The role of the LRRK2 gene in Parkinsonism

Li, Jie-Qiong; Tan, Lan; Yu, Jin-Tai

doi:10.1186/1750-1326-9-47

Cited by 253Parkinson's Disease Mechanisms and TreatmentsNuclear Receptors and SignalingNeurological disorders and treatments

The role of the LRRK2 gene in Parkinsonism

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Li, Jie-Qiong, Tan, Lan, Yu, Jin-Tai·2014·Molecular Neurodegeneration

DOI 10.1186/1750-1326-9-47PMC PMC4246469

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Abstract

Parkinson's disease (PD), like many common age-related conditions, has been recognized to have a substantial genetic component. Multiple lines of evidence suggest that Leucine-rich repeat kinase 2 (LRRK2) is a crucial factor to understanding the etiology of PD. LRRK2 is a large, widely expressed, multi-domain and multifunctional protein. LRRK2 mutations are the major cause to inherited and sporadic PD. In this review, we discuss the pathology and clinical features which show diversity and variability of LRRK2-associated PD. In addition, we do a thorough literature review and provide theoretical data for gene counseling. Further, we present the evidence linking LRRK2 to various possible pathogenic mechanism of PD such as α-synuclein, tau, inflammatory response, oxidative stress, mitochondrial dysfunction, synaptic dysfunction as well as autophagy-lysosomal system. Based on the above work, we investigate activities both within GTPase and outside enzymatic regions in order to obtain a potential therapeutic approach to solve the LRRK2 problem.

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PD is characterized by filamentous and oligomeric α-synuclein accumulation and degeneration of dopaminergic neurons in the substantia nigra pars compacta leading to motor impairments.
“It is characterized by filamentous and oligomeric 𝛂 -synuclein ( 𝛂 -syn) accumulation, and degeneration of dopaminergic neurons in the substantia nigra pars compacta (SNpc) leading to motor impairments (357, 616).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [357]
The Introduction describes loss of dopaminergic neurons in the substantia nigra pars compacta, α-synuclein-positive Lewy inclusions, and motor symptoms of PD. The LRRK2 and α-synuclein section also discusses α-synuclein aggregation. Neither passage specifies filamentous and oligomeric α-synuclein accumulation, so that detail is unsupported by this source. (LLM, conf=0.86)
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The most common LRRK2 mutation, G2019S (gain of function), is associated with 2% of sporadic cases and 6% of familial cases.
“The most common LRRK2 mutation, G2019S (gain of function), is associated with 2% of sporadic cases and 6% of familial cases (357).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [357]
LRRK2 (PARK8) gene mutations are the most common genetic cause of both familial and sporadic PD.
“LRRK2 (PARK8) gene mutations are the most common genetic cause of both familial and sporadic PD.257”
From Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets (2023) · cites this paper as [257]

