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LRRK2-Related Parkinson’s Disease Due to Altered Endolysosomal Biology With Variable Lewy Body Pathology: A Hypothesis
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LRRK2 plays a role in the endolysosomal system.
“Multiple lines of evidence indicate that LRRK2 plays a role in the endolysosomal system [20]”
From Distinct Roles for RAB10 and RAB29 in Pathogenic LRRK2-Mediated Endolysosomal Trafficking Alterations (2020) · cites this paper as [20]
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International Parkinson's Disease Genomics Consortium (IPDGC), Nalls, M. A., Parkinson's Study Group (PSG) Parkinson's Research: The Organized GENetics Initiative (PROGENI), 23andMe, GenePD, NeuroGenetics Research Consortium (NGRC), Hussman Institute of Human Genomics (HIHG), Investigator, T. A. J. D., (CHARGE), C. F. H. A. A. R. I. G. E., North American Brain Expression Consortium (NABEC), et al. (2014) · Nature Genetics · doi:10.1038/ng.3043 · Cited by 1,895
Li, J.-Y., Englund, E., Holton, J. L., Soulet, D., Hagell, P., Lees, A. J., Lashley, T., Quinn, N. P., Rehncrona, S., Björklund, A., et al. (2008) · Nature Medicine · doi:10.1038/nm1746 · Cited by 1,845
Lewy body–like pathology in long-term embryonic nigral transplants in Parkinson's disease
Kordower, J. H., Chu, Y., Hauser, R. A., Freeman, T. B., & Olanow, C. W. (2008) · Nature Medicine · doi:10.1038/nm1747 · Cited by 1,722
Termination of autophagy and reformation of lysosomes regulated by mTOR
Yu, L., McPhee, C. K., Zheng, L., Mardones, G. A., Rong, Y., Peng, J., Mi, N., Zhao, Y., Liu, Z., Wan, F., et al. (2010) · Nature · doi:10.1038/nature09076 · Cited by 1,544
α-Synuclein Is Degraded by Both Autophagy and the Proteasome
Webb, J. L., Ravikumar, B., Atkins, J., Skepper, J. N., & Rubinsztein, D. C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300227200 · Cited by 1,429
Zhang, W., Wang, T., Pei, Z., Miller, D. S., Wu, X., Block, M. L., Wilson, B., Zhang, W., Zhou, Y., Hong, J.-S., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-2751com · Cited by 1,265
Vogiatzi, T., Xilouri, M., Vekrellis, K., & Stefanis, L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801992200 · Cited by 683
Rab Proteins and the Compartmentalization of the Endosomal System
Wandinger-Ness, A., & Zerial, M. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a022616 · Cited by 586
Vanlandingham, P. A., & Ceresa, B. P. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809277200 · Cited by 441
Chaperone-mediated autophagy: selectivity pays off
Cuervo, A. M. (2010) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2009.10.003 · Cited by 260 · cited 1×
“CMA is the process by which substrate proteins are selectively targeted to lysosomes and translocated into their lumen through a coordinated action of chaperones and LAMP2A, which translocates substrates directly into the lysosomal lumen (Cuervo, 2010; Cuervo and Wong, 2013).”
BackgroundHenry, A. G., Aghamohammadzadeh, S., Samaroo, H., Chen, Y., Mou, K., Needle, E., & Hirst, W. D. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv314 · Cited by 235
TBC proteins: GAPs for mammalian small GTPase Rab?
Fukuda, M. (2011) · Bioscience Reports · doi:10.1042/bsr20100112 · Cited by 207
Bonello, F., Hassoun, S.-M., Mouton-Liger, F., Shin, Y. S., Muscat, A., Tesson, C., Lesage, S., Beart, P. M., Brice, A., Krupp, J., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz004 · Cited by 163
Yu, W. H., Dorado, B., Figueroa, H. Y., Wang, L., Planel, E., Cookson, M. R., Clark, L. N., & Duff, K. E. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.080928 · Cited by 155 · cited 1×
“Whilst a role for macroautophagy in the clearance of α-synuclein oligomers is supported by various studies (Webb et al., 2003; Spencer et al., 2009; Yu et al., 2009), others have questioned its relevance.”
