Cited by 525Parkinson's Disease Mechanisms and TreatmentsAutophagy in Disease and TherapyNuclear Receptors and Signaling

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Mitochondrial dysfunction and mitophagy in Parkinson's: from familial to sporadic disease

Ryan, Brent J., Hoek, Selim, Fon, Edward A., Wade-Martins, Richard·2015·Trends in Biochemical Sciences

DOI 10.1016/j.tibs.2015.02.003

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Abstract

Parkinson's disease (PD) is a progressive neurodegenerative disorder characterised by the preferential loss of dopaminergic neurons in the substantia nigra. Mitochondrial dysfunction is increasingly appreciated as a key determinant of dopaminergic neuronal susceptibility in PD and is a feature of both familial and sporadic disease, as well as in toxin-induced Parkinsonism. Recently, the mechanisms by which PD-associated mitochondrial proteins phosphatase and tensin homolog deleted on chromosome 10 (PTEN)-induced putative kinase 1 (PINK1) and parkin function and induce neurodegeneration have been identified. In addition, increasing evidence implicates other PD-associated proteins such as α-synuclein (α-syn) and leucine-rich repeat kinase 2 (LRRK2) in mitochondrial dysfunction in genetic cases of PD with the potential for a large functional overlap with sporadic disease. This review highlights how recent advances in understanding familial PD-associated proteins have identified novel mechanisms and therapeutic strategies for addressing mitochondrial dysfunction in PD.

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Bender, A., Desplats, P., Spencer, B. J., Rockenstein, E. M., Adame, A., Elstner, M., Laub, C., Mueller, S. K., Koob, A. O., Mante, M., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062277 · Cited by 151
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PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
Geisler, S., Holmström, K. M., Skujat, D., Fiesel, F. C., Rothfuss, O. C., Kahle, P. J., & Springer, W. (2010) · Nature Cell Biology · doi:10.1038/ncb2012 · Cited by 2,835
Pathological α-Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice
Luk, K. C., Kehm, V., Carroll, J., Zhang, B., O’Brien, P., Trojanowski, J. Q., & Lee, V. M.-Y. (2012) · Science · doi:10.1126/science.1227157 · Cited by 2,563
ER Tubules Mark Sites of Mitochondrial Division
Friedman, J. R., Lackner, L. L., West, M., DiBenedetto, J. R., Nunnari, J., & Voeltz, G. K. (2011) · Science · doi:10.1126/science.1207385 · Cited by 2,072
PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
Matsuda, N., Sato, S., Shiba, K., Okatsu, K., Saisho, K., Gautier, C. A., Sou, Y.-S., Saiki, S., Kawajiri, S., Sato, F., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200910140 · Cited by 1,969
Large-scale meta-analysis of genome-wide association data identifies six new risk loci for Parkinson’s disease
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
MITOCHONDRIAL COMPLEX I DEFICIENCY IN PARKINSON'S DISEASE
Schapira, A. H. V., Cooper, J. A. D., Dexter, D. T., Jenner, P. G., Clark, J. B., & MARSDEN, C. D. (1989) · The Lancet · doi:10.1016/s0140-6736(89)92366-0 · Cited by 1,757
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Hamasaki, M., Furuta, N., Matsuda, A., Nezu, A., Yamamoto, A., Fujita, N., Oomori, H., Noda, T., Haraguchi, T., Hiraoka, Y., et al. (2013) · Nature · doi:10.1038/nature11910 · Cited by 1,683
Ubiquitin is phosphorylated by PINK1 to activate parkin
Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., et al. (2014) · Nature · doi:10.1038/nature13392 · Cited by 1,477
Self-citation
PINK1-Phosphorylated Mitofusin 2 Is a Parkin Receptor for Culling Damaged Mitochondria
Chen, Y., & Dorn, G. W. (2013) · Science · doi:10.1126/science.1231031 · Cited by 1,323

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Authors: Ryan, B. J., Hoek, S., Fon, E. A., & Wade-Martins, R.
Affiliations: University of Oxford (GB)
Montreal Neurological Institute and Hospital (CA)
ORCID: Ryan, Brent J.
Fon, Edward A.
Venue: Trends in Biochemical Sciences
Publisher: Elsevier BV
Published: 2015-04
Volume: 40
Issue: 4
Pages: 200-210
ISSN: 0968-0004 (ISSN-L)
DOI: 10.1016/j.tibs.2015.02.003
OpenAlex: W2021439462
Cited by: 524
References: 115
Citations by year: 2026: 25 · 2025: 30 · 2024: 37 · 2023: 28 · 2022: 45 · 2021: 65 · 2020: 56 · 2019: 50 · 2018: 63 · 2017: 53 · 2016: 52 · 2015: 20
FWCI: 8.25
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Biochemical Sciences (publishedVersion)
PubMed (publishedVersion)
Funders: Parkinson's UK (J-0901)
Canadian Institutes of Health Research
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 › Molecular Biology › Nuclear Receptors and Signaling
Keywords: Parkinson's disease, mitochondrial dysfunction, mitophagy, PINK1, Parkin, alpha-synuclein, LRRK2, dopaminergic neurons, familial Parkinson's disease, sporadic Parkinson's disease, neurodegeneration, treatment options
MeSH terms: Animals, Humans, Mitochondria, Parkinson Disease, alpha-Synuclein

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Mitochondrial dysfunction and mitophagy in Parkinson's: from familial to sporadic disease

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