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

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

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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

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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

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Autophagosomes form at ER–mitochondria contact sites

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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

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

PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity

Kane, L. A., Lazarou, M., Fogel, A. I., Li, Y., Yamano, K., Sarraf, S. A., Banerjee, S., & Youle, R. J. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201402104 · Cited by 1,298

PINK1 and Parkin Target Miro for Phosphorylation and Degradation to Arrest Mitochondrial Motility

Wang, X., Winter, D., Ashrafi, G., Schlehe, J. S., Wong, Y. L., Selkoe, D. J., Rice, S. E., Steen, J. A. J., LaVoie, M. J., & Schwarz, T. L. (2011) · Cell · doi:10.1016/j.cell.2011.10.018 · Cited by 1,198

The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization

Canet-Aviles, R., Wilson, M. A., Miller, D. W., Ahmad, R., McLendon, C., Bandyopadhyay, S., Baptista, M. J., Ringe, D., Petsko, G. A., & Cookson, M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402959101 · Cited by 1,115

Cardiolipin externalization to the outer mitochondrial membrane acts as an elimination signal for mitophagy in neuronal cells

Chu, C. T., Ji, J., Dagda, R. K., Jiang, J. F., Tyurina, Y. Y., Kapralov, A. A., Tyurin, V. A., Yanamala, N., Shrivastava, I. H., Mohammadyani, D., et al. (2013) · Nature Cell Biology · doi:10.1038/ncb2837 · Cited by 1,083

Mitochondrial superoxide: production, biological effects, and activation of uncoupling proteins

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Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization

Sarraf, S. A., Raman, M., Guarani-Pereira, V., Sowa, M. E., Huttlin, E. L., Gygi, S. P., & Harper, J. W. (2013) · Nature · doi:10.1038/nature12043 · Cited by 1,010

‘Rejuvenation’ protects neurons in mouse models of Parkinson’s disease

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Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1

Guzmán, J. N., Sánchez-Padilla, J., Wokosin, D. L., Kondapalli, J., Ilijić, E., Schumacker, P. T., & Surmeier, D. J. (2010) · Nature · doi:10.1038/nature09536 · Cited by 864

Neuron-released oligomeric α-synuclein is an endogenous agonist of TLR2 for paracrine activation of microglia

Kim, C., Ho, D.-H., Suk, J.-E., You, S., Michael, S., Kang, J., Joong Lee, S., Masliah, E., Hwang, D., Lee, H.-J., et al. (2013) · Nature Communications · doi:10.1038/ncomms2534 · Cited by 856

α-Synuclein propagates from mouse brain to grafted dopaminergic neurons and seeds aggregation in cultured human cells

Hansen, C., Angot, E., Bergström, A.-L., Steiner, J. A., Pieri, L., Paul, G., Outeiro, T. F., Melki, R., Kallunki, P., Fog, K., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43366 · Cited by 842

Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65

Kazlauskaite, A., Kondapalli, C., Gourlay, R., Campbell, D. G., Ritorto, M. S., Hofmann, K., Alessi, D. R., Knebel, A., Trost, M., & Muqit, M. M. K. (2014) · Biochemical Journal · doi:10.1042/bj20140334 · Cited by 806

LRRK2 Mutant iPSC-Derived DA Neurons Demonstrate Increased Susceptibility to Oxidative Stress

Nguyen, H. N., Byers, B., Cord, B. J., Shcheglovitov, A., Byrne, J., Gujar, P., Kee, K., Schüle, B., Dolmetsch, R. E., Langston, J. W., et al. (2011) · Cell stem cell · doi:10.1016/j.stem.2011.01.013 · Cited by 767

A Vesicular Transport Pathway Shuttles Cargo from Mitochondria to Lysosomes

Soubannier, V., McLelland, G., Zunino, R., Braschi, E., Rippstein, P. U., Fon, E. A., & McBride, H. M. (2012) · Current Biology · doi:10.1016/j.cub.2011.11.057 · Cited by 755

Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control

McLelland, G., Soubannier, V., Chen, C. X., McBride, H. M., & Fon, E. A. (2014) · The EMBO Journal · doi:10.1002/embj.201385902 · Cited by 743

Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis

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Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment

Greene, A. W., Grenier, K., Aguileta, M. A., Muise, S., Farazifard, R., Haque, M. E., McBride, H. M., Park, D. S., & Fon, E. A. (2012) · The EMBO Reports · doi:10.1038/embor.2012.14 · Cited by 711

Alpha‐synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease

Appel‐Cresswell, S., Vilariño‐Güell, C., Encarnacion, M. J., Sherman, H. E., Yu, I. S., Shah, B., Weir, D., Thompson, C., Szu‐Tu, C., Trinh, J., et al. (2013) · Movement Disorders · doi:10.1002/mds.25421 · Cited by 685

PINK1-associated Parkinson's disease is caused by neuronal vulnerability to calcium-induced cell death