ResultAhmed, I., Liang, Y., Schools, S., Dawson, V. L., Dawson, T. M., & Savitt, J. M. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0209-12.2012 · Cited by 144
Verma, M., Callio, J., Otero, P. A., Sekler, I., Wills, Z. P., & Chu, C. T. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.3791-16.2017 · Cited by 128
Flagged first, then by citations
Research works printed but not linked: 172
- Agin-Liebes, 2019, Movement disorders rounds: a case of missing pathology in a patient with LRRK2 Parkinson’s disease., Parkinsonism Relat. Disord., 10.1016/j.parkreldis.2019.11.006 · DOI
- Akgoc, 2015, Bis(monoacylglycero)phosphate: a secondary storage lipid in the gangliosidoses., J. Lipid Res., 56, 1006, 10.1194/jlr.M057851 · DOI
- Alcalay, 2020, Higher urine bis(Monoacylglycerol)phosphate levels in LRRK2 G2019S mutation carriers: implications for therapeutic development., Mov. Disord., 35, 134, 10.1002/mds.27818 · DOI
- Alegre-Abarrategui, 2009, LRRK2 regulates autophagic activity and localizes to specific membrane microdomains in a novel human genomic reporter cellular model., Hum. Mol. Genet., 18, 4022, 10.1093/hmg/ddp346 · DOI
- Anand, 2009, Investigation of leucine-rich repeat kinase 2., FEBS J., 276, 466, 10.1111/j.1742-4658.2008.06789.x · DOI
- Anderson, 2006, Phosphorylation of ser-129 is the dominant pathological modification of α-synuclein in familial and sporadic Lewy body disease., J. Biol. Chem., 281, 29739, 10.1074/jbc.M600933200 · DOI
- Beilina, 2014, Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease., Proc. Natl. Acad. Sci. U.S.A., 111, 2626, 10.1073/pnas.1318306111 · DOI · Paper page
- Berg, 2014, Time to redefine PD? Introductory statement of the MDS task force on the definition of Parkinson’s disease., Mov. Disord., 29, 454, 10.1002/mds.25844 · DOI
- Billingsley, 2018, Genetic risk factors in Parkinson’s disease., Cell Tissue Res., 373, 9, 10.1007/s00441-018-2817-y · DOI
- Boassa, 2013, Mapping the subcellular distribution of α-synuclein in neurons using genetically encoded probes for correlated light and electron microscopy: implications for Parkinson’s disease pathogenesis., J. Neurosci., 33, 2605, 10.1523/JNEUROSCI.2898-12.2013 · DOI
- Bonet-Ponce, 2020, LRRK2 mediates tubulation and vesicle sorting from membrane damaged lysosomes., bioRxiv, 10.1101/2020.01.23.917252 · DOI
- Book, 2018, A meta-analysis of α-synuclein multiplication in familial parkinsonism., Front. Neurol., 9, 10.3389/fneur.2018.01021 · DOI
- Braak, 2003, Staging of brain pathology related to sporadic Parkinson’s disease., Neurobiol. Aging, 24, 197, 10.1016/S0197-4580(02)00065-9 · DOI · Paper page
- Braun, 2015, The Rho-specific GAP protein DLC3 coordinates endocytic membrane trafficking., J. Cell Sci., 128, 1386, 10.1242/jcs.163857 · DOI · Paper page
- Bravo-San Pedro, 2013, The LRRK2 G2019S mutant exacerbates basal autophagy through activation of the MEK/ERK pathway., Cell. Mol. Life Sci., 70, 121, 10.1007/s00018-012-1061-y · DOI
- Brice, 2005, Genetics of Parkinson’s disease: LRRK2 on the rise., Brain, 128, 2760, 10.1093/brain/awh676 · DOI
- Bridi, 2018, Mechanisms of α-Synuclein Induced Synaptopathy in Parkinson’s disease., Front. Neurosci., 12, 10.3389/fnins.2018.00080 · DOI
- Bucci, 2012, Molecular basis of charcot-marie-tooth type 2B disease., Biochem. Soc. Trans, 40, 1368, 10.1042/BST20120197 · DOI
- Bucci, 2000, Rab7: a key to lysosome biogenesis., Mol. Biol. Cell, 11, 467, 10.1091/mbc.11.2.467 · DOI
- Burré, 2010, Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro., Science, 329, 1663, 10.1126/science.1195227 · DOI
- Burton, 1994, Specific interactions of Mss4 with members of the Rab GTPase subfamily., EMBO J., 13, 5547, 10.1002/j.1460-2075.1994.tb06892.x · DOI
- Caballero, 2018, Interplay of pathogenic forms of human tau with different autophagic pathways., Aging Cell, 17, 10.1111/acel.12692 · DOI · Paper page
- Ceresa, 2006, Rab7 activity affects epidermal growth factor:epidermal growth factor receptor degradation by regulating endocytic trafficking from the late endosome., J. Biol. Chem., 281, 1099, 10.1074/jbc.M504175200 · DOI
- 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 · DOI
