Updated on 2022/12/01

写真a

 
INNOKENTEV ALEKSEI
 
Organization
Academic Assembly Institute of Medicine and Dentistry Specially Appointed Assistant Professor
Graduate School of Medical and Dental Sciences Specially Appointed Assistant Professor
Title
Specially Appointed Assistant Professor
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Degree

  • 博士(医学) ( 2021.3   仙台大学 )

  • PhD(Biological Science) ( 2021.1 )

Research Interests

  • The Far complex

  • Yeast

  • Mitophagy

  • Atg32

  • Autophagy

Research Areas

  • Life Science / Molecular biology

Research History (researchmap)

  • Niigata University   Graduate School of Medical and Dental Sciences   Cellular Biology   Assistant professor for special purpose

    2021.4

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    Country:Japan

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Research History

  • Niigata University   Graduate School of Medical and Dental Sciences   Specially Appointed Assistant Professor

    2021.4

  • Niigata University   Institute of Medicine and Dentistry, Academic Assembly   Specially Appointed Assistant Professor

    2021.4

  • Niigata University   Graduate School of Medical and Dental Sciences   Specially Appointed Assistant

    2020.11 - 2021.3

Education

  • Niigata University   Graduate School of Medical and Dental Sciences   Cellular Physiology

    2018.10 - 2021.3

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    Country: Japan

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  • The Far Eastern State Medical University   Clinical Laboratory Diagnostics

    2016.9 - 2017.7

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    Country: Russian Federation

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  • The Far Eastern State Medical University   Medical Biochemistry

    2010.9 - 2016.7

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    Country: Russian Federation

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Papers

  • Mitophagy in Yeast: Molecular Mechanism and Regulation

    Aleksei Innokentev, Tomotake Kanki

    Cells   10 ( 12 )   3569 - 3569   2021.12

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    Publishing type:Research paper (scientific journal)   Publisher:MDPI AG  

    Mitophagy is a type of autophagy that selectively degrades mitochondria. Mitochondria, known as the “powerhouse of the cell”, supply the majority of the energy required by cells. During energy production, mitochondria produce reactive oxygen species (ROS) as byproducts. The ROS damage mitochondria, and the damaged mitochondria further produce mitochondrial ROS. The increased mitochondrial ROS damage cellular components, including mitochondria themselves, and leads to diverse pathologies. Accordingly, it is crucial to eliminate excessive or damaged mitochondria to maintain mitochondrial homeostasis, in which mitophagy is believed to play a major role. Recently, the molecular mechanism and physiological role of mitophagy have been vigorously studied in yeast and mammalian cells. In yeast, Atg32 and Atg43, mitochondrial outer membrane proteins, were identified as mitophagy receptors in budding yeast and fission yeast, respectively. Here we summarize the molecular mechanisms of mitophagy in yeast, as revealed by the analysis of Atg32 and Atg43, and review recent progress in our understanding of mitophagy induction and regulation in yeast.

    DOI: 10.3390/cells10123569

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  • Mitophagy regulation mediated by the Far complex in yeast International journal

    Kentaro Furukawa, Aleksei Innokentev, Tomotake Kanki

    Autophagy   17 ( 4 )   1042 - 1043   2021.4

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Informa UK Limited  

    Mitochondrial autophagy (mitophagy) selectively degrades mitochondria and plays an important role in mitochondrial homeostasis. In the yeast Saccharomyces cerevisiae, the phosphorylation of the mitophagy receptor Atg32 by casein kinase 2 is essential for mitophagy, whereas this phosphorylation is counteracted by the protein phosphatase Ppg1. Although Ppg1 functions cooperatively with the Far complex (Far3, Far7, Far8, Vps64/Far9, Far10 and Far11), their relationship and the underlying phosphoregulatory mechanism of Atg32 remain unclear. Our recent study revealed: (i) the Far complex plays its localization-dependent roles, regulation of mitophagy and target of rapamycin complex 2 (TORC2) signaling, via the mitochondria- and endoplasmic reticulum (ER)-localized Far complexes, respectively; (ii) Ppg1 and Far11 form a subcomplex, and Ppg1 activity is required to assemble the sub- and core-Far complexes; (iii) association and dissociation between the Far complex and Atg32 are crucial determinants for mitophagy regulation. Here, we summarize our findings and discuss unsolved issues.

