References
- Cheng HC, Ulane CM, Burke RE. Clinical progression in Parkinson disease and the neurobiology of axons. Ann Neurol. 2010;67:715–725.
- Fearnley JM, Lees AJ. Ageing and Parkinson’s disease: substantia nigra regional selectivity. Brain. 1991;114(Pt 5):2283–2301.
- Ross GW, Petrovitch H, Abbott RD, et al. Parkinsonian signs and substantia nigra neuron density in decendents elders without PD. Ann Neurol. 2004;56:532–539.
- Whone AL, Watts RL, Stoessl AJ, et al. Slower progression of Parkinson’s disease with ropinirole versus levodopa: the REAL-PET study. Ann Neurol. 2003;54:93–101.
- Dos Santos V, Thomann PA, Wustenberg T, et al. Morphological cerebral correlates of CERAD test performance in mild cognitive impairment and Alzheimer’s disease. J Alzheimers Dis. 2011;23:411–420.
- Marsili L, Rizzo G, Colosimo C. Diagnostic criteria for Parkinson’s disease: from James Parkinson to the concept of prodromal disease. Front Neurol. 2018;9:156.
- Postuma RB, Berg D, Stern M, et al. MDS clinical diagnostic criteria for Parkinson’s disease. Mov Disord. 2015;30:1591–1601.
- Zhao H, Wang C, Zhao N, et al. Potential biomarkers of Parkinson’s disease revealed by plasma metabolic profiling. J Chromatogr B Analyt Technol Biomed Life Sci. 2018;1081-1082:101–108.
- Kish SJ, Bergeron C, Rajput A, et al. Brain cytochrome oxidase in Alzheimer’s disease. J Neurochem. 1992;59:776–779.
- Nixon RA, Wegiel J, Kumar A, et al. Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study. J Neuropathol Exp Neurol. 2005;64:113–122.
- Schapira AH, Cooper JM, Dexter D, et al. Mitochondrial complex I deficiency in Parkinson’s disease. J Neurochem. 1990;54:823–827.
- Kitada T, Asakawa S, Hattori N, et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature. 1998;392:605–608.
- Valente EM, Abou-Sleiman PM, Caputo V, et al. Hereditary early-onset Parkinson’s disease caused by mutations in PINK1. Science. 2004;304:1158–1160.
- Geisler S, Holmstrom KM, Skujat D, et al. PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat Cell Biol. 2010;12:119–131.
- Geisler S, Holmstrom KM, Treis A, et al. The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations. Autophagy. 2010;6:871–878.
- Greene JC, Whitworth AJ, Kuo I, et al. Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants. Proc Natl Acad Sci U S A. 2003;100:4078–4083.
- Matsuda N, Sato S, Shiba K, et al. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J Cell Biol. 2010;189:211–221.
- Narendra D, Tanaka A, Suen DF, et al. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol. 2008;183:795–803.
- Narendra DP, Jin SM, Tanaka A, et al. PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol. 2010;8:e1000298.
- Truban D, Hou X, Caulfield TR, et al. PINK1, Parkin, and Mitochondrial quality control: what can we learn about Parkinson’s disease pathobiology? J Parkinsons Dis. 2017;7:13–29.
- Vives-Bauza C, Zhou C, Huang Y, et al. PINK1-dependent recruitment of Parkin to mitochondria in mitophagy. Proc Natl Acad Sci U S A. 2010;107:378–383.
- Ziviani E, Tao RN, Whitworth AJ. Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc Natl Acad Sci U S A. 2010;107:5018–5023.
- Matheoud D, Cannon T, Voisin A, et al. Intestinal infection triggers Parkinson’s disease-like symptoms in Pink1(-/-) mice. Nature. 2019;571:565–569.
- Matheoud D, Sugiura A, Bellemare-Pelletier A, et al. Parkinson’s disease-related proteins PINK1 and Parkin repress mitochondrial antigen presentation. Cell. 2016;166:314–327.
- Kane LA, Lazarou M, Fogel AI, et al. PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity. J Cell Biol. 2014;205:143–153.
- Kazlauskaite A, Kondapalli C, Gourlay R, et al. Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65. Biochem J. 2014;460:127–139.
- Koyano F, Okatsu K, Kosako H, et al. Ubiquitin is phosphorylated by PINK1 to activate parkin. Nature. 2014;510:162–166.
- Iguchi M, Kujuro Y, Okatsu K, et al. Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-dependent phosphorylation. J Biol Chem. 2013;288:22019–22032.
- Kondapalli C, Kazlauskaite A, Zhang N, et al. PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65. Open Biol. 2012;2:120080.
- Shiba-Fukushima K, Imai Y, Yoshida S, et al. PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy. Sci Rep. 2012;2:1002.
- Okatsu K, Koyano F, Kimura M, et al. Phosphorylated ubiquitin chain is the genuine Parkin receptor. J Cell Biol. 2015;209:111–128.
- Ordureau A, Sarraf SA, Duda DM, et al. Quantitative proteomics reveal a feedforward mechanism for mitochondrial PARKIN translocation and ubiquitin chain synthesis. Mol Cell. 2014;56:360–375.
- Shiba-Fukushima K, Arano T, Matsumoto G, et al. Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tethering. PLoS Genet. 2014;10:e1004861.
- Fiesel FC, Ando M, Hudec R, et al. (Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylation. EMBO Rep. 2015;16:1114–1130.
- Fiesel FC, Springer W. Disease relevance of phosphorylated ubiquitin (p-S65-Ub). Autophagy. 2015;11:2125–2126.
