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- Title
Properties of native brain α-synuclein.
- Authors
Burré, Jacqueline; Vivona, Sandro; Diao, Jiajie; Sharma, Manu; Brunger, Axel T.; Südhof, Thomas C.
- Abstract
Arising from T. Bartels, J. G. Choi & D. J. Selkoe. 477, 107-110 (2011).α-Synuclein is an abundant presynaptic protein that binds to negatively charged phospholipids, functions as a SNARE-complex chaperone and contributes to Parkinson's disease pathogenesis. Recombinant α-synuclein in solution is largely unfolded and devoid of tertiary structure, but Bartels et al. have proposed that native α-synuclein purified from human erythrocytes forms a stably folded, soluble tetramer that resists aggregation. By contrast, we show here that native α-synuclein purified from mouse brain consists of a largely unstructured monomer, exhibits no stable tetramer formation, and is prone to aggregation. The native state of α-synuclein is important for understanding its pathological effects as a stably folded protein would be much less prone to aggregation than a conformationally labile protein. There is a Reply to this Brief Communication Arising by Bartels, T. & Selkoe, D. J. Nature 498, http://dx.doi.org/10.1038/nature12126 (2013).
- Subjects
SYNUCLEINS; PROTEINS; PHOSPHOLIPIDS; MOLECULAR chaperones; PARKINSON'S disease; ERYTHROCYTES; BRAIN physiology; LABORATORY mice
- Publication
Nature, 2013, Vol 498, Issue 7453, pE4
- ISSN
0028-0836
- Publication type
Article
- DOI
10.1038/nature12125