    DOI: 10.1080/15548627.2021.1885184

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  • Association and dissociation between the mitochondrial Far complex and Atg32 regulate mitophagy International journal

    Aleksei Innokentev, Kentaro Furukawa, Tomoyuki Fukuda, Tetsu Saigusa, Keiichi Inoue, Shun-ichi Yamashita, Tomotake Kanki

    eLife   9   2020.12

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:eLife Sciences Publications, Ltd  

    Mitophagy plays an important role in mitochondrial homeostasis. In yeast, the phosphorylation of the mitophagy receptor Atg32 by casein kinase 2 is essential for mitophagy. This phosphorylation is counteracted by the yeast equivalent of the STRIPAK complex consisting of the PP2A-like protein phosphatase Ppg1 and Far3-7-8-9-10-11 (Far complex), but the underlying mechanism remains elusive. Here we show that two subpopulations of the Far complex reside in the mitochondria and endoplasmic reticulum, respectively, and play distinct roles; the former inhibits mitophagy via Atg32 dephosphorylation, and the latter regulates TORC2 signaling. Ppg1 and Far11 form a subcomplex, and Ppg1 activity is required for the assembling integrity of Ppg1-Far11-Far8. The Far complex preferentially interacts with phosphorylated Atg32, and this interaction is weakened by mitophagy induction. Furthermore, the artificial tethering of Far8 to Atg32 prevents mitophagy. Taken together, the Ppg1-mediated Far complex formation and its dissociation from Atg32 are crucial for mitophagy regulation.

    DOI: 10.7554/elife.63694

    PubMed

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    Other Link: https://cdn.elifesciences.org/articles/63694/elife-63694-v1.xml

  • Regulatory Mechanisms of Mitochondrial Autophagy: Lessons From Yeast

    Kentaro Furukawa, Aleksei Innokentev, Tomotake Kanki

    Frontiers in Plant Science   10   2019.11

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    Publishing type:Research paper (scientific journal)   Publisher:Frontiers Media SA  

    DOI: 10.3389/fpls.2019.01479

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Presentations

  • Association and dissociation between the mitochondrial Far complex and Atg32 regulate mitophagy

    Innokentev Aleksei

    2020.12 

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    Language:English   Presentation type:Oral presentation (general)  

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  • Association and dissociation between the mitochondrial Far complex and Atg32 regulate mitophagy

    Innokentev Aleksei

    2020.10 

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    Language:English   Presentation type:Oral presentation (general)  

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  • Association and dissociation between the mitochondrial Far complex and Atg32 regulate mitophagy

    Innokentev Aleksei

    1st Far East International Medical Congress (Russia)  2020.10 

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    Language:English   Presentation type:Oral presentation (general)  

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  • Analysis of the Ppg1-Far complex that negatively regulates mitophagy in yeast

    Innokentev Aleksei

    第12回オートファジー研究会 若手の会  2019.10 

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    Language:English   Presentation type:Poster presentation  

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  • Analysis of the Ppg1-Far complex that negatively regulates mitophagy in yeast

    Innokentev Aleksei

    第12回オートファジー研究会 若手の会  2019.10 

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    Language:English   Presentation type:Oral presentation (general)  

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  • Analysis of the Ppg1-Far complex that negatively regulates mitophagy in yeast

    Innokentev Aleksei

    2019.7 

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    Language:English   Presentation type:Poster presentation  

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Awards

  • Niigata University Student Award (President's Award)

    2021.4   Niigata University  

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  • Niigata University Young Medical Research Award - Mikan no kai #27

    2020.10   Niigata University   Association and dissociation between the mitochondrial Far complex and Atg32 regulate mitophagy

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Teaching Experience (researchmap)

  • Histological techniques for Medical Biochemistry students' practice

    2016.9
    -
    2018.5
    Institution name:The Far Eastern State Medical University

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Media Coverage

  • ミトコンドリアの恒常性維持 「マイトファジー」制御機構解明 ~新潟大グループが成果~ Newspaper, magazine

    2021.1

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