Cited by 1,203Parkinson's Disease Mechanisms and TreatmentsMitochondrial Function and PathologyNuclear Receptors and Signaling

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Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants

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Greene, Jessica C., Whitworth, Alexander J., Kuo, Isabella, Andrews, Laurie A., Feany, Mel B., Pallanck, Leo J.·2003·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0737556100PMC PMC153051

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Abstract

Parkinson's disease (PD) is a common neurodegenerative disorder characterized by loss of dopaminergic neurons in the substantia nigra. Several lines of evidence strongly implicate mitochondrial dysfunction as a major causative factor in PD, although the molecular mechanisms responsible for mitochondrial dysfunction are poorly understood. Recently, loss-of-function mutations in the parkin gene, which encodes a ubiquitin-protein ligase, were found to underlie a familial form of PD known as autosomal recessive juvenile parkinsonism (AR-JP). To gain insight into the molecular mechanism responsible for selective cell death in AR-JP, we have created a Drosophila model of this disorder. Drosophila parkin null mutants exhibit reduced lifespan, locomotor defects, and male sterility. The locomotor defects derive from apoptotic cell death of muscle subsets, whereas the male sterile phenotype derives from a spermatid individualization defect at a late stage of spermatogenesis. Mitochondrial pathology is the earliest manifestation of muscle degeneration and a prominent characteristic of individualizing spermatids in parkin mutants. These results indicate that the tissue-specific phenotypes observed in Drosophila parkin mutants result from mitochondrial dysfunction and raise the possibility that similar mitochondrial impairment triggers the selective cell loss observed in AR-JP.