- Hou X, Fiesel FC, Truban D, et al. Age- and disease-dependent increase of the mitophagy marker phospho-ubiquitin in normal aging and Lewy body disease. Autophagy. 2018;14:1404–1418.
- McWilliams TG, Prescott AR, Montava-Garriga L, et al. Basal mitophagy occurs independently of PINK1 in mouse tissues of high metabolic demand. Cell Metab. 2018;27:439–49 e5.
- Harper JW, Ordureau A, Heo JM. Building and decoding ubiquitin chains for mitophagy. Nat Rev Mol Cell Biol. 2018;19:93–108.
- Shiba-Fukushima K, Ishikawa KI, Inoshita T, et al. Evidence that phosphorylated ubiquitin signaling is involved in the etiology of Parkinson’s disease. Hum Mol Genet. 2017;26:3172–3185.
- Tholen DW, Kristian Linnet MD, Kondratovich M, et al. Protocols for determination of limits of detection and limits of quantitation; approved guideline (EP17-A). 940 West Valley Road, Suite 1400, Wayne, Pennsylvania 19087-1898, USA: NCCLS; 2004.
- Armbruster DA, Pry T. Limit of blank, limit of detection and limit of quantitation. Clin Biochem Rev. 2008;29(Suppl 1):S49–52.
- Siuda J, Jasinska-Myga B, Boczarska-Jedynak M, et al. Early-onset Parkinson’s disease due to PINK1 p.Q456X mutation–clinical and functional study. Parkinsonism Relat Disord. 2014;20:1274–1278.
- Puschmann A, Fiesel FC, Caulfield TR, et al. Heterozygous PINK1 p.G411S increases risk of Parkinson’s disease via a dominant-negative mechanism. Brain. 2017;140:98–117.
- Liu G, Locascio JJ, Corvol JC, et al. Prediction of cognition in Parkinson’s disease with a clinical-genetic score: a longitudinal analysis of nine cohorts. Lancet Neurol. 2017;16:620–629.
- Gladkova C, Schubert AF, Wagstaff JL, et al. An invisible ubiquitin conformation is required for efficient phosphorylation by PINK1. Embo J. 2017;36:3555–3572.
- Akundi RS, Huang Z, Eason J, et al. Increased mitochondrial calcium sensitivity and abnormal expression of innate immunity genes precede dopaminergic defects in Pink1-deficient mice. PLoS One. 2011;6:e16038.
- Gispert S, Ricciardi F, Kurz A, et al. Parkinson phenotype in aged PINK1-deficient mice is accompanied by progressive mitochondrial dysfunction in absence of neurodegeneration. PLoS One. 2009;4:e5777.
- Goldberg MS, Fleming SM, Palacino JJ, et al. Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons. J Biol Chem. 2003;278:43628–43635.
- Kitada T, Pisani A, Porter DR, et al. Impaired dopamine release and synaptic plasticity in the striatum of PINK1-deficient mice. Proc Natl Acad Sci U S A. 2007;104:11441–11446.
- Noda S, Sato S, Fukuda T, et al. Loss of Parkin contributes to mitochondrial turnover and dopaminergic neuronal loss in aged mice. Neurobiol Dis. 2020;136:104717.
- Pickrell AM, Huang CH, Kennedy SR, et al. Endogenous Parkin preserves dopaminergic substantia nigral neurons following mitochondrial DNA mutagenic stress. Neuron. 2015;87:371–381.
- Sliter DA, Martinez J, Hao L, et al. Parkin and PINK1 mitigate STING-induced inflammation. Nature. 2018;561:258–262.
- Hou X, Watzlawik JO, Cook C, et al. Mitophagy alterations in Alzheimer’s disease are associated with granulovacuolar degeneration and early tau pathology. Alzheimer’s Dementia. 2020. (in press). DOI:https://doi.org/10.1002/alz.12198.
- Ando M, Fiesel FC, Hudec R, et al. The PINK1 p.I368N mutation affects protein stability and ubiquitin kinase activity. Mol Neurodegener. 2017;12:32.
- Cao Y, Li C, Zhang Q, et al. Extracellular ubiquitin enhances the suppressive effects of regulatory T cells on effector T cell responses. Clin Lab. 2014;60:1983–1991.
- Majetschak M, Krehmeier U, Bardenheuer M, et al. Extracellular ubiquitin inhibits the TNF-alpha response to endotoxin in peripheral blood mononuclear cells and regulates endotoxin hyporesponsiveness in critical illness. Blood. 2003;101:1882–1890.
- Saini V, Marchese A, Tang WJ, et al. Structural determinants of ubiquitin-CXC chemokine receptor 4 interaction. J Biol Chem. 2011;286:44145–44152.
- Wong YM, LaPorte HM, Albee LJ, et al. Ubiquitin Urine Levels in Burn Patients. J Burn Care Res. 2017;38:e133–e43.
- Gersch M, Gladkova C, Schubert AF, et al. Mechanism and regulation of the Lys6-selective deubiquitinase USP30. Nat Struct Mol Biol. 2017;24:920–930.
- Swatek KN, Usher JL, Kueck AF, et al. Insights into ubiquitin chain architecture using Ub-clipping. Nature. 2019;572:533–537.
- Wauer T, Swatek KN, Wagstaff JL, et al. Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis. Embo J. 2015;34:307–325.
- Cong L, Ran FA, Cox D, et al. Multiplex genome engineering using CRISPR/Cas systems. Science. 2013;339(6121):819–823. .
- Fiesel FC, Moussaud-Lamodiere EL, Ando M, et al. A specific subset of E2 ubiquitin-conjugating enzymes regulate Parkin activation and mitophagy differently. J Cell Sci. 2014;127:3488–3504.