Interactions between metals and α-synuclein − function or artefact?

Authors


D. R. Brown, Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK
Fax: +44 1225 386779
Tel: +44 1225 383133
E-mail: bssdrb@bath.ac.uk

Abstract

α-synuclein is one of a family of proteins whose function remains unknown. This protein has become linked to a number of neurodegenerative disease although its potential causative role in these diseases remains mysterious. In diseases such as Parkinson's disease and Lewy body dementias, α-synuclein becomes deposited in aggregates termed Lewy bodies. Also, some inherited forms of Parkinson's diseases are linked to mutations in the gene for α-synuclein. Studies have mostly focussed on what causes the aggregation of the protein but, like many amyloidogenic proteins associated with a neurodegenerative disorder, this protein has now been suggested to bind copper. This finding is currently controversial. This review examines the evidence that α-synuclein is a copper binding protein and discusses whether this has any significance in determining the function of the protein or whether copper binding is at all necessary for aggregation.

Ancillary