Mitochondria in neurodegeneration

van Putten, 2021, Dysregulation of astrocyte ion homeostasis and its relevance for stroke-induced brain damage, Int J Mol Sci, 22, 10.3390/ijms22115679 Rahman, 2020, Mitochondrial disease in children, J Intern Med, 287, 609, 10.1111/joim.13054 Davis, 1979, Chronic Parkinsonism secondary to intravenous injection of meperidine analogues, Psychiatry Res, 1, 249, 10.1016/0165-1781(79)90006-4 Langston, 1983, Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis, Science, 219, 979, 10.1126/science.6823561 Nicklas, 1985, Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine, Life Sci, 36, 2503, 10.1016/0024-3205(85)90146-8 Parker, 1989, Abnormalities of the electron transport chain in idiopathic Parkinson’s disease, Ann Neurol, 26, 719, 10.1002/ana.410260606 Moran, 2012, Mitochondrial respiratory chain dysfunction: implications in neurodegeneration, Free Radic Biol Med, 53, 595, 10.1016/j.freeradbiomed.2012.05.009 Betarbet, 2000, Chronic systemic pesticide exposure reproduces features of Parkinson’s disease, Nat Neurosci, 3, 1301, 10.1038/81834 Valente, 2004, Hereditary early-onset Parkinson’s disease caused by mutations in PINK1, Science, 304, 1158, 10.1126/science.1096284 Hatano, 2004, Novel PINK1 mutations in early-onset parkinsonism, Ann Neurol, 56, 424, 10.1002/ana.20251 Dagda, 2009, Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission, J Biol Chem, 284, 13843, 10.1074/jbc.M808515200 Kawajiri, 2010, PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy, FEBS Lett, 584, 1073, 10.1016/j.febslet.2010.02.016 Narendra, 2010, PINK1 is selectively stabilized on impaired mitochondria to activate Parkin, PLoS Biol, 8, 10.1371/journal.pbio.1000298 Narendra, 2008, Parkin is recruited selectively to impaired mitochondria and promotes their autophagy, J Cell Biol, 183, 795, 10.1083/jcb.200809125 Matsuda, 2010, PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy, J Cell Biol, 189, 211, 10.1083/jcb.200910140 Chu, 2019, Mechanisms of selective autophagy and mitophagy: implications for neurodegenerative diseases, Neurobiol Dis, 122, 23, 10.1016/j.nbd.2018.07.015 Pickrell, 2015, The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson’s disease, Neuron, 85, 257, 10.1016/j.neuron.2014.12.007 Ge, 2020, PINK1 and Parkin mitochondrial quality control: a source of regional vulnerability in Parkinson’s disease, Mol Neurodegener, 15, 20, 10.1186/s13024-020-00367-7 Schubert, 2017, Structure of PINK1 in complex with its substrate ubiquitin, Nature, 552, 51, 10.1038/nature24645 Rasool, 2018, PINK1 autophosphorylation is required for ubiquitin recognition, EMBO Rep, 19, 10.15252/embr.201744981 Gan, 2021, Activation mechanism of PINK1, Nature, 602, 328, 10.1038/s41586-021-04340-2 Rasool, 2022, Mechanism of PINK1 activation by autophosphorylation and insights into assembly on the TOM complex, Mol Cell, 82, 44, 10.1016/j.molcel.2021.11.012 Wang, 2018, PINK1 interacts with VCP/p97 and activates PKA to promote NSFL1C/p47 phosphorylation and dendritic arborization in neurons, eNeuro, 5, 10.1523/ENEURO.0466-18.2018 Wang, 2003, D1 ring is stable and nucleotide-independent, whereas D2 ring undergoes major conformational changes during the ATPase cycle of p97-VCP, J Biol Chem, 278, 32784, 10.1074/jbc.M303869200 Kim, 2013, VCP is essential for mitochondrial quality control by PINK1/Parkin and this function is impaired by VCP mutations, Neuron, 