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Cellular and Molecular Life Sciences: CMLS logoLink to Cellular and Molecular Life Sciences: CMLS
. 2007 Jul 2;64(17):2194–2201. doi: 10.1007/s00018-007-7217-5

Physiological and pathological properties of α-synuclein

G K Tofaris 1, M G Spillantini 1,
PMCID: PMC11135986  PMID: 17605001

Abstract.

α-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial α-helical conformation. Under certain pathogenic conditions, α-synuclein aggregates to form oligomers and insoluble fibrils with increased ß-sheet configuration. Although genetic mutations and multiplications of the gene have been found in familial cases, the mechanism by which this protein aggregates in sporadic cases of Parkinson’s disease, dementia with Lewy bodies and multisystem atrophy is not fully understood. Here we review the function of α-synuclein and recent insight into the mechanisms by which it aggregates.

Keywords. α-Synuclein, Parkinson’s disease, α-synucleinopathies, neurodegeneration, Lewy body


Articles from Cellular and Molecular Life Sciences: CMLS are provided here courtesy of Springer

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