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α-Synuclein has been implicated in the pathogenesis of Parkinson's disease based on mutations in familial cases of the disease and its presence in Lewy bodies. Here we show that over-expression of wild-type human α-synuclein is sufficient to induce inclusion formation in SH-SY5Y cells. In this cellular model, proteasome inhibition leads to an increase of α-synuclein accumulation in vivo without ubiquitylation. In accordance, we find that in vitro, unmodified α-synuclein can be directly degraded by the 20S proteasome. These findings suggest an ubiquitin-independent mechanism of proteasomal degradation for α-synuclein and other natively unfolded proteins. © 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

Original publication

DOI

10.1016/S0014-5793(01)03115-5

Type

Journal article

Journal

FEBS Letters

Publication Date

30/11/2001

Volume

509

Pages

22 - 26