78, 65, 10.1016/j.neuron.2013.02.029 Wang, 2016, Drosophila clueless is involved in Parkin-dependent mitophagy by promoting VCP-mediated Marf degradation, Hum Mol Genet, 25, 1946, 10.1093/hmg/ddw067 Mengus, 2022, VCP/p97 cofactor UBXN1/SAKS1 regulates mitophagy by modulating MFN2 removal from mitochondria, Autophagy, 18, 171, 10.1080/15548627.2021.1922982 McLelland, 2018, Mfn2 ubiquitination by PINK1/parkin gates the p97-dependent release of ER from mitochondria to drive mitophagy, Elife, 7, 10.7554/eLife.32866 Ye, 2015, Parkin-mediated mitophagy in mutant hAPP neurons and Alzheimer’s disease patient brains, Hum Mol Genet, 24, 2938, 10.1093/hmg/ddv056 Franco-Iborra, 2021, Mutant HTT (huntingtin) impairs mitophagy in a cellular model of Huntington disease, Autophagy, 17, 672, 10.1080/15548627.2020.1728096 Evans, 2019, Autophagy and mitophagy in ALS, Neurobiol Dis, 122, 35, 10.1016/j.nbd.2018.07.005 Harding, 2021, ALS- and FTD-associated missense mutations in TBK1 differentially disrupt mitophagy, Proc Natl Acad Sci USA, 118, 10.1073/pnas.2025053118 Lee, 2017, PINK1 primes Parkin-mediated ubiquitination of PARIS in dopaminergic neuronal survival, Cell Rep, 18, 918, 10.1016/j.celrep.2016.12.090 Gehrke, 2015, PINK1 and Parkin control localized translation of respiratory chain component mRNAs on mitochondria outer membrane, Cell Metab, 21, 95, 10.1016/j.cmet.2014.12.007 Jacoupy, 2019, The PINK1 kinase-driven ubiquitin ligase Parkin promotes mitochondrial protein import through the presequence pathway in living cells, Sci Rep, 9, 10.1038/s41598-019-47352-9 Soman, 2021, Cleaved PINK1 induces neuronal plasticity through PKA-mediated BDNF functional regulation, J Neurosci Res, 99, 2134, 10.1002/jnr.24854 Murata, 2011, A new cytosolic pathway from a Parkinson disease-associated kinase, BRPK/PINK1: activation of AKT via mTORC2, J Biol Chem, 286, 7182, 10.1074/jbc.M110.179390 McWilliams, 2018, Basal mitophagy occurs independently of PINK1 in mouse tissues of high metabolic demand, Cell Metab, 27, 439, 10.1016/j.cmet.2017.12.008 Lee, 2018, Basal mitophagy is widespread in Drosophila but minimally affected by loss of Pink1 or parkin, J Cell Biol, 217, 1613, 10.1083/jcb.201801044 Kim, 2019, Assessment of mitophagy in mt-Keima Drosophila revealed an essential role of the PINK1-Parkin pathway in mitophagy induction in vivo, FASEB J, 33, 9742, 10.1096/fj.201900073R Bus, 2020, Human dopaminergic neurons lacking PINK1 exhibit disrupted dopamine metabolism related to vitamin B6 co-factors, iScience, 23, 10.1016/j.isci.2020.101797 Sterky, 2011, Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo, Proc Natl Acad Sci USA, 108, 12937, 10.1073/pnas.1103295108 Teresak, 2022, Regulation of PRKN-independent mitophagy, Autophagy, 18, 24, 10.1080/15548627.2021.1888244 Chu, 2013, Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells, Nat Cell Biol, 15, 1197, 10.1038/ncb2837 Kagan, 2016, NDPK-D (NM23-H4)-mediated externalization of cardiolipin enables elimination of depolarized mitochondria by mitophagy, Cell Death Differ, 23, 1140, 10.1038/cdd.2015.160 Koentjoro, 2017, Nix restores mitophagy and mitochondrial function to protect against PINK1/Parkin-related Parkinson’s disease, Sci Rep, 7, 10.1038/srep44373 Lin, 2017, Releasing syntaphilin removes stressed mitochondria from axons independent of mitophagy under pathophysiological conditions, Neuron, 94, 595, 10.1016/j.neuron.2017.04.004 