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Manzoni, C., Mamais, A., Dihanich, S., Abeti, R., Soutar, M. P. M., Plun‐Favreau, H., Giunti, P., Tooze, S. A., Bandopadhyay, R., & Lewis, P. A. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.07.020 · Cited by 151 · see citing works
LRRK2-mediated neurodegeneration and dysfunction of dopaminergic neurons in a Caenorhabditis elegans model of Parkinson's disease
Yao, C., Khoury, R. E., Wang, W., Byrd, T. A., Pehek, E. A., Thacker, C. M., Zhu, X., Smith, M. A., Wilson‐Delfosse, A. L., & Chen, S. G. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.04.002 · Cited by 148 · see citing works
LRRK2 in Parkinson’s disease: genetic and clinical studies from patients
Kumari, U., & Tan, E. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07344.x · Cited by 144 · see citing works
Development and Characterization of a New Parkinson's Disease Model Resulting from Impaired Autophagy
Ahmed, 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 · see citing works
Brain stem pathology in Parkinson's disease: An evaluation of the Braak staging model
Kingsbury, A. E., Bandopadhyay, R., Silveira‐Moriyama, L., Ayling, H., Kallis, C., Sterlacci, W., Maeir, H., Poewe, W. H., & Lees, A. J. (2010) · Movement Disorders · doi:10.1002/mds.23305 · Cited by 142 · see citing works
Mechanistic insight into the dominant mode of the Parkinson's disease-associated G2019S LRRK2 mutation
Luzón-Toro, B., de la Torre, E. R., Delgado, A., Pérez‐Tur, J., & Hilfiker, S. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm151 · Cited by 140 · see citing works
Mutant LRRK2 Toxicity in Neurons Depends on LRRK2 Levels and Synuclein But Not Kinase Activity or Inclusion Bodies
Skibinski, G., Nakamura, K., Cookson, M., & Finkbeiner, S. M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.2712-13.2014 · Cited by 138 · see citing works
A Direct Interaction between Leucine-rich Repeat Kinase 2 and Specific β-Tubulin Isoforms Regulates Tubulin Acetylation
Law, B. M. H., Spain, V. A., Leinster, V. H. L., Chia, R., Beilina, A. G., Cho, H. J., Taymans, J., Urban, M. K., Sancho, R. M., Ramírez, M. B., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.507913 · Cited by 135 · see citing works
Mutations in LRRK2 increase phosphorylation of peroxiredoxin 3 exacerbating oxidative stress-induced neuronal death
Angeles, D. C., Gan, B.-H., Onstead, L., Zhao, Y., Lim, K., Dächsel, J. C., Melrose, H. L., Farrer, M. J., Wszołek, Z. K., Dickson, D. W., et al. (2011) · Human Mutation · doi:10.1002/humu.21582 · Cited by 129 · see citing works
LRRK2 Phosphorylates Tubulin-Associated Tau but Not the Free Molecule: LRRK2-Mediated Regulation of the Tau-Tubulin Association and Neurite Outgrowth
Kawakami, F., Takatoshi, Y., Ohta, E., Maekawa, T., Shimada, N., Suzuki, M., Maruyama, H., Ichikawa, T., & Obata, F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030834 · Cited by 123 · see citing works
LRRK2 enhances oxidative stress-induced neurotoxicity via its kinase activity
Heo, H. Y., Park, J.-M., Kim, C.-H., Han, B., Kim, K., & Seol, W. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.09.014 · Cited by 122 · see citing works
Familial parkinsonism: Study of original Sagamihara PARK8 (I2020T) kindred with variable clinicopathologic outcomes
Hasegawa, K., Stoessl, A. J., Yokoyama, T., Kowa, H., Wszołek, Z. K., & Yagishita, S. (2008) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2008.07.010 · Cited by 118 · see citing works
The WD40 Domain Is Required for LRRK2 Neurotoxicity
Jorgensen, N. D., Peng, Y., Ho, C. C., Rideout, H. J., Petrey, D. S., Liu, P., & Dauer, W. T. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008463 · Cited by 111 · see citing works
Genetic characteristics of leucine-rich repeat kinase 2 (LRRK2) associated Parkinson’s disease
Bardien, S., Lesage, S., Brice, A., & Carr, J. A. (2011) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2010.11.008 · Cited by 111 · see citing works
Activity-related redistribution of presynaptic proteins at the active zone
