Cited by 323Parkinson's Disease Mechanisms and TreatmentsAutophagy in Disease and TherapyCellular transport and secretion

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Synaptic, Mitochondrial, and Lysosomal Dysfunction in Parkinson’s Disease

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Nguyen, Maria, Wong, Yvette C., Ysselstein, Daniel, Severino, Alex, Krainc, Dimitri·2019·Trends in Neurosciences

DOI 10.1016/j.tins.2018.11.001PMC PMC6452863

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Abstract

The discovery of genetic forms of Parkinson's disease (PD) has highlighted the importance of the autophagy/lysosomal and mitochondrial/oxidative stress pathways in disease pathogenesis. However, recently identified PD-linked genes, including DNAJC6 (auxilin), SYNJ1 (synaptojanin 1), and the PD risk gene SH3GL2 (endophilin A1), have also highlighted disruptions in synaptic vesicle endocytosis (SVE) as a significant contributor to disease pathogenesis. Additionally, the roles of other PD genes such as LRRK2, PRKN, and VPS35 in the regulation of SVE are beginning to emerge. Here we discuss the recent work on the contribution of dysfunctional SVE to midbrain dopaminergic neurons' selective vulnerability and highlight pathways that demonstrate the interplay of synaptic, mitochondrial, and lysosomal dysfunction in the pathogenesis of PD.

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Poewe, W., Seppi, K., Tanner, C. M., Halliday, G. M., Brundin, P., Volkmann, J., Schrag, A.-E., & Lang, A. E. (2017) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2017.13 · Cited by 5,415
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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
The Role of Oxidative Stress in Parkinson's Disease
Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845
A meta-analysis of genome-wide association studies identifies 17 new Parkinson's disease risk loci
Chang, D., Nalls, M. A., Hallgrímsdóttir, I. B., Hunkapiller, J., van der Brug, M., Cai, F., International Parkinson's Disease Genomics Consortium, 23andMe Research Team, Kerchner, G. A., Ayalon, G., et al. (2017) · Nature Genetics · doi:10.1038/ng.3955 · Cited by 1,112
Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases
Steger, M., Tonelli, F., Ito, G., Davies, P., Trost, M., Vetter, M., Wachter, S., Lorentzen, E., Duddy, G., Wilson, S., et al. (2016) · eLife · doi:10.7554/elife.12813 · Cited by 1,042
Mitochondria–lysosome contacts regulate mitochondrial fission via RAB7 GTP hydrolysis
Wong, Y. C., Ysselstein, D., & Krainc, D. (2018) · Nature · doi:10.1038/nature25486 · Cited by 911
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Burbulla, L. F., Song, P., Mazzulli, J. R., Zampese, E., Wong, Y. C., Jeon, S., Santos, D. P., Blanz, J., Obermaier, C. D., Strojny, C., et al. (2017) · Science · doi:10.1126/science.aam9080 · Cited by 874
Self-citation
Activity-driven local ATP synthesis is required for synaptic function
Rangaraju, V., Calloway, N., & Ryan, T. A. (2014) · Cell · doi:10.1016/j.cell.2013.12.042 · Cited by 836
Complexity of dopamine metabolism
Meiser, J., Weindl, D., & Hiller, K. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-34 · Cited by 726
Elevated Mitochondrial Bioenergetics and Axonal Arborization Size Are Key Contributors to the Vulnerability of Dopamine Neurons
Pacelli, C., Giguère, N., Bourque, M.-J., Lévesque, M., Slack, R. S., & Trudeau, L. (2015) · Current Biology · doi:10.1016/j.cub.2015.07.050 · Cited by 530

