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Research Article

Iron Supply via NCOA4-Mediated Ferritin Degradation Maintains Mitochondrial Functions

Motoki Fujimaki, Norihiko Furuya, Shinji Saiki, Taku Amo, Yoko Imamichi, Nobutaka Hattori
Motoki Fujimaki
aDepartment of Neurology, Juntendo University School of Medicine, Tokyo, Japan
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Norihiko Furuya
aDepartment of Neurology, Juntendo University School of Medicine, Tokyo, Japan
bDivision for Development of Autophagy Modulating Drugs, Juntendo University Graduate School of Medicine, Tokyo, Japan
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  • ORCID record for Norihiko Furuya
Shinji Saiki
aDepartment of Neurology, Juntendo University School of Medicine, Tokyo, Japan
bDivision for Development of Autophagy Modulating Drugs, Juntendo University Graduate School of Medicine, Tokyo, Japan
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Taku Amo
cDepartment of Applied Chemistry, National Defense Academy, Yokosuka, Kanagawa, Japan
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Yoko Imamichi
aDepartment of Neurology, Juntendo University School of Medicine, Tokyo, Japan
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Nobutaka Hattori
aDepartment of Neurology, Juntendo University School of Medicine, Tokyo, Japan
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DOI: 10.1128/MCB.00010-19
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ABSTRACT

Iron is an essential nutrient for mitochondrial metabolic processes, including mitochondrial respiration. Ferritin complexes store excess iron and protect cells from iron toxicity. Therefore, iron stored in the ferritin complex might be utilized under iron-depleted conditions. In this study, we show that the inhibition of lysosome-dependent protein degradation by bafilomycin A1 and the knockdown of NCOA4, an autophagic receptor for ferritin, reduced mitochondrial respiration, respiratory chain complex assembly, and membrane potential under iron-sufficient conditions. However, autophagy did not contribute to degradation of the ferritin complex under iron-sufficient conditions. Knockout of the ferritin light chain, a subunit of the ferritin complex, inhibited ferritin degradation by decreasing interactions with NCOA4. However, ferritin light chain knockout did not affect mitochondrial functions under iron-sufficient conditions, and ferritin light chain knockout cells showed a rapid reduction of mitochondrial functions compared with wild-type cells under iron-depleted conditions. These results indicate that the constitutive degradation of the ferritin complex contributes to the maintenance of mitochondrial functions.

FOOTNOTES

    • Received 3 January 2019.
    • Returned for modification 28 January 2019.
    • Accepted 29 April 2019.
    • Accepted manuscript posted online 6 May 2019.
  • Supplemental material for this article may be found at https://doi.org/10.1128/MCB.00010-19.

  • Copyright © 2019 American Society for Microbiology.

All Rights Reserved.

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Iron Supply via NCOA4-Mediated Ferritin Degradation Maintains Mitochondrial Functions
Motoki Fujimaki, Norihiko Furuya, Shinji Saiki, Taku Amo, Yoko Imamichi, Nobutaka Hattori
Molecular and Cellular Biology Jun 2019, 39 (14) e00010-19; DOI: 10.1128/MCB.00010-19

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Iron Supply via NCOA4-Mediated Ferritin Degradation Maintains Mitochondrial Functions
Motoki Fujimaki, Norihiko Furuya, Shinji Saiki, Taku Amo, Yoko Imamichi, Nobutaka Hattori
Molecular and Cellular Biology Jun 2019, 39 (14) e00010-19; DOI: 10.1128/MCB.00010-19
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KEYWORDS

mitochondria
NCOA4
ferritin complex
ferritin heavy chain
ferritin light chain
iron
lysosome
mitochondrial respiration
mitochondrial respiratory chain complex

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