title: Selective removal of mitochondria via mitophagy: distinct pathways for different mitochondrial stresses.
abstract: The efficient and selective elimination of damaged or excessive mitochondria in response to bioenergetic and environmental cues is critical for maintaining a healthy and appropriate population of mitochondria. Mitophagy is considered to be the central mechanism of mitochondrial quality and quantity control. Atg32, a mitophagy receptor in yeast, recruits mitochondria targeted for degradation into the isolation membrane via both direct and indirect interactions with Atg8. In mammals, different mitophagy effectors, including the mitophagy receptors NIX, BNIP3 and FUDNC1 and the PINK1/Parkin pathway, have been identified to participate in the selective clearance of mitochondria. One common feature of mitophagy receptors is that they harbor an LC3-interacting region (LIR) that interacts with LC3, thus promoting the sequestration of mitochondria into the isolation membrane. Additionally, both receptor- and Parkin/PINK1-mediated mitophagy have been found to be regulated by reversible phosphorylation. Here, we review the recent progress in the understanding of the molecular mechanisms involved in selective mitophagy at multiple levels. We also discuss different mitophagy receptors from an evolutionary perspective and highlight the specific functions of and possible cooperation between distinct mechanisms of mitophagy.
authors.affiliation: State Key Laboratory of Biomembrane and Membrane Biotechnology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China.
authors.forename: Huifang
authors.initials: H
authors.lastname: Wei
authors.affiliation: State Key Laboratory of Biomembrane and Membrane Biotechnology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China.
authors.forename: Lei
authors.initials: L
authors.lastname: Liu
authors.affiliation: State Key Laboratory of Biomembrane and Membrane Biotechnology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China; University of Chinese Academy of Sciences, Beijing 100049, China; Tianjin Key Laboratory of Protein Science, College of Life Sciences, Nankai University, Tianjin 300071, China. Electronic address: chenq@ioz.ac.cn.
authors.forename: Quan
authors.initials: Q
authors.lastname: Chen
mesh_terms: D008928:Mitochondria / Q000235:genetics / Q000378:metabolism*; D024101:Mitochondrial Proteins / Q000235:genetics / Q000378:metabolism*; D063306:Mitophagy / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D013312:Stress, Physiological / Q000502:physiology*
chemical_list: D024101:Mitochondrial Proteins; D029701:Saccharomyces cerevisiae Proteins
keywords: Atg32; FUNDC1; Mitophagy; Mitophagy receptor; Parkin