Evidence map›Paper›PMID 30530489›Full record

ArticleThe Journal of biological chemistry2019

Lysine methylation by the mitochondrial methyltransferase FAM173B optimizes the function of mitochondrial ATP synthase.

Jędrzej M Małecki, Hanneke L D M Willemen, Rita Pinto, Angela Y Y Ho, Anders Moen, Ingrid F Kjønstad, Boudewijn M T Burgering, Fried Zwartkruis, Niels Eijkelkamp, Pål Ø Falnes

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

  1. Pharmacological and Genetic Approaches to Downregulate FIS1 Mitigate Neuropathic Pain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  2. Review
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  5. Article
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  8. Protein methylation in mitochondria.The Journal of biological chemistry · 2022
    Review
  9. Article
  10. Mitochondria and sensory processing in inflammatory and neuropathic pain.Frontiers in pain research (Lausanne, Switzerland) · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  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

10 authors at 2 institutions in 2 countries.

Jędrzej M MałeckiDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, 0316 Oslo, Norway. Electronic address: j.m.malecki@ibv.uio.no.
Hanneke L D M WillemenLaboratory of Translational Immunology (LTI), 3584 EA Utrecht, The Netherlands.
Rita PintoDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, 0316 Oslo, Norway.
Angela Y Y HoDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, 0316 Oslo, Norway.
Anders MoenDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, 0316 Oslo, Norway.
Ingrid F KjønstadDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, 0316 Oslo, Norway.
Boudewijn M T BurgeringMolecular Cancer Research, Center for Molecular Medicine, Oncode Institute, University Medical Center Utrecht, Utrecht University, 3584 EA Utrecht, The Netherlands.
Fried ZwartkruisMolecular Cancer Research, Center for Molecular Medicine, Oncode Institute, University Medical Center Utrecht, Utrecht University, 3584 EA Utrecht, The Netherlands.
Niels EijkelkampLaboratory of Translational Immunology (LTI), 3584 EA Utrecht, The Netherlands.
Pål Ø FalnesDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, 0316 Oslo, Norway. Electronic address: pal.falnes@ibv.uio.no.
University of Oslo · NOUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine methylation is an important post-translational modification that is also present on mitochondrial proteins, but the mitochondrial lysine-specific methyltransferases (KMTs) responsible for modification are in most cases unknown. Here, we set out to determine the function of human family with sequence similarity 173 member B (FAM173B), a mitochondrial methyltransferase (MTase) reported to promote chronic pain. Using bioinformatics analyses and biochemical assays, we found that FAM173B contains an atypical, noncleavable mitochondrial targeting sequence responsible for its localization to mitochondria. Interestingly, CRISPR/Cas9-mediated KO of FAM173B in mammalian cells abrogated trimethylation of Lys-43 in ATP synthase c-subunit (ATPSc), a modification previously reported as ubiquitous among metazoans. ATPSc methylation was restored by complementing the KO cells with enzymatically active human FAM173B or with a putative FAM173B orthologue from the nematode

Indexed as

AnimalsCell LineComputational BiologyHeLa CellsHistone-Lysine N-MethyltransferaseHumansLysineMethylationMiceMitochondriaMitochondrial Proton-Translocating ATPasesATPSCKMT protein, humanHistone-Lysine N-MethyltransferaseLysineMitochondrial Proton-Translocating ATPasesATPSc-KMTATP synthaseATP synthase c-subunitF1F0-ATPaseFAM173BKMTmetabolic regulationmethyltransferasemitochondriamitochondrial respiratory chain complexoxidative phosphorylationpost-translational modification (PTM)protein lysine methylationprotein methylation

Identifiers

PMID30530489
PMCPMC6349101
OpenAlexW2904673898

What Socratic 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 Socratic graph.