Properties of native brain α-synuclein

Jacqueline Burré, Sandro Vivona, Jiajie Diao, Manu Sharma, Axel T. Brunger and Thomas C. Südhof ()
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Jacqueline Burré: Stanford University School of Medicine
Sandro Vivona: Stanford University School of Medicine
Jiajie Diao: Stanford University School of Medicine
Manu Sharma: Stanford University School of Medicine
Axel T. Brunger: Stanford University School of Medicine
Thomas C. Südhof: Stanford University School of Medicine

Nature, 2013, vol. 498, issue 7453, E4-E6

Abstract: Abstract Arising from T. Bartels, J. G. Choi & D. J. Selkoe. Nature 477, 107–110 (2011).10.1038/nature10324 α-Synuclein is an abundant presynaptic protein that binds to negatively charged phospholipids1,2, functions as a SNARE-complex chaperone3 and contributes to Parkinson’s disease pathogenesis4,5. Recombinant α-synuclein in solution is largely unfolded and devoid of tertiary structure6,7,8,9,10,11, but Bartels et al.12 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).

Date: 2013
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DOI: 10.1038/nature12125

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