Evidence map›Paper›PMID 33498827›Full record

ArticleInternational journal of molecular sciences2021

Regulation of the CoA Biosynthetic Complex Assembly in Mammalian Cells.

Jovana Baković, David López Martínez, Savvas Nikolaou, Bess Yi Kun Yu, Maria-Armineh Tossounian, Yugo Tsuchiya, Christopher Thrasivoulou, Valeriy Filonenko, Ivan Gout

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. PKAN pathogenesis and treatment.Molecular genetics and metabolism · 2022
    Review
  10. CoA in Health and Disease.International journal of molecular sciences · 2022
    Article
  11. Article
  12. Review
  13. 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

9 authors at 3 institutions in 2 countries.

Jovana BakovićDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.
David López MartínezDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.
Savvas NikolaouDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.ORCID 0000-0001-6936-5911
Bess Yi Kun YuDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.ORCID 0000-0002-4619-2226
Maria-Armineh TossounianDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.ORCID 0000-0003-3679-7376
Yugo TsuchiyaDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.
Christopher ThrasivoulouResearch Department of Cell and Developmental Biology, The Centre for Cell and Molecular Dynamics, University College London, London WC1E 6BT, UK.ORCID 0000-0001-9425-8624
Valeriy FilonenkoInstitute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, 03680 Kyiv, Ukraine.
Ivan GoutDepartment of Structural and Molecular Biology, University College London, London WC1E 6BT, UK.
Institute of Structural and Molecular Biology · GBNational Academy of Sciences of Ukraine · UAMRC Laboratory for Molecular Cell Biology · GB

Funding

Biotechnology and Biological Sciences Research Council BBSRC BB/L010410/1 and BB/S009027/1
6 · The paper itself

Abstract

Coenzyme A (CoA) is an essential cofactor present in all living cells. Under physiological conditions, CoA mainly functions to generate metabolically active CoA thioesters, which are indispensable for cellular metabolism, the regulation of gene expression, and the biosynthesis of neurotransmitters. When cells are exposed to oxidative or metabolic stress, CoA acts as an important cellular antioxidant that protects protein thiols from overoxidation, and this function is mediated by protein CoAlation. CoA and its derivatives are strictly maintained at levels controlled by nutrients, hormones, metabolites, and cellular stresses. Dysregulation of their biosynthesis and homeostasis has deleterious consequences and has been noted in a range of pathological conditions, including cancer, diabetes, Reye's syndrome, cardiac hypertrophy, and neurodegeneration. The biochemistry of CoA biosynthesis, which involves five enzymatic steps, has been extensively studied. However, the existence of a CoA biosynthetic complex and the mode of its regulation in mammalian cells are unknown. In this study, we report the assembly of all five enzymes that drive CoA biosynthesis, in HEK293/Pank1β and A549 cells, using the in situ proximity ligation assay. Furthermore, we show that the association of CoA biosynthetic enzymes is strongly upregulated in response to serum starvation and oxidative stress, whereas insulin and growth factor signaling downregulate their assembly.

Indexed as

Gene Expression RegulationOxidative StressA549 CellsBiosynthetic PathwaysCoenzyme AHEK293 CellsHumansInsulinIntercellular Signaling Peptides and ProteinsSignal TransductionCoenzyme AInsulinIntercellular Signaling Peptides and Proteinscoenzyme Acoenzyme A biosynthesisextracellular stimulioxidative stress

Identifiers

PMID33498827
PMCPMC7865483
OpenAlexW3123510228

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.