Evidence map›Paper›PMID 32287270›Full record

ArticlePloS one2020

Mitochondrial localization of SESN2.

Irina E Kovaleva, Artem V Tokarchuk, Andrei O Zheltukhin, Alexandra A Dalina, Grigoriy G Safronov, Alexandra G Evstafieva, Konstantin G Lyamzaev, Peter M Chumakov, Andrei V Budanov

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2020. 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
2.2field-weighted citation impact, top 13% 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, 34 citations in OpenAlex.

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  8. Mitochondrial Biogenesis in Skeletal Muscle.Advances in experimental medicine and biology · 2025
    Review
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  11. Article
  12. Review
  13. Review
  14. Sestrins in Physiological Stress Responses.Annual review of physiology · 2021
    Review
  15. Review
  16. Article
  17. 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

9 authors at 3 institutions in 2 countries.

Irina E KovalevaBelozersky Institute of Physico-Chemical Biology, Moscow, Russia.
Artem V TokarchukBelozersky Institute of Physico-Chemical Biology, Moscow, Russia.
Andrei O ZheltukhinSchool of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin, Ireland.
Alexandra A DalinaSchool of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin, Ireland.
Grigoriy G SafronovBelozersky Institute of Physico-Chemical Biology, Moscow, Russia.
Alexandra G EvstafievaBelozersky Institute of Physico-Chemical Biology, Moscow, Russia.
Konstantin G LyamzaevBelozersky Institute of Physico-Chemical Biology, Moscow, Russia.
Peter M ChumakovCenter for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.ORCID 0000-0002-8078-2908
Andrei V BudanovSchool of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin, Ireland.ORCID 0000-0001-9505-1908
Engelhardt Institute of Molecular Biology · RULomonosov Moscow State University · RUPhysico-Technical Institute · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SESN2 is a member of the evolutionarily conserved sestrin protein family found in most of the Metazoa species. The SESN2 gene is transcriptionally activated by many stress factors, including metabolic derangements, reactive oxygen species (ROS), and DNA-damage. As a result, SESN2 controls ROS accumulation, metabolism, and cell viability. The best-known function of SESN2 is the inhibition of the mechanistic target of rapamycin complex 1 kinase (mTORC1) that plays a central role in support of cell growth and suppression of autophagy. SESN2 inhibits mTORC1 activity through interaction with the GATOR2 protein complex preventing an inhibitory effect of GATOR2 on the GATOR1 protein complex. GATOR1 stimulates GTPase activity of the RagA/B small GTPase, the component of RagA/B:RagC/D complex, preventing mTORC1 translocation to the lysosomes and its activation by the small GTPase Rheb. Despite the well-established role of SESN2 in mTORC1 inhibition, other SESN2 activities are not well-characterized. We recently showed that SESN2 could control mitochondrial function and cell death via mTORC1-independent mechanisms, and these activities might be explained by direct effects of SESN2 on mitochondria. In this work, we examined mitochondrial localization of SESN2 and demonstrated that SESN2 is located on mitochondria and can be directly involved in the regulation of mitochondrial functions.

Indexed as

A549 CellsAnimalsCaenorhabditis elegansCell FractionationCell RespirationCytosolHumansMitochondriaNuclear ProteinsReactive Oxygen SpeciesSestrinsNuclear ProteinsReactive Oxygen SpeciesSESN2 protein, humanSestrins

Identifiers

PMID32287270
PMCPMC7156099
OpenAlexW3015230609

What OpenQuestion holds

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LicenceCC BY
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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.