Evidence map›Paper›PMID 31195097›Full record

ReviewMitochondrion2019

Consequences of inner mitochondrial membrane protein misfolding.

Liam P Coyne, Xin Jie Chen

Open access · greenAbstract readReview
In one paragraph

Review in Mitochondrion, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Mitochondrial proteostasis regulated by CRL5Communications biology · 2025
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Genes · 2021
    Review
  14. Review
  15. Molecular Mechanisms of Fuchs and Congenital Hereditary Endothelial Corneal Dystrophies.Reviews of physiology, biochemistry and pharmacology · 2020
    Review
  16. 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

2 authors at 1 institution in 1 country.

Liam P CoyneDepartments of Biochemistry and Molecular Biology, State University of New York Upstate Medical University, Syracuse, NY, USA.
Xin Jie ChenDepartments of Biochemistry and Molecular Biology, State University of New York Upstate Medical University, Syracuse, NY, USA; Neuroscience and Physiology, State University of New York Upstate Medical University, Syracuse, NY, USA. Electronic address: chenx@upstate.edu.
SUNY Upstate Medical University · US

Funding

Ant-induced cell death and human degenerative diseasesR01AG023731 · NIA · UT SOUTHWESTERN MEDICAL CENTER · PI CHEN, XIN JIE · 2005 to 2014
$2.4M
Mechanism of Mitochondria-induced Progressive Muscle WastingR01AG061204 · NIA · UPSTATE MEDICAL UNIVERSITY · PI CHEN, XIN JIE · 2019 to 2023
$2.0M
Mechanism of mitochondria-induced cell degeneration in the central nervous systemR56AG023731 · NIA · UPSTATE MEDICAL UNIVERSITY · PI CHEN, XIN JIE · 2017 to 2017
$405k
Mechanism of age-dependent neuromuscular degeneration caused by protein misfolding on the inner mitochondrial membraneF30AG060702 · NIA · UPSTATE MEDICAL UNIVERSITY · PI COYNE, LIAM PATRICK · 2018 to 2021
$201k
NIA NIH HHS F30 AG060702NIA NIH HHS R01 AG023731NIA NIH HHS R01 AG061204NIA NIH HHS R56 AG023731
6 · The paper itself

Abstract

Proteins embedded in the inner mitochondrial membrane (IMM) perform essential cellular functions. Maintaining the folding state of these proteins is therefore of the utmost importance, and this is ensured by IMM chaperones and proteases that refold and degrade unassembled and misfolded proteins. However, the physiological consequences specific to IMM protein misfolding remain obscure because deletion of these chaperones/proteases (the typical experimental strategy) often affects many mitochondrial processes other than protein folding and turnover. Thus, novel experimental systems are needed to evaluate the direct effects of misfolded protein on the membrane. Such a system has been developed in recent years. Studies suggest that numerous pathogenic mutations in isoform 1 of adenine nucleotide translocase (Ant1) cause its misfolding on the IMM. In this review, we first discuss potential mechanisms by which dominant Ant1 mutations may cause disease, highlighting IMM protein misfolding, per se, as a likely pathological factor. Then we discuss the intramitochondrial effects of Ant1 misfolding such as IMM proteostatic stress, respiratory chain dysfunction, and mtDNA instability. Finally, we summarize the mounting evidence that IMM proteostatic stress can perturb mitochondrial protein import to cause the toxic accumulation of mitochondrial proteins in the cytosol: a cell stress mechanism termed mitochondrial Precursor Overaccumulation Stress (mPOS).

Indexed as

Adenine Nucleotide Translocator 1Molecular ChaperonesMutationProtein FoldingProteostasis DeficienciesAnimalsHumansMitochondrial MembranesProtein TransportAdenine Nucleotide Translocator 1Molecular ChaperonesAnt1MisfoldingMitochondriaMitochondrial carriermPOS

Identifiers

PMID31195097
PMCPMC6885533
OpenAlexW2949387347

What OpenQuestion holds

Textmetadata
LicenceTDM
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.