- Cherry, 2013, Charcot-Marie-Tooth 2B mutations in rab7 cause dosage-dependent neurodegeneration due to partial loss of function., eLife, 2, 10.7554/eLife.01064 · DOI
- Choudhury, 2002, Rab proteins mediate Golgi transport of caveola-internalized glycosphingolipids and correct lipid trafficking in Niemann-Pick C cells., J. Clin. Invest., 109, 1541, 10.1172/JCI0215420 · DOI
- Choudhury, 2004, Elevated endosomal cholesterol levels in Niemann-Pick cells inhibit rab4 and perturb membrane recycling., Mol. Biol. Cell, 15, 4500, 10.1091/mbc.e04-05-0432 · DOI
- Christensen, 2018, LRRK2 exonic variants associated with Parkinson’s disease augment phosphorylation levels for LRRK2-Ser1292 and Rab10-Thr73., bioRxiv, 10.1101/447946 · DOI
- Cogo, 2020, Leucine-rich repeat kinase 2 and lysosomal dyshomeostasis in Parkinson disease., J. Neurochem., 152, 273, 10.1111/jnc.14908 · DOI
- Cole, 2002, Lipid droplet binding and oligomerization properties of the Parkinson’s disease protein α-synuclein., J. Biol. Chem., 277, 6344, 10.1074/jbc.M108414200 · DOI · Paper page
- Conway, 2000, Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson’s disease: implications for pathogenesis and therapy., Proc. Natl. Acad. Sci. U.S.A., 97, 571, 10.1073/pnas.97.2.571 · DOI
- Covy, 2009, Identification of compounds that inhibit the kinase activity of leucine-rich repeat kinase 2., Biochem. Biophys. Res. Commun., 378, 473, 10.1016/j.bbrc.2008.11.048 · DOI
- Cuervo, 2004, Impaired degradation of mutant α-synuclein by chaperone-mediated autophagy., Science, 305, 1292, 10.1126/science.1101738 · DOI · Paper page
- Cuervo, 2013, Chaperone-mediated autophagy: roles in disease and aging., Cell Res., 24, 92, 10.1038/cr.2013.153 · DOI
- Danzer, 2012, Exosomal cell-to-cell transmission of alpha synuclein oligomers., Mol. Neurodegener., 7, 10.1186/1750-1326-7-42 · DOI
- Danzer, 2009, Seeding induced by α-synuclein oligomers provides evidence for spreading of α-synuclein pathology., J. Neurochem., 111, 192, 10.1111/j.1471-4159.2009.06324.x · DOI · Paper page
- Davidson, 1998, Stabilization of α-synuclein secondary structure upon binding to synthetic membranes., J. Biol. Chem., 273, 9443, 10.1074/jbc.273.16.9443 · DOI
- Devergne, 2017, Stratum, a homolog of the human GEF Mss4, partnered with Rab8, controls the basal restriction of basement membrane proteins in epithelial cells., Cell Rep., 18, 1831, 10.1016/j.celrep.2017.02.002 · DOI
- Di Fonzo, 2006, Comprehensive analysis of the LRRK2 gene in sixty families with Parkinson’s disease., Eur. J. Hum. Genet, 14, 322, 10.1038/sj.ejhg.5201539 · DOI
- Do, 2019, Glucocerebrosidase and its relevance to Parkinson disease., Mol. Neurodegener, 14, 10.1186/s13024-019-0336-2 · DOI
- Dodson, 2012, Roles of the Drosophila LRRK2 homolog in Rab7-dependent lysosomal positioning., Hum. Mol. Genet., 21, 1350, 10.1093/hmg/ddr573 · DOI
- Eguchi, 2018, LRRK2 and its substrate Rab GTPases are sequentially targeted onto stressed lysosomes and maintain their homeostasis., Proc. Natl. Acad. Sci. U.S.A., 115, E9115, 10.1073/pnas.1812196115 · DOI
- Follmer, 2015, Oligomerization and membrane-binding properties of covalent adducts formed by the interaction of α-synuclein with the toxic dopamine metabolite 3,4-Dihydroxyphenylacetaldehyde (DOPAL)., J. Biol. Chem., 290, 27660, 10.1074/jbc.M115.686584 · DOI
- Foo, 2013, A rare lysosomal enzyme gene SMPD1 variant (p.R591C) associates with Parkinson’s disease., Neurobiol. Aging, 34, 2890.e13, 10.1016/j.neurobiolaging.2013.06.010 · DOI
- Fortin, 2004, Lipid rafts mediate the synaptic localization of alpha-synuclein., J. Neurosci., 24, 6715, 10.1523/JNEUROSCI.1594-04.2004 · DOI
- Gan-Or, 2013, The p.L302P mutation in the lysosomal enzyme gene SMPD1 is a risk factor for Parkinson disease., Neurology, 80, 1606, 10.1212/WNL.0b013e31828f180e · DOI
- Garrido, 2019, α-synuclein RT-QuIC in cerebrospinal fluid of LRRK2-linked Parkinson’s disease., Ann. Clin. Transl. Neurol., 6, 1024, 10.1002/acn3.772 · DOI
- Gasser, 2015, Usefulness of genetic testing in PD and PD trials: a balanced review., J. Parkinsons. Dis., 5, 209, 10.3233/JPD-140507 · DOI