Davis, 2014, Transcellular degradation of axonal mitochondria, Proc Natl Acad Sci USA, 111, 9633, 10.1073/pnas.1404651111 Yang, 2007, Induction of autophagy in neurite degeneration of mouse superior cervical ganglion neurons, Eur J Neurosci, 26, 2979, 10.1111/j.1460-9568.2007.05914.x Cheng, 2011, Akt suppresses retrograde degeneration of dopaminergic axons by inhibition of macroautophagy, J Neurosci, 31, 2125, 10.1523/JNEUROSCI.5519-10.2011 Zhang, 2019, CKD autophagy activation and skeletal muscle atrophy-a preliminary study of mitophagy and inflammation, Eur J Clin Nutr, 73, 950, 10.1038/s41430-018-0381-x Cherra, 2013, Mutant LRRK2 elicits calcium imbalance and depletion of dendritic mitochondria in neurons, Am J Pathol, 182, 474, 10.1016/j.ajpath.2012.10.027 Su, 2013, Inhibition of excessive mitochondrial fission reduced aberrant autophagy and neuronal damage caused by LRRK2 G2019S mutation, Hum Mol Genet, 22, 4545, 10.1093/hmg/ddt301 Cai, 2012, Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons, Curr Biol, 22, 545, 10.1016/j.cub.2012.02.005 Zhu, 2012, Impaired mitochondrial biogenesis contributes to depletion of functional mitochondria in chronic MPP(+) toxicity: dual roles for ERK1/2, Cell Death Dis, 3, 10.1038/cddis.2012.46 McLelland, 2014, Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control, EMBO J, 33, 282 Vincow, 2013, The PINK1-Parkin pathway promotes both mitophagy and selective respiratory chain turnover in vivo, Proc Natl Acad Sci USA, 110, 6400, 10.1073/pnas.1221132110 Bomba-Warczak, 2021, Long-lived mitochondrial cristae proteins in mouse heart and brain, J Cell Biol, 220, 10.1083/jcb.202005193 Krishna, 2021, Identification of long-lived proteins in the mitochondria reveals increased stability of the electron transport chain, Dev Cell, 56, 2952, 10.1016/j.devcel.2021.10.008 Plun-Favreau, 2007, The mitochondrial protease HtrA2 is regulated by Parkinson’s disease-associated kinase PINK1, Nat Cell Biol, 9, 1243, 10.1038/ncb1644 Whitworth, 2008, Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson’s disease factors Pink1 and Parkin, Dise Models Mech, 1, 168, 10.1242/dmm.000109 Meng, 2022, Serine protease HtrA2/Omi regulates adaptive mitochondrial reprogramming in the brain cortex after ischemia/reperfusion injury via UCP2-SIRT3-PGC1 axis, Human Cell, 35, 63, 10.1007/s13577-021-00610-3 Pridgeon, 2007, PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1, PLoS Biol, 5, 10.1371/journal.pbio.0050172 Cechetto, 2000, Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites, Exp Cell Res, 260, 30, 10.1006/excr.2000.4983 Zhang, 2013, TRAP1 rescues PINK1 loss-of-function phenotypes, Hum Mol Genet, 22, 2829, 10.1093/hmg/ddt132 Morais, 2014, PINK1 loss-of-function mutations affect mitochondrial complex I activity via NdufA10 ubiquinone uncoupling, Science, 344, 203, 10.1126/science.1249161 Beinlich, 2015, Shuttling of PINK1 between mitochondrial microcompartments resolved by triple-color superresolution microscopy, ACS Chem Biol, 10, 1970, 10.1021/acschembio.5b00295 Zurita Rendon, 2018, LONP1 is required for maturation of a subset of mitochondrial proteins, and its loss elicits an integrated stress response, Mol Cell Biol, 38, e00412, 10.1128/MCB.00412-17 Al-Furoukh, 2015, ClpX stimulates the mitochondrial unfolded protein response (UPRmt) in mammalian cells, Biochim Biophys Acta, 1853, 2580, 10.1016/j.bbamcr.2015.06.016 Wang, 