Physiological and pathological properties of alpha-synuclein

alpha-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial alpha-helical conformation. Under certain pathogenic conditions, alpha-synuclein aggregates to form oligomers and insoluble fibrils with increased ss-sheet config...

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Bibliographic Details
Published inCellular and molecular life sciences : CMLS Vol. 64; no. 17; pp. 2194 - 2201
Main Authors Tofaris, G K, Spillantini, M G
Format Journal Article
LanguageEnglish
Published Switzerland Birkhäuser-Verlag 01.09.2007
Subjects
alpha-Synuclein - chemistry
alpha-Synuclein - genetics
alpha-Synuclein - physiology
Humans
Lewy Bodies - metabolism
Multi-author Review
Parkinson Disease - genetics
Parkinson Disease - metabolism
Parkinson Disease - pathology
Protein Processing, Post-Translational
Protein Structure, Tertiary
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Summary:alpha-Synuclein belongs to a small group of natively unfolded proteins that can transiently bind to lipid membranes and acquire a partial alpha-helical conformation. Under certain pathogenic conditions, alpha-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 alpha-synuclein and recent insight into the mechanisms by which it aggregates.
Bibliography:ObjectType-Article-2
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ISSN:1420-682X
1420-9071
DOI:10.1007/s00018-007-7217-5