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Iba, M., Kim, C., Kwon, S., Szabo, M. P., Horan-Portelance, L., Peer, C. J., Figg, W. D., Reed, X., Ding, J., Lee, S., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abq6089 · Cited by 42
Inflammasomes in neurodegenerative diseases
Wang, Q., Yang, S., Zhang, X., Zhang, S., Chen, L., Wang, W., Chen, N., & Yan, J. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00459-0 · Cited by 47
Focused ultrasound in Parkinson's disease: A twofold path toward disease modification
Foffani, G., Trigo‐Damas, I., Pineda‐Pardo, J. A., Blesa, J., Rodríguez‐Rojas, R., Martínez‐Fernández, R., & Obeso, J. A. (2019) · Movement Disorders · doi:10.1002/mds.27805 · Cited by 45
Lysosomal cholesterol accumulation contributes to the movement phenotypes associated with NUS1 haploinsufficiency
Yu, S., Wang, T., Wiggins, K., Louie, R. J., Merino, E. F., Skinner, C. D., Cassera, M. B., Meagher, K., Goldberg, P., Rismanchi, N., et al. (2021) · Genetics in Medicine · doi:10.1038/s41436-021-01137-6 · Cited by 41
RNA-sequencing of peripheral blood circular RNAs in Parkinson disease
Kong, F., Lv, Z., Wang, L., Zhang, K., Cai, Y., Ding, Q., Sun, Z., Zhen, H., Jiao, F., Ma, Q., et al. (2021) · Medicine · doi:10.1097/md.0000000000025888 · Cited by 40
Dopaminergic Vulnerability in Parkinson Disease: The Cost of Humans’ Habitual Performance
Hernández, L. F., Obeso, I., Costa, R. M., Redgrave, P., & Obeso, J. A. (2019) · Trends in Neurosciences · doi:10.1016/j.tins.2019.03.007 · Cited by 40
Organoid and pluripotent stem cells in Parkinson’s disease modeling: an expert view on their value to drug discovery
Marotta, N., Kim, S., & Krainc, D. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1703671 · Cited by 40
Self-citation
β2-adrenergic Agonists Rescue Lysosome Acidification and Function in PSEN1 Deficiency by Reversing Defective ER-to-lysosome Delivery of ClC-7
Lee, J., Wolfe, D. M., Darji, S., McBrayer, M. K., Colacurcio, D. J., Kumar, A. R., Stavrides, P. H., Mohan, P. S., & Nixon, R. A. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.02.021 · Cited by 39
Rosmarinic acid relieves LPS-induced sickness and depressive-like behaviors in mice by activating the BDNF/Nrf2 signaling and autophagy pathway
Yu, Y., Li, Y., Qi, K., Xu, W., & Wei, Y. (2022) · Behavioural Brain Research · doi:10.1016/j.bbr.2022.114006 · Cited by 40
Dopaminergic Axons: Key Recitalists in Parkinson’s Disease
Mishra, A. K., & Dixit, A. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03464-1 · Cited by 37
The function of prohibitins in mitochondria and the clinical potentials
Oyang, L., Li, J., Jiang, X., Lin, J., Xia, L., Yang, L., Tan, S., Wu, N., Han, Y., Yang, Y., et al. (2022) · Cancer Cell International · doi:10.1186/s12935-022-02765-x · Cited by 38
Hypoxia and Alpha-Synuclein: Inextricable Link Underlying the Pathologic Progression of Parkinson's Disease
Guo, M., Ji, X., & Liu, J. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.919343 · Cited by 40
Are neurodegenerative diseases associated with an increased risk of inflammatory bowel disease? A two-sample Mendelian randomization study
Cui, G., Li, S., Ye, H., Yang, Y., Huang, Q., Chu, Y., Shi, Z., & Zhang, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.956005 · Cited by 40
Glia-derived extracellular vesicles in parkinson’s disease.
Marchetti, B., Leggio, L., L’Episcopo, F., Vivarelli, S., Tirolo, C., Paternò, G., Giachino, C., Caniglia, S., Serapide, M. F., & Iraci, N. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9061941 · Cited by 38
The Renin–Angiotensin System Modulates Dopaminergic Neurotransmission: A New Player on the Scene
Kobiec, T., Losada, M. E. O., Chevalier, G., Udovin, L., Bordet, S., Maissonave, C. M., Capani, F., & Perez‐Lloret, S. (2021) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2021.638519 · Cited by 38
Brain energetics, mitochondria, and traumatic brain injury
Benaroya, H. (2020) · Reviews in the Neurosciences · doi:10.1515/revneuro-2019-0086 · Cited by 37
A Critical LRRK at the Synapse? The Neurobiological Function and Pathophysiological Dysfunction of LRRK2
Kuhlmann, N., & Milnerwood, A. J. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00153 · Cited by 37
5-S-cysteinyl-dopamine, a neurotoxic endogenous metabolite of dopamine: Implications for Parkinson's disease
Badillo‐Ramírez, I., Saniger, J. M., & Rivas-Arancibia, S. (2019) · Neurochemistry International · doi:10.1016/j.neuint.2019.104514 · Cited by 36
A primate nigrostriatal atlas of neuronal vulnerability and resilience in a model of Parkinson’s disease
Tang, L., Xu, N., Huang, M., Yi, W., Sang, X., Shao, M., Li, Y., Hao, Z.-Z., Liu, R., Shen, Y., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43213-2 · Cited by 41
ACO2 deficiency increases vulnerability to Parkinson’s disease via dysregulating mitochondrial function and histone acetylation-mediated transcription of autophagy genes
Zhu, J., Xu, F., Lai, H., Yuan, H., Li, X., Hu, J., Li, W., Liu, L., & Wang, C. (2023) · Communications Biology · doi:10.1038/s42003-023-05570-y · Cited by 33
Modeling Parkinson’s Disease Using Induced Pluripotent Stem Cells
Hu, X., Mao, C., Fan, L., Luo, H., Hu, Z., Zhang, S., Yang, Z., Zheng, H., Sun, H., Fan, Y., et al. (2020) · Stem Cells International · doi:10.1155/2020/1061470 · Cited by 36
Boosting Antioxidant Self-defenses by Grafting Astrocytes Rejuvenates the Aged Microenvironment and Mitigates Nigrostriatal Toxicity in Parkinsonian Brain via an Nrf2-Driven Wnt/β-Catenin Prosurvival Axis
Serapide, M. F., L’Episcopo, F., Tirolo, C., Testa, N., Caniglia, S., Giachino, C., & Marchetti, B. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00024 · Cited by 32
TREM2 and Microglia Contribute to the Synaptic Plasticity: from Physiology to Pathology
Yu, C.-J., Wang, M., Ruiyang, L., Wei, T., Yang, H.-C., Yin, Y., Mi, Y., Qin, Q., & Tang, Y. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03100-1 · Cited by 34
PDZD-8 and TEX-2 regulate endosomal PI(4,5)P2 homeostasis via lipid transport to promote embryogenesis in C. elegans
Jeyasimman, D., Ercan, B., Dharmawan, D., Naito, T., Sun, J., & Saheki, Y. (2021) · Nature Communications · doi:10.1038/s41467-021-26177-z · Cited by 30
Hippocampal synaptic failure is an early event in experimental parkinsonism with subtle cognitive deficit
Belloso-Iguerategui, A., Zamarbide, M., Merino-Galán, L., Rodríguez-Chinchilla, T., Gago, B., Santamaría, E., Fernández‐Irigoyen, J., Cotman, C. W., Prieto, G. A., Quiroga‐Varela, A., et al. (2023) · Brain · doi:10.1093/brain/awad227 · Cited by 33
VPS13C regulates phospho-Rab10-mediated lysosomal function in human dopaminergic neurons
Schröder, L. F., Peng, W., Gao, G., Wong, Y. C., Schwake, M., & Krainc, D. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202304042 · Cited by 30
Self-citation
Parkinson’s disease therapy: what lies ahead?
Wolff, A. W., Schumacher, N. U., Pürner, D., Machetanz, G., Demleitner, A. F., Feneberg, E., Hagemeier, M., & Lingor, P. (2023) · Journal of Neural Transmission · doi:10.1007/s00702-023-02641-6 · Cited by 36
Dysfunction of synaptic endocytic trafficking in Parkinson’s disease
Ng, X. Y., & Cao, M. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01624 · Cited by 31
Endosomal sorting pathways in the pathogenesis of Parkinson's disease
(2020) · Progress in Brain Research · doi:10.1016/bs.pbr.2020.02.001 · Cited by 25
Patient-Derived Induced Pluripotent Stem Cell-Based Models in Parkinson’s Disease for Drug Identification
Kouroupi, G., Antoniou, N., Prodromidou, K., Taoufik, E., & Matsas, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197113 · Cited by 30

