Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1818, Issue 4, Pages 1013-1018Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2011.09.008
Keywords
Alpha-synuclein; Parkinson's; Amyloid; Membrane; Aggregation
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Funding
- NIA NIH HHS [R01 AG019391, R37 AG019391-10, R01 AG025440, R01 AG025440-04, R01 AG019391-09, R37 AG019391] Funding Source: Medline
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The protein alpha-synuclein is considered to play a major role in the etiology of Parkinson's disease. Because it is found in a classic amyloid fibril form within the characteristic intra-neuronal Lewy body deposits of the disease, aggregation of the protein is thought to be of critical importance, but the context in which the protein undergoes aggregation within cells remains unknown. The normal function of synucleins is poorly understood, but appears to involve membrane interactions, and in particular reversible binding to synaptic vesicle membranes. Structural studies of different states of alpha-synuclein, in the absence and presence of membranes or membrane mimetics, have led to models of how membrane-bound forms of the protein may contribute both to functional properties of the protein, as well as to membrane-induced self-assembly and aggregation. This article reviews this area, with a focus on a particular model that has emerged in the past few years. This article is part of a Special Issue entitled: Protein Folding in Membranes. (C) 2011 Elsevier B.V. All rights reserved.
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