2019, TDP-43 induces mitochondrial damage and activates the mitochondrial unfolded protein response, PLoS Genet, 15, 10.1371/journal.pgen.1007947 Zuo, 2021, TDP-43 aggregation induced by oxidative stress causes global mitochondrial imbalance in ALS, Nat Struct Mol Biol, 28, 132, 10.1038/s41594-020-00537-7 Montero, 2021, Dendritic architecture predicts in vivo firing pattern in mouse ventral tegmental area and substantia nigra dopaminergic neurons, Front Neural Circuits, 15, 10.3389/fncir.2021.769342 Hegde, 2017, Dendritic architecture of principal basolateral amygdala neurons changes congruently with endocrine response to stress, Int J Environ Res Public Health, 14, 10.3390/ijerph14070779 Luebke, 2010, Dendritic vulnerability in neurodegenerative disease: insights from analyses of cortical pyramidal neurons in transgenic mouse models, Brain Struct Funct, 214, 181, 10.1007/s00429-010-0244-2 Brown, 2021, PINK1 deficiency impairs adult neurogenesis of dopaminergic neurons, Sci Rep, 11, 6617, 10.1038/s41598-021-84278-7 Agnihotri, 2017, Loss of PINK1 leads to metabolic deficits in adult neural stem cells and impedes differentiation of newborn [neurons in the mouse hippocampus, FASEB J, 31, 2839, 10.1096/fj.201600960RR Jarazo, 2022, Parkinson’s disease phenotypes in patient neuronal cultures and brain organoids improved by 2-hydroxypropyl-beta-cyclodextrin treatment, Mov Disord, 37, 80, 10.1002/mds.28810 Liu, 2020, Chemical inhibition of FBXO7 reduces inflammation and confers neuroprotection by stabilizing the mitochondrial kinase PINK1, JCI Insight, 5, 10.1172/jci.insight.131834 Poole, 2008, The PINK1/Parkin pathway regulates mitochondrial morphology, Proc Natl Acad Sci USA, 105, 1638, 10.1073/pnas.0709336105 Wang, 2012, LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1, Hum Mol Genet, 21, 1931, 10.1093/hmg/dds003 Flippo, 2017, Mitochondrial dynamics in neuronal injury, development and plasticity, J Cell Sci, 130, 671 Chen, 2010, Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations, Cell, 141, 280, 10.1016/j.cell.2010.02.026 Kleele, 2021, Distinct fission signatures predict mitochondrial degradation or biogenesis, Nature, 593, 435, 10.1038/s41586-021-03510-6 Fukumitsu, 2016, Mitochondrial fission protein Drp1 regulates mitochondrial transport and dendritic arborization in cerebellar Purkinje cells, Mol Cell Neurosci, 71, 56, 10.1016/j.mcn.2015.12.006 Li, 2004, The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses, Cell, 119, 873, 10.1016/j.cell.2004.11.003 Rangaraju, 2019, Spatially stable mitochondrial compartments fuel local translation during plasticity, Cell, 176, 73, 10.1016/j.cell.2018.12.013 Olesen, 2020, Premature synaptic mitochondrial dysfunction in the hippocampus during aging contributes to memory loss, Redox Biol, 34, 10.1016/j.redox.2020.101558 Lopes, 2017, Tau deletion prevents stress-induced dendritic atrophy in prefrontal cortex: role of synaptic mitochondria, Cereb Cortex, 27, 2580 Liu, 2012, Parkinson’s disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria, PLoS Genet, 8, 10.1371/journal.pgen.1002537 Dagda, 2014, Beyond the mitochondrion: cytosolic PINK1 remodels dendrites through protein kinase A, J Neurochem, 128, 864, 10.1111/jnc.12494 Das Banerjee, 2017, PINK1 regulates mitochondrial trafficking in dendrites of cortical neurons through mitochondrial PKA, J Neurochem, 142, 545, 10.1111/jnc.14083 Gonzalez, 2020, Drosophila