Tao-Cheng, J.-H. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.04.061 · Cited by 104 · see citing works
Inhibition of mitogen-activated protein kinase and stimulation of Akt kinase signaling pathways: Two approaches with therapeutic potential in the treatment of neurodegenerative disease
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A comparative study of Parkinson's disease and leucine-rich repeat kinase 2 p.G2019S parkinsonism
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LRRK2 interactions with α-synuclein in Parkinson’s disease brains and in cell models
Guerreiro, P. S., Huang, Y. M., Gysbers, A. M., Cheng, D., Gai, W., Outeiro, T. F., & Halliday, G. M. (2012) · Journal of Molecular Medicine · doi:10.1007/s00109-012-0984-y · Cited by 83 · see citing works
Structural biology of the LRRK2 GTPase and kinase domains: implications for regulation
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Clinical and brain imaging characteristics in leucine‐rich repeat kinase 2–associated PD and asymptomatic mutation carriers
Brockmann, K., Gröger, A., Santo, A. D., Liepelt, I., Schulte, C., Klose, U., Maetzler, W., Hauser, A., Hilker, R., Gomez‐Mancilla, B., et al. (2011) · Movement Disorders · doi:10.1002/mds.23991 · Cited by 80 · see citing works
Abnormal Localization of Leucine-Rich Repeat Kinase 2 to the Endosomal-Lysosomal Compartment in Lewy Body Disease
Higashi, S., Moore, D. J., Yamamoto, R., Minegishi, M., Sato, K., Togo, T., Katsuse, O., Uchikado, H., Furukawa, Y., Hino, H., et al. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181b44ed8 · Cited by 79 · see citing works
The Neurobiology of LRRK2 and its Role in the Pathogenesis of Parkinson’s Disease
Rideout, H. J., & Stefanis, L. (2013) · Neurochemical Research · doi:10.1007/s11064-013-1073-5 · Cited by 78 · see citing works
Parkinson's disease and family history
Sellbach, A., Boyle, R. S., Silburn, P. A., & Mellick, G. D. (2006) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2006.03.002 · Cited by 76 · see citing works
Ancient Origin of the Parkinson Disease Gene LRRK2
Marı́n, I. (2008) · Journal of Molecular Evolution · doi:10.1007/s00239-008-9122-4 · Cited by 76 · see citing works
Kinase inhibitors arrest neurodegeneration in cell and C. elegans models of LRRK2 toxicity
Yao, C., Johnson, W. M., Gao, Y., Wang, W., Zhang, J., Deák, M., Alessi, D. R., Zhu, X., Mieyal, J. J., Röder, H., et al. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds431 · Cited by 76 · see citing works
LRRK2 and neurodegeneration
Santpere, G., & Ferrer, I. (2009) · Acta Neuropathologica · doi:10.1007/s00401-008-0478-8 · Cited by 73 · see citing works
Lysosomal membrane permeabilization in Parkinson disease
Vila, M., Bové, J., Dehay, B., Rodríguez‐Muela, N., & Boya, P. (2010) · Autophagy · doi:10.4161/auto.7.1.13933 · Cited by 71 · see citing works
Neuropathology of Parkinson's disease with the R1441G mutation in LRRK2
Martí-Massó, J. F., Ruiz‐Martínez, J., Bolaño, M. J., Ruiz, I., Gorostidi, A., Moreno, F., Ferrer, I., & de Munaín, A. L. (2009) · Movement Disorders · doi:10.1002/mds.22677 · Cited by 70 · see citing works
Non-Motor and Motor Features in LRRK2 Transgenic Mice
Bichler, Z., Lim, H. C., Zeng, L., & Tan, E. K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070249 · Cited by 70 · see citing works
Leucine‐rich repeat kinase 2 regulates tau phosphorylation through direct activation of glycogen synthase kinase‐3β
Kawakami, F., Shimada, N., Ohta, E., Kagiya, G., Kawashima, R., Maekawa, T., Maruyama, H., & Ichikawa, T. (2013) · FEBS Journal · doi:10.1111/febs.12579 · Cited by 67 · see citing works
Kinase Inhibitors as Potential Therapeutics for Acute and Chronic Neurodegenerative Conditions
Cuny, G. D. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209789649330 · Cited by 65 · see citing works
Type II Kinase Inhibitors Show an Unexpected Inhibition Mode against Parkinson’s Disease-Linked LRRK2 Mutant G2019S
Liu, M., Bender, S. A., Cuny, G. D., Sherman, W., Glicksman, M. A., & Ray, S. S. (2013) · Biochemistry · doi:10.1021/bi3012077 · Cited by 63 · see citing works
