Cited by 421Autophagy in Disease and TherapyUbiquitin and proteasome pathwaysMitochondrial Function and Pathology

Receptor-mediated mitophagy in yeast and mammalian systems

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Liu, Lei, Sakakibara, Kaori, Chen, Quan, Okamoto, Koji·2014·Cell Research

Abstract

Mitophagy, or mitochondria autophagy, plays a critical role in selective removal of damaged or unwanted mitochondria. Several protein receptors, including Atg32 in yeast, NIX/BNIP3L, BNIP3 and FUNDC1 in mammalian systems, directly act in mitophagy. Atg32 interacts with Atg8 and Atg11 on the surface of mitochondria, promoting core Atg protein assembly for mitophagy. NIX/BNIP3L, BNIP3 and FUNDC1 also have a classic motif to directly bind LC3 (Atg8 homolog in mammals) for activation of mitophagy. Recent studies have shown that receptor-mediated mitophagy is regulated by reversible protein phosphorylation. Casein kinase 2 (CK2) phosphorylates Atg32 and activates mitophagy in yeast. In contrast, in mammalian cells Src kinase and CK2 phosphorylate FUNDC1 to prevent mitophagy. Notably, in response to hypoxia and FCCP treatment, the mitochondrial phosphatase PGAM5 dephosphorylates FUNDC1 to activate mitophagy. Here, we mainly focus on recent advances in our understanding of the molecular mechanisms underlying the activation of receptor-mediated mitophagy and the implications of this catabolic process in health and disease.

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Crossref · 10.1038/cr.2014.75

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  • Decreased mitophagy is associated with aging across multiple species.

    “Decreased mitophagy will result in longer-lived and more damage-prone mitochondria, and decreased mitophagy is associated with aging across multiple species (Gelino and Hansen, 2012; Liu et al., 2014; Richard et al., 2013).”

    From Programmed cell death in aging (2015) · cites this paper as Liu et al., 2014

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Authors
Liu, L., Sakakibara, K., Chen, Q., & Okamoto, K.
Affiliations
  • Chinese Academy of Sciences (CN)
  • The University of Osaka (JP)
Corresponding author
  • Chen, Quan
  • Okamoto, Koji
Venue
Cell Research
Published
2014-06-06
Volume
24
Issue
7
Pages
787-795
ISSN
  • 1001-0602 (ISSN-L)
  • 1748-7838
OpenAlex
W2049172731
Cited by
421
References
88
Citations by year
2026: 25 · 2025: 34 · 2024: 42 · 2023: 49 · 2022: 51 · 2021: 58 · 2020: 30 · 2019: 31 · 2018: 25 · 2017: 19 · 2016: 27 · 2015: 28 · 2014: 2
FWCI
3.38
Type
journal article
Language
en
Open access
Locations
  • Cell Research (publishedVersion, cc-by-nc-sa)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
Japan Society for the Promotion of Science (25291045, 26840067, 25650067)
Topics
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Keywords
mitophagy, Atg32, BNIP3, FUNDC1, LC3, ATG8, Atg11, casein kinase 2, Src kinase, PGAM5, protein phosphorylation, hypoxia, FCCP, yeast, mammalian cells, mitochondrial quality control
MeSH terms
Autophagy-Related Proteins, Autophagy-Related Protein 8 Family, Animals, Humans, Membrane Proteins, Microtubule-Associated Proteins, Mitochondria, Phosphorylation, Proto-Oncogene Proteins, Saccharomyces cerevisiae, Cell Hypoxia, Apoptosis, Receptors, Cytoplasmic and Nuclear, src-Family Kinases, Mitochondrial Proteins, Tumor Suppressor Proteins, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, Casein Kinase II, Mitochondrial Dynamics, Mitophagy

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