Evidence map›Paper›PMID 27694331›Full record

ArticleMolecular & cellular proteomics : MCP2016

A Role for Human N-alpha Acetyltransferase 30 (Naa30) in Maintaining Mitochondrial Integrity.

Petra Van Damme, Thomas V Kalvik, Kristian K Starheim, Veronique Jonckheere, Line M Myklebust, Gerben Menschaert, Jan Erik Varhaug, Kris Gevaert, Thomas Arnesen

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.9field-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

31 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Gene Expression Dysregulation in Whole Blood of Patients withInternational journal of molecular sciences · 2024
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  6. Acetyltransferase in cardiovascular disease and aging.The journal of cardiovascular aging · 2024
    Article
  7. Article
  8. Article
  9. Impact of Protein NLife (Basel, Switzerland) · 2023
    Review
  10. Article
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  14. Article
  15. 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

9 authors at 4 institutions in 2 countries.

Petra Van DammeFrom the ‡Medical Biotechnology Center, VIB, B-9000 Ghent, Belgium; petra.vandamme@vib-ugent.be.ORCID 0000-0001-9090-027X
Thomas V Kalvik¶Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway.
Kristian K Starheim¶Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway.
Veronique JonckheereFrom the ‡Medical Biotechnology Center, VIB, B-9000 Ghent, Belgium.
Line M Myklebust¶Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway.
Gerben Menschaert‡‡Department of Mathematical Modeling, Statistics and Bioinformatics, Ghent University, B-9000 Ghent, Belgium.
Jan Erik Varhaug‖Department of Clinical Science, University of Bergen, N-5020 Bergen, Norway.
Kris GevaertFrom the ‡Medical Biotechnology Center, VIB, B-9000 Ghent, Belgium.
Thomas Arnesen¶Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway.
University of Bergen · NOGhent University · BENorwegian University of Science and Technology · NOVIB-UGent Center for Medical Biotechnology · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-terminal acetylation (Nt-acetylation) by N-terminal acetyltransferases (NATs) is one of the most common protein modifications in eukaryotes. The NatC complex represents one of three major NATs of which the substrate profile remains largely unexplored. Here, we defined the in vivo human NatC Nt-acetylome on a proteome-wide scale by combining knockdown of its catalytic subunit Naa30 with positional proteomics. We identified 46 human NatC substrates, expanding our current knowledge on the substrate repertoire of NatC which now includes proteins harboring Met-Leu, Met-Ile, Met-Phe, Met-Trp, Met-Val, Met-Met, Met-His and Met-Lys N termini. Upon Naa30 depletion the expression levels of several organellar proteins were found reduced, in particular mitochondrial proteins, some of which were found to be NatC substrates. Interestingly, knockdown of Naa30 induced the loss of mitochondrial membrane potential and fragmentation of mitochondria. In conclusion, NatC Nt-acetylates a large variety of proteins and is essential for mitochondrial integrity and function.

Indexed as

AcetylationCell Line, TumorGene Knockdown TechniquesHeLa CellsHumansMitochondrial ProteinsN-Terminal Acetyltransferase CProtein BindingProtein Interaction MapsProteomicsSubstrate SpecificityMitochondrial ProteinsNAA30 protein, humanN-Terminal Acetyltransferase C

Identifiers

PMID27694331
PMCPMC5098035
OpenAlexW2546624599

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.