VCP/p97 mediates dynein-dependent retrograde mitochondrial motility in axons, Front Cell Dev Biol, 8, 256, 10.3389/fcell.2020.00256 Zala, 2013, Vesicular glycolysis provides on-board energy for fast axonal transport, Cell, 152, 479, 10.1016/j.cell.2012.12.029 Orr, 2008, N-terminal mutant huntingtin associates with mitochondria and impairs mitochondrial trafficking, J Neurosci, 28, 2783, 10.1523/JNEUROSCI.0106-08.2008 Kuzniewska, 2020, Mitochondrial protein biogenesis in the synapse is supported by local translation, EMBO Rep, 21, 10.15252/embr.201948882 Alami, 2014, Axonal transport of TDP-43 mRNA granules is impaired by ALS-causing mutations, Neuron, 81, 536, 10.1016/j.neuron.2013.12.018 Volgyi, 2015, Synaptic mitochondria: a brain mitochondria cluster with a specific proteome, J Proteom, 120, 142, 10.1016/j.jprot.2015.03.005 Hasel, 2015, Selective dendritic susceptibility to bioenergetic, excitotoxic and redox perturbations in cortical neurons, Biochim Biophys Acta, 1853, 2066, 10.1016/j.bbamcr.2014.12.021 Baranov, 2019, Mitochondria modulate programmed neuritic retraction, Proc Natl Acad Sci USA, 116, 650, 10.1073/pnas.1811021116 Brown, 2006, Synaptic mitochondria are more susceptible to Ca2+overload than nonsynaptic mitochondria, J Biol Chem, 281, 11658, 10.1074/jbc.M510303200 Sanganahalli, 2013, Mitochondrial calcium uptake capacity modulates neocortical excitability, J Cereb Blood Flow Metab, 33, 1115, 10.1038/jcbfm.2013.61 Ashrafi, 2020, Molecular tuning of the axonal mitochondrial Ca(2+) uniporter ensures metabolic flexibility of neurotransmission, Neuron, 105, 678, 10.1016/j.neuron.2019.11.020 De Marchi, 2014, NCLX protein, but not LETM1, mediates mitochondrial Ca2+ extrusion, thereby limiting Ca2+-induced NAD(P)H production and modulating matrix redox state, J Biol Chem, 289, 20377, 10.1074/jbc.M113.540898 Rangaraju, 2014, Activity-driven local ATP synthesis is required for synaptic function, Cell, 156, 825, 10.1016/j.cell.2013.12.042 Gandhi, 2009, PINK1-associated Parkinson’s disease is caused by neuronal vulnerability to calcium-induced cell death, Mol Cell, 33, 627, 10.1016/j.molcel.2009.02.013 Kostic, 2015, PKA phosphorylation of NCLX reverses mitochondrial calcium overload and depolarization, promoting survival of PINK1-deficient dopaminergic neurons, Cell Rep, 13, 376, 10.1016/j.celrep.2015.08.079 Huang, 2017, PINK1-mediated phosphorylation of LETM1 regulates mitochondrial calcium transport and protects neurons against mitochondrial stress, Nat Commun, 8, 1399, 10.1038/s41467-017-01435-1 Jadiya, 2019, Impaired mitochondrial calcium efflux contributes to disease progression in models of Alzheimer's disease, Nat Commun, 10, 3885, 10.1038/s41467-019-11813-6 Britti, 2020, Tau inhibits mitochondrial calcium efflux and makes neurons vulnerable to calcium-induced cell death, Cell Calcium, 86, 10.1016/j.ceca.2019.102150 Verma, 2017, Mitochondrial calcium dysregulation contributes to dendrite degeneration mediated by PD/LBD-associated LRRK2 mutants, J Neurosci, 37, 11151, 10.1523/JNEUROSCI.3791-16.2017 Plowey, 2014, Mutant LRRK2 enhances glutamatergic synapse activity and evokes excitotoxic dendrite degeneration, Biochim Biophys Acta, 1842, 1596, 10.1016/j.bbadis.2014.05.016 Soman, 2019, Restriction of mitochondrial calcium overload by mcu inactivation renders a neuroprotective effect in zebrafish models of Parkinson’s disease, Biol Open, 