Gandhi, S., Wood-Kaczmar, A., Yao, Z., Plun-Favreau, H., Deas, E., Klupsch, K., Downward, J., Latchman, D. S., Tabrizi, S. J., Wood, N. W., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.013 · Cited by 682

MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond

Vance, J. E. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.11.014 · Cited by 625

PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria

Okatsu, K., Oka, T., Iguchi, M., Imamura, K., Kosako, H., Tani, N., Kimura, M., Go, E., Koyano, F., Funayama, M., et al. (2012) · Nature Communications · doi:10.1038/ncomms2016 · Cited by 624

Kinase activity of mutant LRRK2 mediates neuronal toxicity

Smith, W. W., Pei, Z., Jiang, H., Dawson, V. L., Dawson, T. M., & Ross, C. A. (2006) · Nature Neuroscience · doi:10.1038/nn1776 · Cited by 619

A double‐blind, placebo‐controlled study to assess the mitochondria‐targeted antioxidant MitoQ as a disease‐modifying therapy in Parkinson's disease

Snow, B. J., Rolfe, F. L., Lockhart, M. M., Frampton, C. M., O'Sullivan, J. D., Fung, V., Smith, R. A. J., Murphy, M. P., Taylor, K. M., & On behalf of the Protect Study Group (2010) · Movement Disorders · doi:10.1002/mds.23148 · Cited by 606

Interplay of LRRK2 with chaperone-mediated autophagy

Orenstein, S. J., Kuo, S.-H., Tasset, I., Arias, E., Koga, H., Fernandez-Carasa, I., Cortes, E., Honig, L. S., Dauer, W., Consiglio, A., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3350 · Cited by 588

Disease‐specific phenotypes in dopamine neurons from human iPS‐based models of genetic and sporadic Parkinson's disease

Sánchez‐Danés, A., Richaud‐Patín, Y., Carballo‐Carbajal, I., Jiménez‐Delgado, S., Caig, C., Mora, S., Guglielmo, C. D., Ezquerra, M., Patel, B., Giralt, A., et al. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201200215 · Cited by 571

Dynamic regulation of mitochondrial fission through modification of the dynamin‐related protein Drp1

Chang, C., & Blackstone, C. D. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05629.x · Cited by 570

Structure of Parkin Reveals Mechanisms for Ubiquitin Ligase Activation

Trempe, J.-F., Sauvé, V., Grenier, K., Seirafi, M., Tang, M. Y., Ménade, M., Al-Abdul-Wahid, S., Krett, J., Wong, K., Kozlov, G., et al. (2013) · Science · doi:10.1126/science.1237908 · Cited by 523

α-Synuclein Is Localized to Mitochondria-Associated ER Membranes

Guardia-Laguarta, C., Area-Gomez, E., Rüb, C., Liu, Y., Magrané, J., Becker, D., Voos, W., Schon, E. A., & Przedborski, S. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.2507-13.2014 · Cited by 515

Genetic Correction of a LRRK2 Mutation in Human iPSCs Links Parkinsonian Neurodegeneration to ERK-Dependent Changes in Gene Expression

Reinhardt, P., Schmid, B., Burbulla, L. F., Schöndorf, D. C., Wagner, L., Glatza, M., Höing, S., Hargus, G., Heck, S. A., Dhingra, A., et al. (2013) · Cell stem cell · doi:10.1016/j.stem.2013.01.008 · Cited by 512

Pharmacological rescue of mitochondrial deficits in iPSC-derived neural cells from patients with familial Parkinson’s disease

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Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin

Ashrafi, G., Schlehe, J. S., LaVoie, M. J., & Schwarz, T. L. (2014) · Journal of Cell Biology · doi:10.1083/jcb.201401070 · Cited by 502

PINK1 cleavage at position A103 by the mitochondrial protease PARL

Deas, E., Plun‐Favreau, H., Gandhi, S., Desmond, H., Kjaer, S., Loh, S. H. Y., Renton, A. E., Harvey, R. J., Whitworth, A. J., Martins, L. M., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq526 · Cited by 501

Parkinson's disease mutations in PINK1 result in decreased Complex I activity and deficient synaptic function

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Isogenic Human iPSC Parkinson’s Model Shows Nitrosative Stress-Induced Dysfunction in MEF2-PGC1α Transcription

Ryan, S. D., Dolatabadi, N., Chan, S. F., Zhang, X., Akhtar, M. W., Parker, J., Soldner, F., Sunico, C. R., Nagar, S., Talantova, M. V., et al. (2013) · Cell · doi:10.1016/j.cell.2013.11.009 · Cited by 445

Living on the edge with too many mouths to feed: Why dopamine neurons die

Bolam, J. P., & Pissadaki, E. K. (2012) · Movement Disorders · doi:10.1002/mds.25135 · Cited by 439

LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1

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The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria

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A Randomized Clinical Trial of High-Dosage Coenzyme Q10 in Early Parkinson Disease

