Mitochondrial localization of SESN2.

Autor: Kovaleva IE; Belozersky Institute of Physico-Chemical Biology, Moscow, Russia., Tokarchuk AV; Belozersky Institute of Physico-Chemical Biology, Moscow, Russia., Zheltukhin AO; School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin, Ireland.; Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia., Dalina AA; School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin, Ireland.; Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia., Safronov GG; Belozersky Institute of Physico-Chemical Biology, Moscow, Russia.; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia., Evstafieva AG; Belozersky Institute of Physico-Chemical Biology, Moscow, Russia.; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia., Lyamzaev KG; Belozersky Institute of Physico-Chemical Biology, Moscow, Russia.; Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia., Chumakov PM; Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia., Budanov AV; School of Biochemistry and Immunology, Trinity Biomedical Sciences Institute, Trinity College Dublin, Dublin, Ireland.; Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
Jazyk: angličtina
Zdroj: PloS one [PLoS One] 2020 Apr 14; Vol. 15 (4), pp. e0226862. Date of Electronic Publication: 2020 Apr 14 (Print Publication: 2020).
DOI: 10.1371/journal.pone.0226862
Abstrakt: 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.
Competing Interests: The authors have declared that no competing interests exist.
Databáze: MEDLINE
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