Evidence map›Paper›PMID 28033361›Full record

ArticlePloS one2016

The Role of Mitochondrial Non-Enzymatic Protein Acylation in Ageing.

Shin Yee Hong, Li Theng Ng, Li Fang Ng, Takao Inoue, Nicholas S Tolwinski, Thilo Hagen, Jan Gruber

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. NADAntioxidants & redox signaling · 2023
    Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Proteome changes in the agingInternational journal of mass spectrometry · 2018
    Article
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.

Shin Yee HongDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.
Li Theng NgDepartment of Pharmacology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.
Li Fang NgDepartment of Science, Yale- NUS College, Singapore, Singapore.
Takao InoueDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.
Nicholas S TolwinskiDepartment of Science, Yale- NUS College, Singapore, Singapore.
Thilo HagenDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.
Jan GruberDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.
National University of Singapore · SGYale-NUS College · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In recent years, various large-scale proteomic studies have demonstrated that mitochondrial proteins are highly acylated, most commonly by addition of acetyl and succinyl groups. These acyl modifications may be enzyme catalysed but can also be driven non-enzymatically. The latter mechanism is promoted in mitochondria due to the nature of the mitochondrial microenvironment, which is alkaline and contains high concentrations of acyl-CoA species. Protein acylation may modify enzyme activity, typically inhibiting it. We posited that organismal ageing might be accompanied by an accumulation of acylated proteins, especially in mitochondria, and that this might compromise mitochondrial function and contribute to ageing. In this study, we used R. norvegicus, C. elegans and D. melanogaster to compare the acylation status of mitochondrial proteins between young and old animals. We observed a specific age-dependent increase in protein succinylation in worms and flies but not in rat. Rats have two substrate-specific mitochondrial deacylases, SIRT3 and SIRT5 while both flies and worms lack these enzymes. We propose that accumulation of mitochondrial protein acylation contributes to age-dependent mitochondrial functional decline and that SIRT3 and SIRT5 enzymes may promote longevity through regulation of mitochondrial protein acylation during ageing.

Indexed as

AcylationAgingAnimalsCaenorhabditis elegansDrosophila melanogasterLysineMitochondriaMitochondrial ProteinsProteomicsRatsSirtuin 3LysineMitochondrial ProteinsSirtuin 3

Identifiers

PMID28033361
PMCPMC5199114
OpenAlexW2567446650

What OpenQuestion holds

Textmetadata
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.