- Giasson, 2000, Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions., Science, 290, 985, 10.1126/science.290.5493.985 · DOI
- Gilks, 2005, A common LRRK2 mutation in idiopathic Parkinson’s disease., Lancet, 365, 415, 10.1016/S0140-6736(05)17830-1 · DOI · Paper page
- Gloeckner, 2006, The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity., Hum. Mol. Genet., 15, 223, 10.1093/hmg/ddi439 · DOI
- Goldwurm, 2007, Evaluation of LRRK2 G2019S penetrance: relevance for genetic counseling in Parkinson disease., Neurology, 68, 1141, 10.1212/01.wnl.0000254483.19854.ef · DOI
- Gomez, 2019, Membrane association but not identity is required for LRRK2 activation and phosphorylation of Rab GTPases., J. Cell Biol., 218, 4157, 10.1083/jcb.201902184 · DOI · Paper page
- Gómez-Suaga, 2012, Leucine-rich repeat kinase 2 regulates autophagy through a calcium-dependent pathway involving NAADP., Hum. Mol. Genet., 21, 511, 10.1093/hmg/ddr481 · DOI
- Gómez-Suaga, 2014, LRRK2 delays degradative receptor trafficking by impeding late endosomal budding through decreasing Rab7 activity., Hum. Mol. Genet., 23, 6779, 10.1093/hmg/ddu395 · DOI · Paper page
- Greggio, 2009, Leucine-rich repeat kinase 2 mutations and Parkinson’s disease: three questions., ASN Neuro, 1, 10.1042/AN20090007 · DOI
- Greggio, 2006, Kinase activity is required for the toxic effects of mutant LRRK2/dardarin., Neurobiol. Dis., 23, 329, 10.1016/j.nbd.2006.04.001 · DOI · Paper page
- Greggio, 2007, Mutations in LRRK2/dardarin associated with Parkinson disease are more toxic than equivalent mutations in the homologous kinase LRRK1., J. Neurochem., 102, 93, 10.1111/j.1471-4159.2007.04523.x · DOI
- Guo, 2007, The Parkinson’s disease-associated protein, leucine-rich repeat kinase 2 (LRRK2), is an authentic GTPase thatstimulates kinase activity., Exp. Cell Res., 313, 3658, 10.1016/j.yexcr.2007.07.007 · DOI
- Hallett, 2018, Glycosphingolipid levels and glucocerebrosidase activity are altered in normal aging of the mouse brain., Neurobiol. Aging, 67, 189, 10.1016/j.neurobiolaging.2018.02.028 · DOI
- Halliday, 2012, Evaluation of the Braak hypothesis: how far can it explain the pathogenesis of Parkinson’s disease?, Expert Rev. Neurother., 12, 673, 10.1586/ern.12.47 · DOI
- Hanafusa, 2019, LRRK1 phosphorylation of Rab7 at S72 links trafficking of EGFR-containing endosomes to its effector RILP., J. Cell Sci., 132, 10.1242/jcs.228809 · DOI
- Hattula, 2002, A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport., Mol. Biol. Cell, 13, 3268, 10.1091/mbc.E02-03-0143 · DOI
- Hattula, 2006, Characterization of the Rab8-specific membrane traffic route linked to protrusion formation., J. Cell Sci., 119, 4866, 10.1242/jcs.03275 · DOI
- Hein, 2013, Selective reduction of bis(monoacylglycero)phosphate ameliorates the storage burden in a THP-1 macrophage model of Gaucher disease., J. Lipid Res., 54, 1691, 10.1194/jlr.M038232 · DOI
- Henderson, 2019, Alzheimer’s disease tau is a prominent pathology in LRRK2 Parkinson’s disease., Acta Neuropathol. Commun., 7, 10.1186/s40478-019-0836-x · DOI
- Hobert, 2007, A novel role of the Batten disease gene CLN3: association with BMP synthesis., Biochem. Biophys. Res. Commun., 358, 111, 10.1016/j.bbrc.2007.04.064 · DOI
- Hockey, 2015, Dysregulation of lysosomal morphology by pathogenic LRRK2 is corrected by TPC2 inhibition., J. Cell Sci., 128, 232, 10.1242/jcs.164152 · DOI
- Houlden, 2004, A novel RAB7 mutation associated with ulcero-mutilating neuropathy., Ann Neurol, 56, 586, 10.1002/ana.20281 · DOI
- Hsieh, 2016, Functional impairment in miro degradation and mitophagy is a shared feature in familial and sporadic Parkinson’s disease., Cell Stem Cell, 19, 709, 10.1016/j.stem.2016.08.002 · DOI
- Iaccarino, 2007, Apoptotic mechanisms in mutant LRRK2-mediated cell death., Hum. Mol. Genet., 16, 1319, 10.1093/hmg/ddm080 · DOI
- Imai, 2008, Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila., EMBO J., 27, 2432, 10.1038/emboj.2008.163 · DOI
- Ingelsson, 2016, Alpha-synuclein oligomers-neurotoxic molecules in Parkinson’s disease and other Lewy body disorders., Front. Neurosci., 10, 10.3389/fnins.2016.00408 · DOI · Paper page