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Brand, A. H., & Perrimon, N. (1993) · Development · doi:10.1242/dev.118.2.401 · Cited by 9,510
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
Kitada, T., Asakawa, S., Hattori, N., Matsumine, H., Yamamura, Y., Minoshima, S., Yokochi, M., Mizuno, Y., & Shimizu, N. (1998) · Nature · doi:10.1038/33416 · Cited by 5,227
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Betarbet, R. S., Sherer, T., MacKenzie, G. M., Garcia‐Osuna, M., Panov, A. V., & Greenamyre, J. T. (2000) · Nature Neuroscience · doi:10.1038/81834 · Cited by 3,770
Mitochondrial Complex I Deficiency in Parkinson's Disease
Schapira, A. H. V., Cooper, J. M., Dexter, D., Clark, J. B., Jenner, P., & Marsden, C. D. (1990) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1990.tb02325.x · Cited by 2,283
A Drosophila model of Parkinson's disease
Feany, M. Β., & Bender, W. W. (2000) · Nature · doi:10.1038/35006074 · Cited by 2,156
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Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
Shimura, H., Hattori, N., Kubo, S.-I., Mizuno, Y., Asakawa, S., Minoshima, S., Shimizu, N., Iwai, K., Chiba, T., Tanaka, K., et al. (2000) · Nature Genetics · doi:10.1038/77060 · Cited by 2,024
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
Inhibition of NADH-linked oxidation in brain mitochondria by 1-methyl-4-phenyl-pyridine, a metabolite of the neurotoxin, 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine
Nicklas, W. J., Vyas, I. L., & Heikkila, R. E. (1985) · Life Sciences · doi:10.1016/0024-3205(85)90146-8 · Cited by 1,273
Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease
Auluck, P. K., Chan, H. Y. E., Trojanowski, J. Q., Lee, V. M.-Y., & Bonini, N. M. (2002) · Science · doi:10.1126/science.1067389 · Cited by 1,227
Ubiquitination of a new form of α-synuclein by parkin from human brain: implications for Parkinson's disease
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A comparison of radiation-induced mitochondrial damage between neural progenitor stem cells and differentiated cells
Shimura, T., Sasatani, M., Kawai, H., Kamiya, K., Kobayashi, J., Komatsu, K., & Kunugita, N. (2017) · Cell Cycle · doi:10.1080/15384101.2017.1284716 · Cited by 41
Lon protease inactivation in Drosophila causes unfolded protein stress and inhibition of mitochondrial translation
Pareek, G., Thomas, R. E., Vincow, E. S., Morris, D. R., & Pallanck, L. J. (2018) · Cell Death Discovery · doi:10.1038/s41420-018-0110-1 · Cited by 37
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Lazzari, F. D., Sandrelli, F., Whitworth, A. J., & Bisaglia, M. (2020) · Antioxidants · doi:10.3390/antiox9010052 · Cited by 36
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van der Vlag, M., Havekes, R., & Heckman, P. R. A. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14689 · Cited by 37
Parkinson Disease: Translating Insights from Molecular Mechanisms to Neuroprotection
Pirooznia, S. K., Rosenthal, L. S., Dawson, V. L., & Dawson, T. M. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000189 · Cited by 36
Evaluation of Traditional Medicines for Neurodegenerative Diseases Using Drosophila Models
Lee, S., Bang, S. M., Lee, J. W., & Cho, K. S. (2014) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2014/967462 · Cited by 36
RBR Ubiquitin Ligases: Diversification and Streamlining in Animal Lineages
Marı́n, I. (2009) · Journal of Molecular Evolution · doi:10.1007/s00239-009-9252-3 · Cited by 38
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The STING pathway does not contribute to behavioural or mitochondrial phenotypes in Drosophila Pink1/parkin or mtDNA mutator models
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Pirooznia, S. K., Wang, H., Panicker, N., Kumar, M., Neifert, S., Dar, M. A., Lau, E., Kang, B. G., Redding‐Ochoa, J., Troncoso, J. C., et al. (2022) · Science Advances · doi:10.1126/sciadv.abh1824 · Cited by 34
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Biskup, S., & Moore, D. J. (2006) · BioEssays · doi:10.1002/bies.20471 · Cited by 35
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Self-citation
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Pogson, J. H., Ivatt, R. M., & Whitworth, A. J. (2011) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-011-0187-x · Cited by 26
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Liao, J. Z., Chung, H.-L., Shih, C. R. Y., Wong, K. K. L., Dutta, D., Nil, Z., Burns, C. G., Kanca, O., Park, Y.-J., Zuo, Z., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47623-8 · Cited by 27
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Lu, B., Gehrke, S., & Wu, Z. (2014) · Brain Research · doi:10.1016/j.brainres.2014.03.003 · Cited by 25
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Authors: Greene, J. C., Whitworth, A. J., Kuo, I., Andrews, L. A., Feany, M. B., & Pallanck, L. J.
Affiliations: Brigham and Women's Hospital (US)
Department of Genome Sciences, University of Washington, P.O. Box 357730, Seattle, WA 98195; and Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115
ORCID: Whitworth, Alexander J.
Pallanck, Leo J.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2003-03-17
Volume: 100
Issue: 7
Pages: 4078-4083
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.0737556100
PMC: PMC153051
OpenAlex: W2055124287
Cited by: 1,203
References: 34
Citations by year: 2026: 17 · 2025: 29 · 2024: 34 · 2023: 38 · 2022: 49 · 2021: 64 · 2020: 68 · 2019: 50 · 2018: 64 · 2017: 54 · 2016: 69 · 2015: 56 · 2014: 55 · 2013: 64 · 2012: 67
FWCI: 27.97
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of Neurological Disorders and Stroke (R01NS041780, 1R01NS41780-01, 1R01NS41536-01, R01NS041536)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
Keywords: Parkin, Parkinson's disease, autosomal recessive juvenile parkinsonism, mitochondrial dysfunction, muscle degeneration, apoptosis, Drosophila model, ubiquitin-protein ligase, spermatid individualization, male sterility, locomotion defects, lifespan, selective cell death
MeSH terms: Amino Acid Sequence, Animals, Cloning, Molecular, Drosophila, Ligases, Longevity, Male, Mitochondria, Molecular Sequence Data, Nerve Degeneration, Parkinson Disease, Recombinant Proteins, Spermatids, Mutagenesis, Sequence Alignment, Apoptosis, Sequence Homology, Amino Acid, Muscle, Skeletal, Ubiquitin-Protein Ligases

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Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants

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