[HTML][HTML] Poly-ubiquitin binding by the polyglutamine disease protein ataxin-3 links its normal function to protein surveillance pathways
Y Chai, SS Berke, RE Cohen, HL Paulson - Journal of Biological Chemistry, 2004 - ASBMB
In at least nine inherited diseases polyglutamine expansions cause neurodegeneration
associated with protein misfolding and the formation of ubiquitin-conjugated aggregates.
Although expanded polyglutamine triggers disease, functional properties of host
polyglutamine proteins also must influence pathogenesis. Using complementary in vitro and
cell-based approaches we establish that the polyglutamine disease protein, ataxin-3, is a
poly-ubiquitin-binding protein. In stably transfected neural cell lines, normal and expanded …
associated with protein misfolding and the formation of ubiquitin-conjugated aggregates.
Although expanded polyglutamine triggers disease, functional properties of host
polyglutamine proteins also must influence pathogenesis. Using complementary in vitro and
cell-based approaches we establish that the polyglutamine disease protein, ataxin-3, is a
poly-ubiquitin-binding protein. In stably transfected neural cell lines, normal and expanded …