LRRK2 in Parkinson’s disease: biochemical functions
Anand, V. S., & Braithwaite, S. P. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07341.x · Cited by 60 · see citing works
Analysis of 14 LRRK2 mutations in Parkinson's plus syndromes and late‐onset Parkinson's disease
Tan, E., Skipper, L. M., Chua, E., Wong, M. C., Ratnagopal, P., Bonnard, C., Kolatkar, P. R., & Liu, J. (2006) · Movement Disorders · doi:10.1002/mds.20875 · Cited by 60 · see citing works
Synaptic dysfunction in genetic models of Parkinson's disease: A role for autophagy?
Plowey, E. D., & Chu, C. T. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.10.011 · Cited by 59 · see citing works
Leucine-rich repeat kinase 2 functionally interacts with microtubules and kinase-dependently modulates cell migration
Caesar, M., Zach, S., Carlson, C. B., Brockmann, K., Gasser, T., & Gillardon, F. (2013) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.12.019 · Cited by 59 · see citing works
CORTICOBASAL SYNDROME AND PRIMARY PROGRESSIVE APHASIA AS MANIFESTATIONS OF LRRK2 GENE MUTATIONS
Ross, O. A., Toft, M., & Haugarvoll, K. (2008) · Neurology · doi:10.1212/01.wnl.0000320511.30222.dd · Cited by 57 · see citing works
.ALPHA.-Synuclein Aggregation and Transmission Are Enhanced by Leucine-Rich Repeat Kinase 2 in Human Neuroblastoma SH-SY5Y Cells
Kondo, K., Obitsu, S., & Teshima, R. (2011) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.34.1078 · Cited by 56 · see citing works
Corticobasal syndrome and primary progressive aphasia as manifestations of LRRK2 gene mutations
Chen‐Plotkin, A. S., Yuan, W., Anderson, C., Wood, E. M., Hurtig, H. I., Clark, C. M., Miller, B. L., Lee, V. M.-Y., Trojanowski, J. Q., Grossman, M., et al. (2007) · Neurology · doi:10.1212/01.wnl.0000280574.17166.26 · Cited by 54 · see citing works
Thiol peroxidases ameliorate LRRK2 mutant-induced mitochondrial and dopaminergic neuronal degeneration in Drosophila
Angeles, D. C., Ho, P., Chua, L. L., Wang, C., Yap, Y. W., Ng, C., Zhou, Z., Lim, K., Wszołek, Z. K., Wang, H. Y., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu026 · Cited by 51 · see citing works
LRRK2 as a modulator of lysosomal calcium homeostasis with downstream effects on autophagy
Gómez‐Suaga, P., & Hilfiker, S. (2012) · Autophagy · doi:10.4161/auto.19305 · Cited by 46 · see citing works
LRRK2, but not pathogenic mutants, protects against H2O2 stress depending on mitochondrial function and endocytosis in a yeast model
Pereira, C., Martins, L. M., & Saraiva, L. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.02.015 · Cited by 45 · see citing works
Diapocynin prevents early Parkinson's disease symptoms in the leucine-rich repeat kinase 2 (LRRK2R1441G) transgenic mouse
Dranka, B. P., Gifford, A., Ghosh, A., Zielonka, J., Joseph, J., Kanthasamy, A. G., & Kalyanaraman, B. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.05.034 · Cited by 43 · see citing works
Investigating Convergent Actions of Genes Linked to Familial Parkinson’s Disease
Wolozin, B. L., Saha, S., Guillily, M. D., Ferree, A. W., & Riley, M. M. (2008) · Neurodegenerative Diseases · doi:10.1159/000113697 · Cited by 42 · see citing works
Mood and cognition in leucine‐rich repeat kinase 2 G2019S Parkinson's disease
Shanker, V., Groves, M., Heiman, G. A., Palmese, C. A., Saunders-Pullman, R. J., Ozelius, L. J., Raymond, D., & Bressman, S. (2011) · Movement Disorders · doi:10.1002/mds.23746 · Cited by 40 · see citing works
LRRK2 R1628P variant is a risk factor of Parkinson's disease among Han‐Chinese from mainland China
Zhang, Z., Burgunder, J., An, X., Wu, Y. P., Chen, W., Zhang, J., Wang, Y., Xu, Y., Gou, Y., Yuan, G., et al. (2009) · Movement Disorders · doi:10.1002/mds.22371 · Cited by 39 · see citing works
The LRRK2 G2019S mutation in a series of Argentinean patients with Parkinson's disease: Clinical and demographic characteristics
Gatto, E. M., Parisi, V. L., Converso, D. P., Poderoso, J. J., Carreras, M. C., Martí-Massó, J. F., & Paisán‐Ruiz, C. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.01.011 · Cited by 38 · see citing works