8, bio044347, 10.1242/bio.044347 Xie, 2017, Inhibition of the mitochondrial calcium uniporter inhibits Abeta-induced apoptosis by reducing reactive oxygen species-mediated endoplasmic reticulum stress in cultured microglia, Brain Res, 1676, 100, 10.1016/j.brainres.2017.08.035 Calvo-Rodriguez, 2020, Increased mitochondrial calcium levels associated with neuronal death in a mouse model of Alzheimer’s disease, Nat Commun, 11, 2146, 10.1038/s41467-020-16074-2 Granatiero, 2019, Overexpression of mitochondrial calcium uniporter causes neuronal death, Oxidative Med Cell longev, 2019, 10.1155/2019/1681254 Du, 2017, PINK1 signalling rescues amyloid pathology and mitochondrial dysfunction in Alzheimer’s disease, Brain, 140, 3233, 10.1093/brain/awx258 Hertz, 2013, A neo-substrate that amplifies catalytic activity of Parkinson’s-disease-related kinase PINK1, Cell, 154, 737, 10.1016/j.cell.2013.07.030 Orr, 2017, Long-term oral kinetin does not protect against alpha-synuclein-induced neurodegeneration in rodent models of Parkinson's disease, Neurochem Int, 109, 106, 10.1016/j.neuint.2017.04.006 Osgerby, 2017, Kinetin riboside and its ProTides activate the Parkinson’s disease associated PTEN-induced putative kinase 1 (PINK1) independent of mitochondrial depolarization, J Med Chem, 60, 3518, 10.1021/acs.jmedchem.6b01897 Guardia-Laguarta, 2019, PINK 1 content in mitochondria is regulated by ER-associated degradation, J Neurosci, 39, 7074, 10.1523/JNEUROSCI.1691-18.2019 Deng, 2013, F-box only protein 7 gene in parkinsonian-pyramidal disease, JAMA Neurol, 70, 20, 10.1001/jamaneurol.2013.572 Sun, 2018, Lack of PINK1 alters glia innate immune responses and enhances inflammation-induced, nitric oxide-mediated neuron death, Sci Rep, 8, 383, 10.1038/s41598-017-18786-w Sliter, 2018, Parkin and PINK1 mitigate STING-induced inflammation, Nature, 561, 258, 10.1038/s41586-018-0448-9 Lee, 2012, PINK1 stimulates interleukin-1beta-mediated inflammatory signaling via the positive regulation of TRAF6 and TAK1, Cell Mol Life Sci, 69, 3301, 10.1007/s00018-012-1004-7 Bueno, 2019, PINK1 attenuates mtDNA release in alveolar epithelial cells and TLR9 mediated profibrotic responses, PLoS One, 14, 10.1371/journal.pone.0218003 Weihofen, 2008, Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1, Hum Mol Genet, 17, 602, 10.1093/hmg/ddm334 Wang, 2014, BAG5 protects against mitochondrial oxidative damage through regulating PINK1 degradation, PLoS One, 9 Qu, 2015, BAG2 gene-mediated regulation of PINK1 protein is critical for mitochondrial translocation of PARKIN and neuronal survival, J Biol Chem, 290, 30441, 10.1074/jbc.M115.677815 Verma, 2020, Chronic treatment with the complex I inhibitor MPP(+) depletes endogenous PTEN-induced kinase 1 (PINK1) via up-regulation of Bcl-2-associated athanogene 6 (BAG6), J Biol Chem, 295, 7865, 10.1074/jbc.RA119.010474 Wang, 2011, Valosin-containing protein and neurofibromin interact to regulate dendritic spine density, J Clin Investig, 121, 4820, 10.1172/JCI45677 Marcassa, 2018, Dual role of USP30 in controlling basal pexophagy and mitophagy, EMBO Rep, 19, 10.15252/embr.201745595 Luo, 2021, Pharmacological inhibition of USP30 activates tissue-specific mitophagy, Acta Physiol, 232, 10.1111/apha.13666 Rossi, 2020, Defective mitochondrial pyruvate flux affects cell bioenergetics in Alzheimer’s disease-related models, Cell Rep, 30, 2332, 10.1016/j.celrep.2020.01.060