- Islam, 2017, Mechanisms of LRRK2-dependent neurodegeneration: role of enzymatic activity and protein aggregation., Biochem. Soc. Trans., 45, 163, 10.1042/BST20160264 · DOI
- Itoh, 2006, Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing proteins based on their Rab-binding activity., Genes Cells, 11, 1023, 10.1111/j.1365-2443.2006.00997.x · DOI
- Jäger, 2004, Role for Rab7 in maturation of late autophagic vacuoles., J. Cell Sci., 117, 4837, 10.1242/jcs.01370 · DOI
- Jaleel, 2007, LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson’s disease mutants affect kinase activity., Biochem. J., 405, 307, 10.1042/BJ20070209 · DOI · Paper page
- Jeong, 2018, Dysregulated phosphorylation of Rab GTPases by LRRK2 induces neurodegeneration., Mol. Neurodegener., 13, 10.1186/s13024-018-0240-1 · DOI
- Jimenez-Orgaz, 2018, Control of RAB7 activity and localization through the retromer-TBC1D5 complex enables RAB7-dependent mitophagy., EMBO J., 37, 235, 10.15252/embj.201797128 · DOI · Paper page
- Jordens, 2001, The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors., Curr. Biol., 11, 1680, 10.1016/S0960-9822(01)00531-0 · DOI · Paper page
- Käkelä, 2003, Analysis of phospholipid molecular species in brains from patients with infantile and juvenile neuronal-ceroid lipofuscinosis using liquid chromatography-electrospray ionization mass spectrometry., J. Neurochem., 84, 1051, 10.1046/j.1471-4159.2003.01602.x · DOI
- Kalia, 2019, Expert comment: “A case of missing pathology in a patient with LRRK2 Parkinson’s disease”., Parkinsonism Relat. Disord., 10.1016/j.parkreldis.2019.11.005 · DOI
- Kalia, 2015, Parkinson’s disease., Lancet, 386, 896, 10.1016/S0140-6736(14)61393-3 · DOI · Paper page
- Kalia, 2015, Clinical correlations with Lewy body pathology in LRRK2-related Parkinson disease., JAMA Neurol., 72, 100, 10.1001/jamaneurol.2014.2704 · DOI
- Kim, 2017, The Parkinson’s disease-linked protein TMEM230 is required for Rab8a-mediated secretory vesicle trafficking and retromer trafficking., Hum. Mol. Genet., 26, 729, 10.1093/hmg/ddw413 · DOI
- Kim, 2014, Alpha-synuclein biology in Lewy body diseases., Alzheimers Res. Ther., 6, 10.1186/s13195-014-0073-2 · DOI
- Klemann, 2017, Integrated molecular landscape of Parkinson’s disease., NPJ Parkinsons Dis., 3, 10.1038/s41531-017-0015-3 · DOI
- Korecka, 2019, Mitochondrial clearance and maturation of autophagosomes are compromised in LRRK2 G2019S familial Parkinson’s disease patient fibroblasts., Hum. Mol. Genet., 28, 3232, 10.1093/hmg/ddz126 · DOI
- Lebrand, 2002, Late endosome motility depends on lipids via the small GTPase Rab7., EMBO J., 21, 1289, 10.1093/emboj/21.6.1289 · DOI
- Lee, 2004, Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway., J. Neurosci., 24, 1888, 10.1523/JNEUROSCI.3809-03.2004 · DOI · Paper page
- Lemasters, 2014, Variants of mitochondrial autophagy: types 1 and 2 mitophagy and micromitophagy (Type 3)., Redox Biol., 2, 749, 10.1016/j.redox.2014.06.004 · DOI
- Leng, 2001, Muscarinic receptor stimulation induces translocation of an α-synuclein oligomer from plasma membrane to a light vesicle fraction in cytoplasm., J. Biol. Chem., 276, 28212, 10.1074/jbc.M011121200 · DOI
- Lesage, 2006, LRRK2 G2019S as a cause of Parkinson’s disease in North African Arabs., N. Engl. J. Med, 354, 422, 10.1056/NEJMc055540 · DOI · Paper page
- Lewis, 2007, The R1441C mutation of LRRK2 disrupts GTP hydrolysis., Biochem. Biophys. Res. Commun., 357, 668, 10.1016/j.bbrc.2007.04.006 · DOI
- Linder, 2007, Rab8-dependent recycling promotes endosomal cholesterol removal in normal and sphingolipidosis cells., Mol. Biol. Cell, 18, 47, 10.1091/mbc.E06-07-0575 · DOI
- Liu, 2011, A novel molecular mechanism for nitrated α-synuclein-induced cell death., J. Mol. Cell Biol., 3, 239, 10.1093/jmcb/mjr011 · DOI
- Luzón-Toro, 2007, Mechanistic insight into the dominant mode of the Parkinson’s disease-associated G2019S LRRK2 mutation., Hum. Mol. Genet., 16, 2031, 10.1093/hmg/ddm151 · DOI · Paper page
- MacLeod, 2006, The Familial Parkinsonism gene LRRK2 regulates neurite process morphology., Neuron, 52, 587, 10.1016/j.neuron.2006.10.008 · DOI
- MacLeod, 2013, RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and Parkinson’s disease risk., Neuron, 77, 425, 10.1016/j.neuron.2012.11.033 · DOI · Paper page
- Madero-Pérez, 2018, Parkinson disease-associated mutations in LRRK2 cause centrosomal defects via Rab8a phosphorylation., Mol. Neurodegener., 13, 1, 10.1186/s13024-018-0235-y · DOI
- Manzoni, 2017, The LRRK2–macroautophagy axis and its relevance to Parkinson’s disease., Biochem. Soc. Trans., 45, 155, 10.1042/BST20160265 · DOI
- Manzoni, 2013, Pathogenic Parkinson’s disease mutations across the functional domains of LRRK2 alter the autophagic/lysosomal response to starvation., Biochem. Biophys. Res. Commun., 441, 862, 10.1016/j.bbrc.2013.10.159 · DOI
- Markesbery, 2009, Lewy body pathology in normal elderly subjects., J. Neuropathol. Exp. Neurol., 68, 816, 10.1097/NEN.0b013e3181ac10a7 · DOI · Paper page
- Martinez-Vicente, 2008, Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy., J. Clin. Invest., 118, 777, 10.1172/JCI32806 · DOI
- Meggouh, 2006, Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 gene., Neurology, 67, 1476, 10.1212/01.wnl.0000240068.21499.f5 · DOI
- Mukherjee, 2016, Selective endosomal microautophagy is starvation-inducible in Drosophila., Autophagy, 12, 1984, 10.1080/15548627.2016.1208887 · DOI
- Murphy, 2000, Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons., J. Neurosci., 20, 3214, 10.1523/JNEUROSCI.20-09-03214.2000 · DOI
- Nelson, 2014, Autophagy-lysosome pathway associated neuropathology and axonal degeneration in the brains of alpha-galactosidase A-deficient mice., Acta Neuropathol. Commun., 2, 10.1186/2051-5960-2-20 · DOI
- Nordmann, 2010, The Mon1-Ccz1 complex is the GEF of the late endosomal Rab7 homolog Ypt7., Curr. Biol., 20, 1654, 10.1016/j.cub.2010.08.002 · DOI
- Ozelius, 2006, LRRK2 G2019S as a cause of Parkinson’s disease in Ashkenazi Jews., N. Engl. J. Med, 354, 424, 10.1056/NEJMc055509 · DOI
- Pagano, 2003, Endocytic trafficking of glycosphingolipids in sphingolipid storage diseases., Philos. Trans. R. Soc. Lond. B. Biol. Sci., 358, 885, 10.1098/rstb.2003.1275 · DOI
- Park, 2011, Elevated levels of α-synuclein oligomer in the cerebrospinal fluid of drug-naïve patients with Parkinson’s disease., J. Clin. Neurol., 7, 215, 10.3988/jcn.2011.7.4.215 · DOI
- Pellegrini, 2018, Proteomic analysis reveals co-ordinated alterations in protein synthesis and degradation pathways in LRRK2 knockout mice., Hum. Mol. Genet., 27, 3257, 10.1093/hmg/ddy232 · DOI
- Peng, 2018, Distinct α-Synuclein strains and implications for heterogeneity among α-Synucleinopathies., Neurobiol. Dis., 109, 209, 10.1016/j.nbd.2017.07.018 · DOI
- Peralta, 2010, Differential effects of TBC1D15 and mammalian Vps39 on Rab7 activation state, lysosomal morphology, and growth factor dependence., J. Biol. Chem., 285, 16814, 10.1074/jbc.M110.111633 · DOI
- Peränen, 2011, Rab8 GTPase as a regulator of cell shape., Cytoskeleton, 68, 527, 10.1002/cm.20529 · DOI
- Plowey, 2008, Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells., J. Neurochem., 105, 1048, 10.1111/j.1471-4159.2008.05217.x · DOI
- Poulopoulos, 2012, The neuropathology of genetic Parkinson’s disease., Mov. Disord., 27, 831, 10.1002/mds.24962 · DOI
- Reed, 2019, The role of monogenic genes in idiopathic Parkinson’s disease., Neurobiol. Dis., 124, 230, 10.1016/j.nbd.2018.11.012 · DOI
- Reeve, 2014, Ageing and Parkinson’s disease: why is advancing age the biggest risk factor?, Ageing Res. Rev., 14, 19, 10.1016/j.arr.2014.01.004 · DOI
- Ren, 2019, G2019S variation in LRRK2: an ideal model for the study of Parkinson’s disease?, Front. Hum. Neurosci., 13, 10.3389/fnhum.2019.00306 · DOI
- Rivero-Ríos, 2019, The G2019S variant of leucine-rich repeat kinase 2 (LRRK2) alters endolysosomal trafficking by impairing the function of the GTPase RAB8A., J. Biol. Chem., 294, 4738, 10.1074/jbc.RA118.005008 · DOI · Paper page
- Robak, 2017, Excessive burden of lysosomal storage disorder gene variants in Parkinson’s disease., Brain, 140, 3191, 10.1093/brain/awx285 · DOI · Paper page
- Roberts, 2003, Piecemeal microautophagy of nucleus in Saccharomyces cerevisiae., Mol. Biol. Cell, 14, 129, 10.1091/mbc.e02-08-0483 · DOI · Paper page
