Evidence map›Paper›PMID 30894073›Full record

ArticleAutophagy2019

Loss of MIEF1/MiD51 confers susceptibility to BAX-mediated cell death and PINK1-PRKN-dependent mitophagy.

Hongxu Xian, Yih-Cherng Liou

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
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  7. Mitophagy in Hypertensive Cardiac Hypertrophy: Mechanisms and Therapeutic Implications.Journal of clinical hypertension (Greenwich, Conn.) · 2025
    Review
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  17. Mitochondria in health, disease, and aging.Physiological reviews · 2023
    Review
  18. Review
  19. Article
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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

2 authors at 1 institution in 1 country.

Hongxu XianDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, Singapore.
Yih-Cherng LiouDepartment of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, Singapore.ORCID 0000-0003-0149-6856
National University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial dynamics is highly implicated in a plethora of cellular processes including apoptosis and mitophagy. However, little is known about the scope and precise functions of mitochondrial dynamics proteins for mitochondrial quality control and cellular homeostasis. Whether mitochondrial dynamics proteins serve in cellular processes reliant on mitochondrial fission-fusion is still not fully explored. MIEF1/MiD51 (mitochondrial elongation factor 1) is known to promote mitochondrial fission via the recruitment of GTPase protein DNM1L/DRP1 (dynamin 1 like), but the fundamental understandings of MIEF1 for mitochondrial-dependent cellular processes are largely elusive. Here, we report novel roles of MIEF1 in responding to apoptotic stimuli and mitochondrial damage. Given our result that staurosporine (STS) treatment induced the degradation of MIEF1 via the ubiquitin-proteasome system (UPS), we are motivated to explore the role of MIEF1 in apoptosis. MIEF1 loss triggered the imbalance of BCL2 family members on the mitochondria, consequently initiating the translocation of BAX onto the mitochondria, catalyzing the decrease of mitochondrial membrane potential and promoting the release of DIABLO/SMAC (diablo IAP-binding mitochondrial protein) and CYCS (cytochrome c, somatic). We further demonstrate that MIEF1 deficiency impaired mitochondrial respiration and induced mitochondrial oxidative stress, sensitizing cells to PINK1-PRKN-mediated mitophagy. The recruitment of PRKN to depolarized mitochondria modulated the UPS-dependent degradation of MFN2 (mitofusin 2) and FIS1 (fission, mitochondrial 1) specifically, to further promote mitophagy. Our findings uncover a bridging role of MIEF1 integrating cell death and mitophagy, unlikely dependent on mitochondrial dynamics, implying new insights to mechanisms determining cellular fate.

Indexed as

ApoptosisApoptosis Regulatory Proteinsbcl-2-Associated X Proteinbcl-X ProteinDynaminsGTP PhosphohydrolasesHEK293 CellsHeLa CellsHumansMembrane Potential, MitochondrialMembrane ProteinsMitochondriaMitochondrial DynamicsMitochondrial ProteinsMitophagyPeptide Elongation FactorsApoptosis Regulatory ProteinsBAX protein, humanbcl-2-Associated X ProteinBCL2L1 protein, humanbcl-X ProteinDIABLO protein, humanDNM1L protein, humanDynaminsFIS1 protein, humanGTP PhosphohydrolasesMembrane ProteinsMFN2 protein, humanMiD51 protein, mouseMIEF1 protein, humanMitochondrial Proteinsparkin proteinPeptide Elongation FactorsProteasome Endopeptidase ComplexProtein KinasesPTEN-Induced Putative KinaseReactive Oxygen SpeciesReceptors, Cytoplasmic and NuclearStaurosporineUbiquitin-Protein LigasesApoptosisBAXMIEF1mitochondriamitophagy

Identifiers

PMID30894073
PMCPMC6844504
OpenAlexW2923019118

What OpenQuestion holds

Textmetadata
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.