Evidence map›Paper›PMID 27932492›Full record

ArticleMolecular biology of the cell2017

Novel regulatory roles of Mff and Drp1 in E3 ubiquitin ligase MARCH5-dependent degradation of MiD49 and Mcl1 and control of mitochondrial dynamics.

Edward Cherok, Shan Xu, Sunan Li, Shweta Das, W Alex Meltzer, Michal Zalzman, Chunxin Wang, Mariusz Karbowski

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

63 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Review
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  4. Subcellular Stress Markers in Epithelial Ovarian Cancer.International journal of molecular sciences · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. MARCH5 promotes aerobic glycolysis to facilitate ovarian cancer progression via ubiquitinating MPC1.Apoptosis : an international journal on programmed cell death · 2024
    Article
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  12. Review
  13. Article
  14. Article
  15. Article
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  20. Article

3 more citing papers are in PubMed but not listed here.

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 1 country.

Edward CherokCenter for Biomedical Engineering and Technology, University of Maryland School of Medicine, Baltimore, MD 21201.
Shan XuCenter for Biomedical Engineering and Technology, University of Maryland School of Medicine, Baltimore, MD 21201.
Sunan LiCenter for Biomedical Engineering and Technology, University of Maryland School of Medicine, Baltimore, MD 21201.
Shweta DasCenter for Biomedical Engineering and Technology, University of Maryland School of Medicine, Baltimore, MD 21201.
W Alex MeltzerDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201.
Michal ZalzmanDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201.
Chunxin WangBiochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
Mariusz KarbowskiCenter for Biomedical Engineering and Technology, University of Maryland School of Medicine, Baltimore, MD 21201.
University of Maryland, Baltimore · USNational Institutes of Health · US

Funding

The role of mitochondria-associated RING finger proteins in mitochondrial qualityR01GM083131 · NIGMS · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI KARBOWSKI, MARIUSZ · 2008 to 2012
$1.3M
NIGMS NIH HHS R01 GM083131
6 · The paper itself

Abstract

MARCH5, an OMM-associated E3 ubiquitin ligase, controls mitochondrial function. Despite its importance, the mechanism and factors controlling MARCH5 activity are largely unknown. Here we report that the MARCH5 C-terminal domain plays a critical role in degradation of MARCH5 substrates, likely by facilitating release of ubiquitinated proteins from the OMM. We also found that the mitochondrial fission proteins Drp1 and Mff negatively regulate MARCH5's activity toward MiD49 and Mcl1. Knockouts of either Drp1 or Mff led to reduced expression, shorter half-lives, and increased ubiquitination of MiD49 and Mcl1. Effects of Mff and Drp1 depletion on degradation rates and ubiquitination of Mcl1 and MiD49 were eliminated in Drp1

Indexed as

Cell Culture TechniquesDynaminsGTP PhosphohydrolasesHCT116 CellsHumansMembrane ProteinsMicrotubule-Associated ProteinsMitochondriaMitochondrial DynamicsMitochondrial MembranesMitochondrial ProteinsPeptide Elongation FactorsUbiquitinationUbiquitin-Protein LigasesDNM1L protein, humanDynaminsGTP PhosphohydrolasesMARCHF5 protein, humanMembrane ProteinsMff protein, humanMicrotubule-Associated ProteinsMIEF2 protein, humanMitochondrial ProteinsPeptide Elongation FactorsUbiquitin-Protein Ligases

Identifiers

PMID27932492
PMCPMC5341724
OpenAlexW2560071953

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.