[HTML][HTML] The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains
BJ Winborn, SM Travis, SV Todi, KM Scaglione… - Journal of Biological …, 2008 - ASBMB
Ubiquitin chain complexity in cells is likely regulated by a diverse set of deubiquitinating
enzymes (DUBs) with distinct ubiquitin chain preferences. Here we show that the
polyglutamine disease protein, ataxin-3, binds and cleaves ubiquitin chains in a manner
suggesting that it functions as a mixed linkage, chain-editing enzyme. Ataxin-3 cleaves
ubiquitin chains through its amino-terminal Josephin domain and binds ubiquitin chains
through a carboxyl-terminal cluster of ubiquitin interaction motifs neighboring the pathogenic …
enzymes (DUBs) with distinct ubiquitin chain preferences. Here we show that the
polyglutamine disease protein, ataxin-3, binds and cleaves ubiquitin chains in a manner
suggesting that it functions as a mixed linkage, chain-editing enzyme. Ataxin-3 cleaves
ubiquitin chains through its amino-terminal Josephin domain and binds ubiquitin chains
through a carboxyl-terminal cluster of ubiquitin interaction motifs neighboring the pathogenic …