Cellular and Molecular Life Sciences

, Volume 64, Issue 17, pp 2194–2201

Physiological and pathological properties of α-synuclein

Authors

  • G. K. Tofaris
    • Cambridge Centre for Brain Repair and Department of Clinical Neuroscience Forvie Site
    • Cambridge Centre for Brain Repair and Department of Clinical Neuroscience Forvie Site
Multi-author Review

DOI: 10.1007/s00018-007-7217-5

Cite this article as:
Tofaris, G.K. & Spillantini, M.G. Cell. Mol. Life Sci. (2007) 64: 2194. doi:10.1007/s00018-007-7217-5

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-SynucleinParkinson’s diseaseα-synucleinopathiesneurodegenerationLewy body

Copyright information

© Birkhäuser Verlag, Basel 2007