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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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
Self-citation
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
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Parkin and relatives: the RBR family of ubiquitin ligases
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Jin, X., Wang, K., Wang, L., Liu, W., Zhang, C., Qiu, Y., Liu, W., Zhang, H., Zhang, D., Yang, Z., et al. (2021) · Autophagy · doi:10.1080/15548627.2021.1946739 · Cited by 114
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Cook, C. N., & Petrucelli, L. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.01.012 · Cited by 119

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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