G2019S mutation in the leucine‐rich repeat kinase 2 gene is not associated with multiple system atrophy
Ozelius, L. J., Foroud, T., May, S. J., Senthil, G., Sandroni, P., Low, P. A., Reich, S. G., Colcher, A., Stern, M. B., Ondo, W. G., et al. (2007) · Movement Disorders · doi:10.1002/mds.21343 · Cited by 37 · see citing works
Haplotype analysis of Lrrk2 R1441H carriers with parkinsonism
Ross, O. A., Spanaki, C., Griffith, A., Lin, C., Kachergus, J. M., Haugarvoll, K., Latsoudis, H., Plaitakis, A., Ferreira, J. J., Sampaio, C., et al. (2008) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2008.09.001 · Cited by 35 · see citing works
A common leucine‐rich repeat kinase 2 gene mutation in familial and sporadic Parkinson's disease in Russia
Illarioshkin, S. N., Shadrina, M. I., Slominsky, P. A., Bespalova, E. V., Борисовна, З. Т., Bagyeva, G. K., Markova, E. D., Limborska, S. A., & Ivanova‐Smolenskaya, I. A. (2007) · European Journal of Neurology · doi:10.1111/j.1468-1331.2007.01685.x · Cited by 27 · see citing works
The LRRK2 G2019S mutation status does not affect the outcome of subthalamic stimulation in patients with Parkinson's disease
Greenbaum, L., Israeli‐Korn, S., Cohen, O. S., Elincx-Benizri, S., Yahalom, G., Kozlova, E., Strauss, H., Molshatzki, N., Inzelberg, R., Spiegelmann, R., et al. (2013) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2013.07.005 · Cited by 26 · see citing works
The MAPK1/3 pathway is essential for the deregulation of autophagy observed in G2019S LRRK2 mutant fibroblasts
Pedro, J. M. B., Gómez‐Sánchez, R., Niso‐Santano, M., Pizarro‐Estrella, E., Aiastui, A., Gorostidi, A., Climent, V. E., de Maturana, R. L., Sánchez‐Pernaute, R., de Munaín, A. L., et al. (2012) · Autophagy · doi:10.4161/auto.21270 · Cited by 25 · see citing works
Structural and functional in silico analysis of LRRK2 missense substitutions
Cardona, F., Tormos-Pérez, M., & Pérez-Tur, J. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3111-z · Cited by 25 · see citing works
Expression of leucine-rich repeat kinase 2 (LRRK2) inhibits the processing of uMtCK to induce cell death in a cell culture model system
Cui, J., Yu, M., Niu, J., Yue, Z., & Xu, Z. (2011) · Bioscience Reports · doi:10.1042/bsr20100127 · Cited by 20 · see citing works
Genetic analysis of Parkinson's disease-linked leucine-rich repeat kinase 2
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Co-occurrence of Sporadic Parkinsonism and Late-Onset Alzheimer's Disease in a Brazilian Male with the LRRK2 p.G2019S Mutation
Santos-Rebouças, C. B., Abdalla, C. B., Baldi, F. J. R., Martins, P. Á., Corrêa, J. C., Gonçalves, A. P., Cunha, M. S., de Borges, M. B., Pereira, J. S., Laks, J., et al. (2008) · Genetic Testing · doi:10.1089/gte.2008.0042 · Cited by 18 · see citing works
ATP-competitive LRRK2 inhibitors interfere with monoclonal antibody binding to the kinase domain of LRRK2 under native conditions. A method to directly monitor the active conformation of LRRK2?
Gillardon, F., Kremmer, E., Froehlich, T. W., Ueffing, M., Hengerer, B., & Gloeckner, C. J. (2013) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2012.12.015 · Cited by 12 · see citing works
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Development of Inducible Leucine-rich Repeat Kinase 2 (LRRK2) Cell Lines for Therapeutics Development in Parkinson's Disease
Huang, L., Shimoji, M., Wang, J., Shah, S., Kamila, S., Biehl, E. R., Lim, S., Chang, A., Maguire‐Zeiss, K. A., Su, X., et al. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0208-3 · Cited by 4 · see citing works
[A PARK8 form of Parkinson's disease: a mutational analysis of the LRRK2 gene in Russian population].
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P3‐276: Physical activity is predictive of dementia but not mortality
Garcia, J. M., Erickson, K. I., Raji, C. A., López, O. L., Newman, A. B., Rosano, C., & Kuller, L. H. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2011.05.1718 · Cited by 1 · see citing works

