• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to previous page

Elucidation of the Far3- and Far7-mediated regulatory mechanism of mitochondrial autophagy in yeast

Research Project

Project/Area Number 22K15058
Research Category

Grant-in-Aid for Early-Career Scientists

Allocation TypeMulti-year Fund
Review Section Basic Section 43030:Functional biochemistry-related
Research InstitutionNiigata University

Principal Investigator

Innokentev Aleksei  新潟大学, 医歯学総合研究科, 特任助教 (10907439)

Project Period (FY) 2022-04-01 – 2024-03-31
Project Status Discontinued (Fiscal Year 2023)
Budget Amount *help
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2023: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Fiscal Year 2022: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
KeywordsMitophagy / Atg32 / Ppg1 / The Far complex / Yeast / Autophagy
Outline of Research at the Start

Mitophagy contributes to maintaining mitochondrial quality and quantity. The phosphorylation of the Atg32 is essential for mitophagy and is antagonistically regulated by CK2 and Ppg1. The Ppg1-binding partner Far complex is involved in Atg32 dephosphorylation. Apart from Atg32-Far8, interaction important for mitophagy regulation, it was found that Far3/Far7 interact with Atg32 independently of Far8. Thus, this study aims to clarify
① the structural basis for interaction between Far3/Far7 and Atg32
② the upstream signaling pathway regulating the dissociation between the Far complex and Atg32

Outline of Annual Research Achievements

Mitophagy sustains mitochondrial quality and quantity via Atg32 phosphorylation, involving the enigmatic Far complex interaction. This study seeked to clarify: 1) Far3/7's interplay with Atg32 2) The upstream signaling guiding this interaction.
Interestingly, experiments with Far3/7 phosphorylation mutants revealed no disruption in the Atg32-Far complex interaction. Exploring Far3/7 expression and degradation effects yielded no discernible impact. Likewise, autophagy-associated kinase assessment failed to influence the Atg32-Far complex connection. These findings underscore the intricate regulatory mechanisms behind mitophagy. While specifics of Atg32-Far complex interaction remain elusive, this study contributes to our understanding of mitochondrial quality and quantity control.

Report

(2 results)
  • 2023 Annual Research Report
  • 2022 Research-status Report

URL: 

Published: 2022-04-19   Modified: 2024-12-25  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi