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Reduced LRRK2 in association with retromer dysfunction in post-mortem brain tissue from LRRK2 mutation carriers

Zhao, Ye, Perera, Gayathri, Takahashi-Fujigasaki, Junko, Mash, Deborah C, Vonsattel, Jean Paul G, Uchino, Akiko, Hasegawa, Kazuko, Jeremy Nichols, R, Holton, Janice L, Murayama, Shigeo, Dzamko, Nicolas, Halliday, Glenda M·2018·Brain
DOI 10.1093/brain/awx344PMC PMC5837795
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Research works printed but not linked: 35

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  3. Cookson, 2010, The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease, Nat Rev Neurosci, 11, 791, 10.1038/nrn2935 · DOI
  4. Davies, 2013, Comprehensive characterization and optimization of anti-LRRK2 (leucine-rich repeat kinase 2) monoclonal antibodies, Biochem J, 453, 101, 10.1042/BJ20121742 · DOI
  5. Devine, 2011, Pathogenic LRRK2 mutations do not alter gene expression in cell model systems or human brain tissue, PLoS One, 6, e22489, 10.1371/journal.pone.0022489 · DOI
  6. Dickson, 2009, Neuropathological assessment of Parkinson's disease: refining the diagnostic criteria, Lancet Neurol, 8, 1150, 10.1016/S1474-4422(09)70238-8 · DOI · Paper page
  7. Dzamko, 2017, LRRK2 levels and phosphorylation in Parkinson's disease brain and cases with restricted Lewy bodies, Mov Disord, 32, 423, 10.1002/mds.26892 · DOI
  8. Gan-Or, 2015, Genetic perspective on the role of the autophagy-lysosome pathway in Parkinson disease, Autophagy, 11, 1443, 10.1080/15548627.2015.1067364 · DOI · Paper page
  9. Garcia-Miralles, 2015, No dopamine cell loss or changes in cytoskeleton function in transgenic mice expressing physiological levels of wild type or G2019S mutant LRRK2 and in human fibroblasts, PLoS One, 10, e0118947, 10.1371/journal.pone.0118947 · DOI
  10. Hasegawa, 2009, Familial parkinsonism: study of original Sagamihara PARK8 (I2020T) kindred with variable clinicopathologic outcomes, Parkinsonism Relat Disord, 15, 300, 10.1016/j.parkreldis.2008.07.010 · DOI
  11. Healy, 2008, Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case-control study, Lancet Neurol, 7, 583, 10.1016/S1474-4422(08)70117-0 · DOI · Paper page
  12. Kalia, 2015, Clinical correlations with Lewy body pathology in LRRK2-related Parkinson disease, JAMA Neurol, 72, 100, 10.1001/jamaneurol.2014.2704 · DOI
  13. Linhart, 2014, Vacuolar protein sorting 35 (Vps35) rescues locomotor deficits and shortened lifespan in Drosophila expressing a Parkinson's disease mutant of Leucine-Rich Repeat Kinase 2 (LRRK2), Mol Neurodegener, 9, 23, 10.1186/1750-1326-9-23 · DOI
  14. Lobbestael, 2016, Pharmacological LRRK2 kinase inhibition induces LRRK2 protein destabilization and proteasomal degradation, Sci Rep, 6, 33897, 10.1038/srep33897 · DOI
  15. 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
  16. Malik, 2017, Synthesis and in vitro and in vivo evaluation of [3H]LRRK2-IN-1 as a novel radioligand for LRRK2, Mol Imaging Biol, 19, 837, 10.1007/s11307-017-1070-1 · DOI
  17. Marder, 2015, Age-specific penetrance of LRRK2 G2019S in the Michael J. Fox Ashkenazi Jewish LRRK2 Consortium, Neurology, 85, 89, 10.1212/WNL.0000000000001708 · DOI
  18. Matrone, 2016, Mannose 6-phosphate receptor is reduced in α-synuclein overexpressing models of Parkinsons disease, PLoS One, 11, e0160501, 10.1371/journal.pone.0160501 · DOI
  19. Murphy, 2015, Lysosomal-associated membrane protein 2 isoforms are differentially affected in early Parkinson's disease, Mov Disord, 30, 1639, 10.1002/mds.26141 · DOI
  20. Orenstein, 2013, Interplay of LRRK2 with chaperone-mediated autophagy, Nat Neurosci, 16, 394, 10.1038/nn.3350 · DOI · Paper page
  21. Papkovskaia, 2012, G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization, Hum Mol Genet, 21, 4201, 10.1093/hmg/dds244 · DOI
  22. Sasaki, 2015, Sensitive western blotting for detection of endogenous Ser129-phosphorylated alpha-synuclein in intracellular and extracellular spaces, Sci Rep, 5, 14211, 10.1038/srep14211 · DOI
  23. Sharma, 2011, LRRK2 expression in idiopathic and G2019S positive Parkinson's disease subjects: a morphological and quantitative study, Neuropathol Appl Neurobiol, 37, 777, 10.1111/j.1365-2990.2011.01187.x · DOI
  24. Sheng, 2012, Ser1292 autophosphorylation is an indicator of LRRK2 kinase activity and contributes to the cellular effects of PD mutations, Sci Transl Med, 4, 164ra1, 10.1126/scitranslmed.3004485 · DOI
  25. Siebert, 2014, Glucocerebrosidase is shaking up the synucleinopathies, Brain, 137, 1304, 10.1093/brain/awu002 · DOI
  26. Smith, 2016, Fibroblast biomarkers of sporadic Parkinson's disease and LRRK2 kinase inhibition, Mol Neurobiol, 53, 5161, 10.1007/s12035-015-9435-4 · DOI
  27. Steger, 2016, Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases, Elife, 10.7554/eLife.12813 · DOI · Paper page
  28. Struhal, 2014, VPS35 Parkinson's disease phenotype resembles the sporadic disease, J Neural Transm, 121, 755, 10.1007/s00702-014-1179-1 · DOI
  29. Trinh, 2014, Disease penetrance of late-onset parkinsonism: a meta-analysis, JAMA Neurol, 71, 1535, 10.1001/jamaneurol.2014.1909 · DOI
  30. Trousdale, 2015, Retromer: structure, function, and roles in mammalian disease, Eur J Cell Biol, 94, 513, 10.1016/j.ejcb.2015.07.002 · DOI
  31. Tsika, 2014, Parkinson's disease-linked mutations in VPS35 induce dopaminergic neurodegeneration, Hum Mol Genet, 23, 4621, 10.1093/hmg/ddu178 · DOI · Paper page
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  33. Williams, 2017, VPS35, the retromer complex and Parkinson's disease, J Parkinsons Dis, 7, 219, 10.3233/JPD-161020 · DOI
  34. Zhou, 2011, Changes in the solubility and phosphorylation of alpha-synuclein over the course of Parkinson's disease, Acta Neuropathol, 121, 695, 10.1007/s00401-011-0815-1 · DOI
  35. Zimprich, 2011, A mutation in VPS35, encoding a subunit of the retromer complex, causes late-onset Parkinson disease, Am J Hum Genet, 89, 168, 10.1016/j.ajhg.2011.06.008 · DOI · Paper page

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Metadata

Authors
Zhao, Y., Perera, G., Takahashi-Fujigasaki, J., Mash, D. C., Vonsattel, J. P. G., Uchino, A., Hasegawa, K., Jeremy Nichols, R., Holton, J. L., Murayama, S., Dzamko, N., & Halliday, G. M.
Venue
Brain
Publisher
Oxford University Press (OUP)
Published
2017-12-14
Volume
141
Issue
2
Pages
486-495
ISSN
  • 0006-8950
  • 1460-2156
DOI
10.1093/brain/awx344
PMC
PMC5837795
Cited by
49
References
2
Language
en
Licence
creativecommons.org/licenses/by-nc/4.0/ (vor)
Funders
  • National Institutes of Health
  • National Institute of Mental Health
  • National Institute of Neurological Disorders and Stroke

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