Evidence map›Paper›PMID 38267654›Full record

ArticleThe EMBO journal2024

Shared structural features of Miro binding control mitochondrial homeostasis.

Christian Covill-Cooke, Brian Kwizera, Guillermo López-Doménech, Caleb Od Thompson, Ngaam J Cheung, Ema Cerezo, Martin Peterka, Josef T Kittler, Benoît Kornmann

Abstract read
In one paragraph

Article in The EMBO journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

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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.

Christian Covill-CookeDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. christian.covill-cooke@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0002-4479-8734
Brian KwizeraDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Guillermo López-DoménechDepartment of Neuroscience, Physiology and Pharmacology, University College London, Gower Street, London, WC1E 6BT, UK.ORCID http://orcid.org/0000-0002-3114-2082
Caleb Od ThompsonDepartment of Neuroscience, Physiology and Pharmacology, University College London, Gower Street, London, WC1E 6BT, UK.
Ngaam J CheungDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Ema CerezoDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Martin PeterkaInstitute of Biochemistry, ETH Zurich, 8093, Zurich, Switzerland.
Josef T KittlerDepartment of Neuroscience, Physiology and Pharmacology, University College London, Gower Street, London, WC1E 6BT, UK.ORCID http://orcid.org/0000-0002-3437-9456
Benoît KornmannDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK. benoit.kornmann@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0002-6030-8555

Funding

UKRI | MRC | Medical Research Foundation 2397875Wellcome TrustWellcome Trust (WT) 214291/Z/18/ZWellcome Trust (WT) 222/519/Z/21/ZWellcome Trust (WT) 223202/Z/21/Z
6 · The paper itself

Abstract

Miro proteins are universally conserved mitochondrial calcium-binding GTPases that regulate a multitude of mitochondrial processes, including transport, clearance, and lipid trafficking. The exact role of Miro in these functions is unclear but involves binding to a variety of client proteins. How this binding is operated at the molecular level and whether and how it is important for mitochondrial health, however, remains unknown. Here, we show that known Miro interactors-namely, CENPF, Trak, and MYO19-all use a similar short motif to bind the same structural element: a highly conserved hydrophobic pocket in the first calcium-binding domain of Miro. Using these Miro-binding motifs, we identified direct interactors de novo, including MTFR1/2/1L, the lipid transporters Mdm34 and VPS13D, and the ubiquitin E3-ligase Parkin. Given the shared binding mechanism of these functionally diverse clients and its conservation across eukaryotes, we propose that Miro is a universal mitochondrial adaptor coordinating mitochondrial health.

Indexed as

CalciumMitochondriaHomeostasisHumansLipidsMitochondrial ProteinsProteinsrho GTP-Binding ProteinsUbiquitin-Protein LigasesCalciumLipidsMitochondrial ProteinsProteinsrho GTP-Binding ProteinsUbiquitin-Protein LigasesVPS13D protein, humanAlphaFoldERMESLipid TransportMitophagyOrganelle Transport

Identifiers

PMID38267654
PMCPMC10897228

What OpenQuestion holds

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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.