Climbing the scaffolds of Parkinson's disease pathogenesis.
Several neurodegenerative disorders, including Parkinson's and Alzheimer's diseases, are characterized neuropathologically by accumulation of misfolded proteins such as alpha-synuclein that disrupts scaffold molecules in the caveolae. A new study by Ihara et al. in this issue of Neuron shows that a novel scaffold protein, Sept4, may be an important player in modulating the pathological alterations of alpha-synuclein in models of Parkinson's disease, suggesting that gene therapies targeting scaffold proteins might be effective in the treatment of neurodegenerative disorders.
Spencer
Brian
B
Department of Neurosciences, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
Crews
Leslie
L
Masliah
Eliezer
E
D000818:Animals; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D006801:Humans; D009474:Neurons / Q000378:metabolism; D010300:Parkinson Disease / Q000209:etiology / Q000378:metabolism / Q000473:pathology; D017510:Protein Folding; D058112:Septins; D051844:alpha-Synuclein / Q000378:metabolism
D003598:Cytoskeletal Proteins; D051844:alpha-Synuclein; D020558:GTP Phosphohydrolases; C492027:SEPTIN4 protein, human; D058112:Septins