One neuronal characteristic of Parkinson disease is the presence of Lewy bodies–intracytoplasmic accumulations of protein. A new study draws a molecular link between the formation of these bodies, the ubiquitin protein degradation system, parkin and synphilin-1. (pages 1144–1150)
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Stephen Horwitz
Stephen Horwitz
References
Chung, K.K.K. et al. Parkin ubiquitinates the α-synuclein-interacting protein synphilin-1: Implications for Lewy body formation in Parkinson disease. Nature Med. 7, 1144–1150 (2001).
Weissman, A.M. Themes and variations on ubiquitylation. Nature Rev. Cell Mol. Biol. 2, 169–179 (2001).
Voges, D., Zwickl, P. & Baumeister, W. The 26S proteasome: A molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68, 1015–1068 (1999).
Shimura, H. et al. Familial Parkinson disease gene product, Parkin, is a ubiquitin-protein ligase. Nat. Genet. 25, 302–305 (2000).
Kitada, T. et al. Mutations in the Parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392, 605–608 (1998).
Shimura, H. et al. Ubiquitination of a new form of α-synuclein by Parkin from human brain: Implications for Parkinson's disease. Science 293, 263–269 (2001).
Cummings, C.J. et al. Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron 24, 879–892 (1999).
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Ciechanover, A. Linking ubiquitin, parkin and synphilin-1. Nat Med 7, 1108–1109 (2001). https://doi.org/10.1038/nm1001-1108
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DOI: https://doi.org/10.1038/nm1001-1108
