechnique, Palaiseau, France.
Alexis GautreauCNRS UMR7654, Ecole Polytechnique, Palaiseau, France.
Vincent ContremoulinsInstitut Jacques Monod, UMR7592 CNRS Université Paris-Diderot, Sorbonne Paris Cité, Paris, France.
Jean-Marc VerbavatzInstitut Jacques Monod, UMR7592 CNRS Université Paris-Diderot, Sorbonne Paris Cité, Paris, France. jean-marc.verbavatz@ijm.fr.
Catherine L JacksonInstitut Jacques Monod, UMR7592 CNRS Université Paris-Diderot, Sorbonne Paris Cité, Paris, France. cathy.jackson@ijm.fr.ORCID http://orcid.org/0000-0002-0843-145X
Centre National de la Recherche Scientifique · FRMax Planck Institute of Molecular Cell Biology and Genetics · DE

Funding

Agence Nationale de la Recherche (French National Research Agency) ANR-13-BSV2-0013Fondation pour la Recherche Médicale (Foundation for Medical Research in France) DEQ20150934717
6 · The paper itself

Abstract

The spatial organization of cells depends on coordination between cytoskeletal systems and intracellular organelles. The Arf1 small G protein and its activator GBF1 are important regulators of Golgi organization, maintaining its morphology and function. Here we show that GBF1 and its substrate Arf1 regulate the spatial organization of mitochondria in a microtubule-dependent manner. Miro is a mitochondrial membrane protein that interacts through adaptors with microtubule motor proteins such as cytoplasmic dynein, the major microtubule minus end directed motor. We demonstrate a physical interaction between GBF1 and Miro, and also between the active GTP-bound form of Arf1 and Miro. Inhibition of GBF1, inhibition of Arf1 activation, or overexpression of Miro, caused a collapse of the mitochondrial network towards the centrosome. The change in mitochondrial morphology upon GBF1 inhibition was due to a two-fold increase in the time engaged in retrograde movement compared to control conditions. Electron tomography revealed that GBF1 inhibition also resulted in larger mitochondria with more complex morphology. Miro silencing or drug inhibition of cytoplasmic dynein activity blocked the GBF1-dependent repositioning of mitochondria. Our results show that blocking GBF1 function promotes dynein- and Miro-dependent retrograde mitochondrial transport along microtubules towards the microtubule-organizing center, where they form an interconnected network.

Indexed as

ADP-Ribosylation Factor 1Brefeldin ACells, CulturedDyneinsGuanine Nucleotide Exchange FactorsHeLa CellsHumansMicrotubulesMitochondriaMitochondrial ProteinsMutationPyridinesQuinolinesRetinal Pigment Epitheliumrho GTP-Binding ProteinsRNA InterferenceADP-Ribosylation Factor 1ARF1 protein, humanBrefeldin ADyneinsGBF1 protein, humangolgicide AGuanine Nucleotide Exchange FactorsMitochondrial ProteinsPyridinesQuinolinesrho GTP-Binding ProteinsRHOT2 protein, human

Identifiers

PMID30459446
PMCPMC6244289
OpenAlexW2901044762

What OpenQuestion holds

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LicenceCC BY
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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.