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Blood-Brain Barrier: From Physiology to Disease and Back
Sweeney, M. D., Zhao, Z., Montagne, A., Nelson, A. R., & Zlokovic, B. V. (2019) · Physiological Reviews · doi:10.1152/physrev.00050.2017 · Cited by 2,294 · see citing works
Microglia in neurodegenerative diseases: mechanism and potential therapeutic targets
Gao, C., Jiang, J., Tan, Y., & Chen, S. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01588-0 · Cited by 1,616 · see citing works
Inflammation in Parkinson’s Disease: Mechanisms and Therapeutic Implications
Pajares, M., I. Rojo, A., Manda, G., Boscá, L., & Cuadrado, A. (2020) · Cells · doi:10.3390/cells9071687 · Cited by 779 · see citing works
Brain-Gut-Microbiota Axis in Parkinson’s Disease
Mulak, A. (2015) · World Journal of Gastroenterology · doi:10.3748/wjg.v21.i37.10609 · Cited by 583 · see citing works
Autophagy in Parkinson's Disease
Hou, X., Watzlawik, J. O., Fiesel, F. C., & Springer, W. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.037 · Cited by 355 · see citing works
Alpha-Synuclein Aggregation in Parkinson's Disease
Srinivasan, E., Chandrasekhar, G., Chandrasekar, P., Anbarasu, K., Vickram, A. S., Karunakaran, R., Rajasekaran, R., & Srikumar, P. S. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.736978 · Cited by 262 · see citing works
Autophagy, aging, and age-related neurodegeneration
Palmer, J. E., Wilson, N., Son, S. M., Obrocki, P., Wróbel, L., Rob, M., Takla, M., Korolchuk, V. I., & Rubinsztein, D. C. (2024) · Neuron · doi:10.1016/j.neuron.2024.09.015 · Cited by 255 · see citing works
microRNAs in Parkinson’s Disease: From Pathogenesis to Novel Diagnostic and Therapeutic Approaches
Leggio, L., Vivarelli, S., L’Episcopo, F., Tirolo, C., Caniglia, S., Testa, N., Marchetti, B., & Iraci, N. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122698 · Cited by 216 · see citing works
Parkinson's disease: Cause factors, measurable indicators, and early diagnosis
Bhat, S., Acharya, U. R., Hagiwara, Y., Dadmehr, N., & Adeli, H. (2018) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2018.09.008 · Cited by 211 · see citing works
The Parkinson's disease VPS35[D620N] mutation enhances LRRK2-mediated Rab protein phosphorylation in mouse and human
Mir, R., Tonelli, F., Lis, P., Macartney, T., Polinski, N. K., Martinez, T. N., Chou, M.-Y., Howden, A. J. M., König, T., Hotzy, C., et al. (2018) · Biochemical Journal · doi:10.1042/bcj20180248 · Cited by 205 · see citing works
LRRK2 kinase activity regulates lysosomal glucocerebrosidase in neurons derived from Parkinson’s disease patients
Ysselstein, D., Nguyen, M. N., Young, T. J., Severino, A., Schwake, M., Merchant, K., & Krainc, D. (2019) · Nature Communications · doi:10.1038/s41467-019-13413-w · Cited by 188 · see citing works
The impact of obesity on neurodegenerative diseases.
Mazon, J. N., de Mello, A. H., Ferreira, G. K., & Rezin, G. T. (2017) · Life Sciences · doi:10.1016/j.lfs.2017.06.002 · Cited by 185 · see citing works
Brain Disorders Due to Lysosomal Dysfunction
Fraldi, A., Klein, A. D., Medina, D. L., & Settembre, C. (2016) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-070815-014031 · Cited by 169 · see citing works
Early synaptic dysfunction in Parkinson's disease: Insights from animal models
Schirinzi, T., Madeo, G., Martella, G., Maltese, M., Picconi, B., Calabresi, P., & Pisani, A. (2016) · Movement Disorders · doi:10.1002/mds.26620 · Cited by 161 · see citing works