- Roberts, 2015, Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson’s disease brain., Brain, 138, 1642, 10.1093/brain/awv040 · DOI
- Rocha, 2015, Progressive decline of glucocerebrosidase in aging and Parkinson’s disease., Ann. Clin. Transl. Neurol., 2, 433, 10.1002/acn3.177 · DOI
- Rojas, 2008, Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7., J. Cell Biol., 183, 513, 10.1083/jcb.200804048 · DOI · Paper page
- Rothaug, 2014, LIMP-2 expression is critical for β-glucocerebrosidase activity and α-synuclein clearance., Proc. Natl. Acad. Sci. U.S.A, 111, 15573, 10.1073/pnas.1405700111 · DOI
- Saha, 2015, Mutations in LRRK2 potentiate age-related impairment of autophagic flux., Mol. Neurodegener., 10, 10.1186/s13024-015-0022-y · DOI
- Sahu, 2011, Microautophagy of cytosolic proteins by late endosomes., Dev. Cell, 20, 131, 10.1016/j.devcel.2010.12.003 · DOI · Paper page
- Saito, 2004, Aberrant phosphorylation of α-synuclein in human niemann-pick type C1 disease., J. Neuropathol. Exp. Neurol., 63, 323, 10.1093/jnen/63.4.323 · DOI
- Sánchez-Danés, 2012, Disease-specific phenotypes in dopamine neurons from human iPS-based models of genetic and sporadic Parkinson’s disease., EMBO Mol. Med., 4, 380, 10.1002/emmm.201200215 · DOI
- Sanyal, 2020, Lysosome and inflammatory defects in GBA1-mutant astrocytes are normalized by LRRK2 inhibition., Mov. Disord., 10.1002/mds.27994 · DOI
- Schapansky, 2018, Familial knockin mutation of LRRK2 causes lysosomal dysfunction and accumulation of endogenous insoluble α-synuclein in neurons., Neurobiol. Dis., 111, 26, 10.1016/j.nbd.2017.12.005 · DOI
- Schneider, 2017, Neuropathology of genetic synucleinopathies with parkinsonism: review of the literature., Mov. Disord., 32, 1504, 10.1002/mds.27193 · DOI
- Segrest, 1992, The amphipathic helix in the exchangeable apolipoproteins: a review of secondary structure and function., J. Lipid Res., 33, 141, 10.1016/S0022-2275(20)41536-6 · DOI
- Seo, 2017, AMPK and vacuole-associated Atg14p orchestrate μ-lipophagy for energy production and long-term survival under glucose starvation., eLife, 6, 10.7554/eLife.21690 · DOI
- Shachar, 2011, Lysosomal storage disorders and Parkinson’s disease: gaucher disease and beyond., Mov. Disord., 26, 1593, 10.1002/mds.23774 · DOI
- Shahmoradian, 2019, Lewy pathology in Parkinson’s disease consists of crowded organelles and lipid membranes., Nat. Neurosci., 22, 1099, 10.1038/s41593-019-0423-2 · DOI
- Sherer, 2003, Subcutaneous rotenone exposure causes highly selective dopaminergic degeneration and α-synuclein aggregation., Exp. Neurol., 179, 9, 10.1006/exnr.2002.8072 · DOI
- Smith, 2014, Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease., J. Pathol., 232, 509, 10.1002/path.4328 · DOI
- Smith, 2006, Kinase activity of mutant LRRK2 mediates neuronal toxicity., Nat. Neurosci., 9, 1231, 10.1038/nn1776 · DOI · Paper page
- Spencer, 2009, Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson’s and Lewy body diseases., J. Neurosci, 29, 13578, 10.1523/JNEUROSCI.4390-09.2009 · DOI · Paper page
- Sridhar, 2013, The lipid kinase PI4KIIIβ preserves lysosomal identity., EMBO J., 32, 324, 10.1038/emboj.2012.341 · DOI · Paper page
- Stefanis, 2019, How is alpha-synuclein cleared from the cell?, J. Neurochem., 150, 577, 10.1111/jnc.14704 · DOI
- Steger, 2017, Systematic proteomic analysis of LRRK2-mediated rab GTPase phosphorylation establishes a connection to ciliogenesis., eLife, 6, 10.7554/eLife.31012 · DOI · Paper page
- Steger, 2016, Phosphoproteomics reveals that Parkinson’s disease kinase LRRK2 regulates a subset of Rab GTPases., eLife, 5, 10.7554/eLife.12813 · DOI · Paper page
- Surmeier, 2017, Parkinson’s disease is not simply a prion disorder., J. Neurosci., 37, 9799, 10.1523/JNEUROSCI.1787-16.2017 · DOI
- Suzuki, 2007, Neuronal and glial accumulation of α- and β-synucleins in human lipidoses., Acta Neuropathol., 114, 481, 10.1007/s00401-007-0264-z · DOI
- Taylor, 2020, Advances in elucidating the function of leucine-rich repeat protein kinase-2 in normal cells and Parkinson’s disease., Curr. Opin. Cell Biol., 63, 102, 10.1016/j.ceb.2020.01.001 · DOI · Paper page
- Tekirdag, 2018, Chaperone-mediated autophagy and endosomal microautophagy: joint by a chaperone., J. Biol. Chem., 293, 5414, 10.1074/jbc.R117.818237 · DOI
- Thirstrup, 2017, Selective LRRK2 kinase inhibition reduces phosphorylation of endogenous Rab10 and Rab12 in human peripheral mononuclear blood cells., Sci. Rep., 7, 10.1038/s41598-017-10501-z · DOI
- Tokuda, 2010, Detection of elevated levels of α-synuclein oligomers in CSF from patients with Parkinson disease., Neurology, 75, 1766, 10.1212/WNL.0b013e3181fd613b · DOI
- Tsuji, 2017, Niemann-pick type C proteins promote microautophagy by expanding raft-like membrane domains in the yeast vacuole., eLife, 6, 10.7554/eLife.25960 · DOI
- Twohig, 2019, α-synuclein in the pathophysiology of Alzheimer’s disease., Mol. Neurodegener., 14, 10.1186/s13024-019-0320-x · DOI · Paper page
- Vaibhava, 2012, Optineurin mediates a negative regulation of Rab8 by the GTPase-activating protein TBC1D17., J. Cell Sci., 125, 5026, 10.1242/jcs.102327 · DOI
- Vanier, 1983, Biochemical studies in niemann-pick disease I. Major sphingolipids of liver and spleen., Biochim. Biophys. Acta, 750, 178, 10.1016/0005-2760(83)90218-7 · DOI
- Verhoeven, 2003, Mutations in the small GTP-ase late endosomal protein RAB7 cause Charcot-Marie-Tooth type 2B neuropathy., Am. J. Hum. Genet, 72, 722, 10.1086/367847 · DOI
- Walkley, 2009, Secondary lipid accumulation in lysosomal disease., Biochim. Biophys. Acta, 1793, 726, 10.1016/j.bbamcr.2008.11.014 · DOI
- Wallings, 2019, LRRK2 interacts with the vacuolar-type H+-ATPase pump a1 subunit to regulate lysosomal function., Hum. Mol. Genet., 28, 2696, 10.1093/hmg/ddz088 · DOI
- Walter, 2019, Neural stem cells of Parkinson’s disease patients exhibit aberrant mitochondrial morphology and functionality., Stem Cell Rep., 12, 878, 10.1016/j.stemcr.2019.03.004 · DOI
- West, 2017, Achieving neuroprotection with LRRK2 kinase inhibitors in Parkinson disease., Exp. Neurol., 298, 236, 10.1016/j.expneurol.2017.07.019 · DOI
- West, 2005, Parkinson’s disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity., Proc. Natl. Acad. Sci. U.S.A., 102, 16842, 10.1073/pnas.0507360102 · DOI · Paper page
- West, 2007, Parkinson’s disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity., Hum. Mol. Genet., 16, 223, 10.1093/hmg/ddl471 · DOI · Paper page
- Xu, 2010, Multi-system disorders of glycosphingolipid and ganglioside metabolism., J. Lipid Res., 51, 1643, 10.1194/jlr.R003996 · DOI
- Yakhine-Diop, 2014, G2019S LRRK2 mutant fibroblasts from Parkinson’s disease patients show increased sensitivity to neurotoxin 1-methyl-4-phenylpyridinium dependent of autophagy., Toxicology, 324, 1, 10.1016/j.tox.2014.07.001 · DOI
- Yasuda, 2016, Mon1-Ccz1 activates Rab7 only on late endosomes and dissociates from the lysosome in mammalian cells., J. Cell Sci., 129, 329, 10.1242/jcs.178095 · DOI
- Yoshimura, 2010, Family-wide characterization of the DENN domain Rab GDP-GTP exchange factors., J. Cell Biol., 191, 367, 10.1083/jcb.201008051 · DOI · Paper page
- Ysselstein, 2019, LRRK2 kinase activity regulates lysosomal glucocerebrosidase in neurons derived from Parkinson’s disease patients., Nat. Commun., 10, 10.1038/s41467-019-13413-w · DOI
- Zhang, 2018, Tau pathology in Parkinson’s disease., Front. Neurol., 9, 10.3389/fneur.2018.00809 · DOI
- Zhang, 2005, TBC domain family, member 15 is a novel mammalian Rab GTPase-activating protein with substrate preference for Rab7., Biochem. Biophys. Res. Commun., 335, 154, 10.1016/j.bbrc.2005.07.070 · DOI
- Zunke, 2018, Reversible conformational conversion of α-synuclein into toxic assemblies by glucosylceramide., Neuron, 97, 92, 10.1016/j.neuron.2017.12.012 · DOI
Cited by
Sorted by citations
Rivero-Ríos, P., Romo-Lozano, M., Fernández, B., Fdez, E., & Hilfiker, S. (2020) · Cells · doi:10.3390/cells9071719 · Cited by 38
Self-citation
Metadata
- Authors
- Rivero-Ríos, P., Romo-Lozano, M., Fasiczka, R., Naaldijk, Y., & Hilfiker, S.
- Venue
- Frontiers in Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2020-06-04
- Volume
- 14
- ISSN
- 1662-453X
- PMC
- PMC7287096
- Cited by
- 31
- References
- 16
- Funders
- Michael J. Fox Foundation for Parkinson's Research
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