Interactions between metals and alpha-synuclein--function or artefact?
alpha-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, alpha-synuclein becomes deposited in aggregates termed Lewy bodies. Also, some inherited forms of Parkinson's diseases are linked to mutations in the gene for alpha-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 alpha-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.
Brown
David R
DR
Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath, UK. bssdrb@bath.ac.uk
D000818:Animals; D016477:Artifacts; D006801:Humans; D008670:Metals / Q000378:metabolism*; D009154:Mutation / Q000235:genetics; D011485:Protein Binding; D051844:alpha-Synuclein / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure
D008670:Metals; D051844:alpha-Synuclein