Recent Advances in Pyrimidine-Based Drugs
Nammalwar, B., & Bunce, R. A. (2024) · Pharmaceuticals · doi:10.3390/ph17010104 · Cited by 168 · see citing works
The Overcrowded Crossroads: Mitochondria, Alpha-Synuclein, and the Endo-Lysosomal System Interaction in Parkinson’s Disease
Lin, K.-J., Lin, K.-L., Chen, S., Liou, C., Chuang, Y., Lin, H., & Lin, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215312 · Cited by 141 · see citing works
Zebrafish as a model organism for neurodegenerative disease
Chia, K., Klingseisen, A., Sieger, D., & Priller, J. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.940484 · Cited by 134 · see citing works
Blood–brain barrier: emerging trends on transport models and new-age strategies for therapeutics intervention against neurological disorders
Alajangi, H. K., Kaur, M., Sharma, A., Rana, S., Thakur, S., Chatterjee, M., Singla, N., Jaiswal, P. K., Singh, G., & Barnwal, R. P. (2022) · Molecular Brain · doi:10.1186/s13041-022-00937-4 · Cited by 130 · see citing works
Early Life Stress, Depression And Parkinson’s Disease: A New Approach
Dallé, E., & Mabandla, M. V. (2018) · Molecular Brain · doi:10.1186/s13041-018-0356-9 · Cited by 124 · see citing works
Mitophagy and reactive oxygen species interplay in Parkinson’s disease
Xiao, B., Kuruvilla, J., & Tan, E. (2022) · npj Parkinson s Disease · doi:10.1038/s41531-022-00402-y · Cited by 112 · see citing works
The associations between Parkinson’s disease and cancer: the plot thickens
Feng, D. D., Cai, W., & Chen, X. M. (2015) · Translational Neurodegeneration · doi:10.1186/s40035-015-0043-z · Cited by 103 · see citing works
Autophagy in Parkinson’s Disease
Nechushtai, L., Frenkel, D., & Pinkas‐Kramarski, R. (2023) · Biomolecules · doi:10.3390/biom13101435 · Cited by 107 · see citing works
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Authors: Li, J.-Q., Tan, L., & Yu, J.-T.
Affiliations: Qingdao University (CN)
Corresponding author: Tan, Lan
Yu, Jin-Tai
ORCID: Tan, Lan
Yu, Jin-Tai
Venue: Molecular Neurodegeneration
Publisher: Springer Science and Business Media LLC
Published: 2014-11-12
Volume: 9
Issue: 1
Pages: 47-47
ISSN: 1750-1326 (ISSN-L)
DOI: 10.1186/1750-1326-9-47
PMC: PMC4246469
OpenAlex: W2145005920
Cited by: 249
References: 127
Citations by year: 2026: 9 · 2025: 18 · 2024: 24 · 2023: 29 · 2022: 27 · 2021: 15 · 2020: 28 · 2019: 30 · 2018: 30 · 2017: 17 · 2016: 12 · 2015: 10
FWCI: 1.79
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
Locations: Molecular Neurodegeneration (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Natural Science Foundation of China (81371406, ZR2011HZ001, 81171209, 81471309, ZR2010HQ004)
Natural Science Foundation of Shandong Province (ZR2011HZ001, ZR2010HQ004)
Topics: Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nuclear Receptors and Signaling
Health Sciences › Medicine › Neurology › Neurological disorders and treatments
Keywords: LRRK2, Parkinson's disease, leucine-rich repeat kinase 2, LRRK2 mutations, alpha-synuclein, tau protein, neuroinflammation, oxidative stress, mitochondrial dysfunction, synaptic dysfunction, autophagy-lysosome pathway, therapeutic target
MeSH terms: Leucine-Rich Repeat Serine-Threonine Protein Kinase-2, Animals, Humans, Protein Serine-Threonine Kinases, Parkinsonian Disorders

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The role of the LRRK2 gene in Parkinsonism

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