Ubiquitin and Receptor-Dependent Mitophagy Pathways and Their Implication in Neurodegeneration. Issue 8 (3rd April 2020)

• Record Type: Journal Article
• Authors: Fritsch, Lauren E.; Moore, M. Elyse; Sarraf, Shireen A.; Pickrell, Alicia M.
• Is Part Of: Journal of molecular biology. Volume 432:Issue 8(2020)
• Page Start: 2510
• Page End: 2524
• Publication Date: 2020-04-03
• Subjects: Mitochondria -- PINK1/Parkin -- Ubiquitin -- BNIP3L/Nix -- Autophagosome; amyotrophic lateral sclerosis ALS -- autophagy-related gene ATG -- B-cell leukemia/lymphoma BCL -- BCL2-homology 3 BH3 -- BCL2/adenovirus E1B-19 kDa–interacting protein 3 BNIP3 -- carbonyl cyanide m-chlorophenylhydrazone CCCP -- dopaminergic DA -- deferiprone DFP -- dynamin-related protein 1 DRP-1 -- mitochondrial fission protein 1 Fis1 -- deubiquitinases Dub -- frontal temporal dementia FTD -- FUN14 Domain-Containing Protein 1 FUNDC1 -- gamma-aminobutyric acid receptor–associated protein GABARAP -- glucosylceramidase beta GBA -- Huntington's disease HD -- inner mitochondrial membrane IMM -- inner membrane space IMS -- induced pluripotent stem cells iPSCs -- lysine K -- knockdown KD -- knockout KO -- microtubule-associated protein light chain 3 LC3 -- LC3-interacting region LIR -- mitochondrial-anchored protein ligase MAPL -- mitochondrial-derived vesicles MDVs -- mitochondrial DNA mtDNA -- mitochondrial targeting signal MTS -- mitochondrial ubiquitin ligase 1 Mul1 -- mitochondrial ubiquitin ligase activator of NF-κB MULAN -- Nip-like protein X NIX/BNIP3L -- outer mitochondrial membrane OMM -- oxidative phosphorylation OXPHOS -- phosphatidylinositol-3-phosphate PtdIns3P -- phosphorylated ubiquitin p-UB -- Parkinson's disease PD -- prohibitin PHB -- PTEN-induced putative kinase protein 1 PINK1 -- retinal ganglion cell RGC -- reactive oxygen species ROS -- serine S -- superoxide dismutase SOD -- small ubiquitin-like modifiers SUMOs -- Tank Binding Kinase 1 TBK1 -- transmembrane TM -- translocase of the outer membrane TOM -- ubiquitin Ub -- ubiquitin binding domain UBD -- ubiquitin-like domain UBL -- ubiquitin proteasome system UPS -- ubiquitin-specific protease USP -- vacuolar protein sorting-35 VPS35 -- zinc finger ZF -- mitochondria membrane potential Δψm; Molecular biology -- Periodicals; Biology -- Periodicals; Biochemistry -- Periodicals; Bacteriology -- Periodicals; Molecular Biology -- Periodicals; Biochemistry -- Periodicals; Biologie moléculaire -- Périodiques; Biologie -- Périodiques; Biochimie -- Périodiques; Moleculaire biologie; Biochemistry; Biology; Molecular biology; Periodicals; 572.805
• DOI: 10.1016/j.jmb.2019.10.015
• Languages: English
• ISSNs: 0022-2836

Abstract

Abstract: Selective autophagy of mitochondria, or mitophagy, refers to the specific removal and degradation of damaged or surplus mitochondria via targeting to the lysosome for destruction. Disruptions in this homeostatic process may contribute to disease. The identification of diverse mitophagic pathways and how selectivity for each of these pathways is conferred is just beginning to be understood. The removal of both damaged and healthy mitochondria under disease and physiological conditions is controlled by either ubiquitin-dependent or receptor-dependent mechanisms. In this review, we will discuss the known types of mitophagy observed in mammals, recent findings related to PINK1/Parkin-mediated mitophagy (which is the most well-studied form of mitophagy), the implications of defective mitophagy to neurodegenerative processes, and unanswered questions inspiring future research that would enhance our understanding of mitochondrial quality control. Highlights: Mitophagy pathways are either receptor or ubiquitin dependent. Mitophagy degrades damaged organelles for quality control. Mitophagy degrades healthy organelles for cellular differentiation. Defective mitophagy pathways are implicated in neurodegenerative diseases.