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Trends Mol Med. 2013 Jun;19(6):368-77. doi: 10.1016/j.molmed.2013.04.002. Epub 2013 May 3.

The remarkable conformational plasticity of alpha-synuclein: blessing or curse?

Author information

1
Laboratory for Neurobiology and Gene Therapy, Department of Neurosciences and Leuven Research Institute for Neuroscience and Disease (LIND), KU Leuven, Flanders, Belgium.

Abstract

The aggregation of the protein alpha-synuclein (α-SYN) is believed to be a critical event in Parkinson's disease (PD). α-SYN is characterized by a remarkable conformational plasticity, adopting different conformations depending on the environment. In vitro, α-SYN lacks a well-defined structure. Therefore, it was classified as an 'intrinsically disordered protein'. A debate has recently begun over how α-SYN behaves in the cell: is it an intrinsically disordered protein or a stable tetramer with a low propensity for aggregation? In this review, we discuss the aggregation of α-SYN and describe factors that influence this process and their potential relevance in PD pathogenesis. We address the ways in which aggregated α-SYN mediates toxicity and might lead to PD, and propose possible therapeutic strategies.

PMID:
23648364
DOI:
10.1016/j.molmed.2013.04.002
[Indexed for MEDLINE]

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