Hosting neurotoxicity in polyglutamine disease.
Polyglutamine diseases are caused by an expanded glutamine domain thought to confer a toxic activity onto the respective disease proteins. In this issue, propose that toxicity of the polyglutamine protein Ataxin-1 may not be due to abberant protein interactions mediated by the polyglutamine expansion. Instead, they suggest that toxicity is solely due to interactions of Ataxin-1 with its normal binding partners.
Liu
Nan
N
Department of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.
Bonini
Nancy M
NM
D000818:Animals; D000067696:Ataxin-1; D000067528:Ataxins; D004330:Drosophila / Q000196:embryology / Q000502:physiology; D006801:Humans; D051379:Mice; D008959:Models, Neurological; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D019636:Neurodegenerative Diseases / Q000209:etiology* / Q000235:genetics; D009687:Nuclear Proteins / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D012097:Repressor Proteins / Q000378:metabolism*; D020754:Spinocerebellar Ataxias / Q000209:etiology* / Q000235:genetics
C000593749:ATXN1 protein, human; D000067696:Ataxin-1; D000067528:Ataxins; C000593750:Atxn1 protein, mouse; C498611:Cic protein, mouse; D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; D010455:Peptides; D012097:Repressor Proteins; C097188:polyglutamine