Evidence map›Paper›PMID 34674699›Full record

ArticleBMC biology2021

MIEF1/2 orchestrate mitochondrial dynamics through direct engagement with both the fission and fusion machineries.

Rong Yu, Tong Liu, Shao-Bo Jin, Maria Ankarcrona, Urban Lendahl, Monica Nistér, Jian Zhao

Open access · goldAbstract read
In one paragraph

Article in BMC biology, 2021. 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
1.6field-weighted citation impact, top 16% 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, 30 citations in OpenAlex.

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  16. Mitochondrial dynamics proteins as emerging drug targets.Trends in pharmacological sciences · 2023
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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

7 authors at 2 institutions in 1 country.

Rong YuDepartment of Oncology-Pathology, Karolinska Institutet, BioClinicum, Visionsgatan 4, Karolinska University Hospital Solna, SE-171 64, Solna, Sweden.
Tong LiuDepartment of Oncology-Pathology, Karolinska Institutet, BioClinicum, Visionsgatan 4, Karolinska University Hospital Solna, SE-171 64, Solna, Sweden.
Shao-Bo JinDepartment of Cell and Molecular Biology, Karolinska Institutet, Biomedicum, Solnavägen 9, SE-171 77, Stockholm, Sweden.
Maria AnkarcronaDepartment of Neurobiology, Care Sciences and Society, Center for Alzheimer Research, Division of Neurogeriatrics, Karolinska Institutet, BioClinicum J9:20, Visionsgatan 4, SE-171 64, Solna, Sweden.
Urban LendahlDepartment of Cell and Molecular Biology, Karolinska Institutet, Biomedicum, Solnavägen 9, SE-171 77, Stockholm, Sweden.
Monica Nistér *Department of Oncology-Pathology, Karolinska Institutet, BioClinicum, Visionsgatan 4, Karolinska University Hospital Solna, SE-171 64, Solna, Sweden. monica.nister@ki.se.
Jian Zhao *Department of Oncology-Pathology, Karolinska Institutet, BioClinicum, Visionsgatan 4, Karolinska University Hospital Solna, SE-171 64, Solna, Sweden. jian.zhao@ki.se.ORCID 0000-0001-5659-730X
Karolinska University Hospital · SEKarolinska Institutet · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMitochondrial dynamics is the result of a dynamic balance between fusion and fission events, which are driven via a set of mitochondria-shaping proteins. These proteins are generally considered to be binary components of either the fission or fusion machinery, but potential crosstalk between the fission and fusion machineries remains less explored. In the present work, we analyzed the roles of mitochondrial elongation factors 1 and 2 (MIEF1/2), core components of the fission machinery in mammals.

resultsWe show that MIEFs (MIEF1/2), besides their action in the fission machinery, regulate mitochondrial fusion through direct interaction with the fusion proteins Mfn1 and Mfn2, suggesting that MIEFs participate in not only fission but also fusion. Elevated levels of MIEFs enhance mitochondrial fusion in an Mfn1/2- and OPA1-dependent but Drp1-independent manner. Moreover, mitochondrial localization and self-association of MIEFs are crucial for their fusion-promoting ability. In addition, we show that MIEF1/2 can competitively decrease the interaction of hFis1 with Mfn1 and Mfn2, alleviating hFis1-induced mitochondrial fragmentation and contributing to mitochondrial fusion.

conclusionsOur study suggests that MIEFs serve as a central hub that interacts with and regulates both the fission and fusion machineries, which uncovers a novel mechanism for balancing these opposing forces of mitochondrial dynamics in mammals.

Indexed as

DynaminsMitochondrial DynamicsAnimalsMitochondriaMitochondrial ProteinsPeptide Elongation FactorsDynaminsMitochondrial ProteinsPeptide Elongation FactorsDrp1hFis1Mfn1/2MIEF1/2Mitochondrial dynamicsMitochondrial fissionMitochondrial fusion

Identifiers

PMID34674699
PMCPMC8532385
OpenAlexW3205050010

What OpenQuestion holds

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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.