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Parkin Ubiquitinates Drp1 for Proteasome-dependent Degradation

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PINK1 Loss-of-Function Mutations Affect Mitochondrial Complex I Activity via NdufA10 Ubiquinone Uncoupling

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Parkinson's Disease–Associated Kinase PINK1 Regulates Miro Protein Level and Axonal Transport of Mitochondria

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Vitamin K 2 Is a Mitochondrial Electron Carrier That Rescues Pink1 Deficiency

Vos, M. H., Esposito, G., Edirisinghe, J. N., Vilain, S., Haddad, D., Slabbaert, J. R., Meensel, S. V., Schaap, O., Strooper, B. D., Meganathan, R., et al. (2012) · Science · doi:10.1126/science.1218632 · Cited by 366

The energy cost of action potential propagation in dopamine neurons: clues to susceptibility in Parkinson's disease

Pissadaki, E. K., & Bolam, J. P. (2013) · Frontiers in Computational Neuroscience · doi:10.3389/fncom.2013.00013 · Cited by 349

Reconstitution of Mitochondria Derived Vesicle Formation Demonstrates Selective Enrichment of Oxidized Cargo

Soubannier, V., Rippstein, P. U., Kaufman, B. A., Shoubridge, E. A., & McBride, H. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052830 · Cited by 346

Deficits in dopaminergic transmission precede neuron loss and dysfunction in a new Parkinson model

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α-Synuclein Immunotherapy Blocks Uptake and Templated Propagation of Misfolded α-Synuclein and Neurodegeneration

Tran, H., Chung, C. H.-Y., Iba, M., Zhang, B., Trojanowski, J. Q., Luk, K. C., & Lee, V. M. ‐. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.033 · Cited by 334

Soluble, Prefibrillar α-Synuclein Oligomers Promote Complex I-dependent, Ca2+-induced Mitochondrial Dysfunction

Luth, E. S., Stavrovskaya, I. G., Bartels, T., Kristal, B. S., & Selkoe, D. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.545749 · Cited by 296

A neo-substrate that amplifies catalytic activity of Parkinson's-disease-related kinase PINK1

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Identification and Characterization of Cholest-4-en-3-one, Oxime (TRO19622), a Novel Drug Candidate for Amyotrophic Lateral Sclerosis

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Human DJ-1 and its homologs are novel glyoxalases

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Dysregulation of glucose metabolism is an early event in sporadic Parkinson's disease

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Calcium, Bioenergetics, and Neuronal Vulnerability in Parkinson's Disease

Surmeier, D. J., & Schumacker, P. T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r112.410530 · Cited by 240

Inhibition of excessive mitochondrial fission reduced aberrant autophagy and neuronal damage caused by LRRK2 G2019S mutation

Su, Y.-C., & Qi, X. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt301 · Cited by 231

Alpha-synuclein Post-translational Modifications as Potential Biomarkers for Parkinson Disease and Other Synucleinopathies

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Impaired intracellular trafficking defines early Parkinson's disease

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Neuronal vulnerability in Parkinson’s disease

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Mitochondrial DNA damage: Molecular marker of vulnerable nigral neurons in Parkinson's disease

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Mitochondrial translocation of α-synuclein is promoted by intracellular acidification

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The H50Q Mutation Enhances α-Synuclein Aggregation, Secretion, and Toxicity

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The LRRK2 G2019S mutant exacerbates basal autophagy through activation of the MEK/ERK pathway

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G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization

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Leucine‐rich repeat kinase 2 disturbs mitochondrial dynamics via Dynamin‐like protein

Niu, J., Yu, M., Wang, C., & Xu, Z. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07809.x · Cited by 166

DJ-1 interactions with α-synuclein attenuate aggregation and cellular toxicity in models of Parkinson’s disease

Zondler, L., Miller‐Fleming, L., Repici, M., Gonçalves, S. A., Tenreiro, S., Rosado-Ramos, R., Betzer, C., Straatman, K. R., Jensen, P. H., Giorgini, F., et al. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.307 · Cited by 161

The TOMM machinery is a molecular switch in PINK1 and PARK2/PARKIN-dependent mitochondrial clearance

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Enhancing nucleotide metabolism protects against mitochondrial dysfunction and neurodegeneration in a PINK1 model of Parkinson’s disease

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Functional interaction of Parkinson's disease-associated LRRK2 with members of the dynamin GTPase superfamily

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Structure and Function of Parkin, PINK1, and DJ-1, the Three Musketeers of Neuroprotection

Trempe, J., & Fon, E. A. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00038 · Cited by 136

Cytosolic cleaved PINK1 represses Parkin translocation to mitochondria and mitophagy

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Drosophila Trap1 protects against mitochondrial dysfunction in a PINK1/parkin model of Parkinson’s disease

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Ursocholanic acid rescues mitochondrial function in common forms of familial Parkinson’s disease

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Region specific mitochondrial impairment in mice with widespread overexpression of alpha-synuclein

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