title: Snaring the function of alpha-synuclein.
abstract: It is well established that the abundant neuronal protein alpha-synuclein has a causal role in Parkinson's disease, yet the normal functions of this protein remain unclear. In this issue of Cell, Chandra et al. (2005) reveal that alpha-synuclein acts as a molecular chaperone, assisting in the folding and refolding of synaptic proteins called SNAREs. These proteins are crucial for release of neurotransmitters at the neuronal synapse, vesicle recycling, and synaptic integrity.
authors.affiliation: Department of Biology and Howard Hughes Medical Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
authors.forename: Nancy M
authors.initials: NM
authors.lastname: Bonini
authors.forename: Benoit I
authors.initials: BI
authors.lastname: Giasson
mesh_terms: D000818:Animals; D050956:HSP40 Heat-Shock Proteins / Q000235:genetics / Q000502:physiology*; D006801:Humans; D018832:Molecular Chaperones / Q000235:genetics / Q000502:physiology*; D009154:Mutation; D009474:Neurons / Q000378:metabolism; D010300:Parkinson Disease / Q000235:genetics / Q000378:metabolism; D017510:Protein Folding; D021381:Protein Transport; D050600:SNARE Proteins / Q000378:metabolism*; D013569:Synapses / Q000378:metabolism; D013572:Synaptic Vesicles / Q000378:metabolism*; D051844:alpha-Synuclein / Q000235:genetics / Q000502:physiology*
chemical_list: D050956:HSP40 Heat-Shock Proteins; D018832:Molecular Chaperones; D050600:SNARE Proteins; D051844:alpha-Synuclein