Authors: Nguyen, M., Wong, Y. C., Ysselstein, D., Severino, A., & Krainc, D.
Affiliations: Northwestern University (US)
Corresponding author: Krainc, Dimitri
ORCID: Wong, Yvette C.
Ysselstein, Daniel
Severino, Alex
Krainc, Dimitri
Venue: Trends in Neurosciences
Publisher: Elsevier BV
Published: 2019-02
Volume: 42
Issue: 2
Pages: 140-149
ISSN: 0166-2236 (ISSN-L)
DOI: 10.1016/j.tins.2018.11.001
PMC: PMC6452863
OpenAlex: W2903418495
Cited by: 323
References: 89
Citations by year: 2026: 25 · 2025: 38 · 2024: 53 · 2023: 42 · 2022: 45 · 2021: 57 · 2020: 45 · 2019: 18
FWCI: 4.73
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Trends in Neurosciences (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: NIH (2T32AG020506-16, K99 NS109252, T32 NS041234, R01 NS076054, R37 NS096241)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: Parkinson's disease, synaptic vesicle endocytosis, mitochondrial dysfunction, oxidative stress, DNAJC6, auxilin, SYNJ1, SH3GL2, endophilin A1, LRRK2, Parkin, VPS35, midbrain dopaminergic neurons, selective neuronal vulnerability, risk genes
MeSH terms: Leucine-Rich Repeat Serine-Threonine Protein Kinase-2, Animals, Autophagy, Dopamine, Endocytosis, Humans, Lysosomes, Mitochondria, Parkinson Disease, Synaptic Vesicles, Oxidative Stress, Genetic Predisposition to Disease, alpha-Synuclein, Dopaminergic Neurons

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Synaptic, Mitochondrial, and Lysosomal Dysfunction in Parkinson’s Disease

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