Brett J. Winborn

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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(More)
Deubiquitinating enzymes (DUBs) control the ubiquitination status of proteins in various cellular pathways. Regulation of the activity of DUBs, which is critically important to cellular homoeostasis, can be achieved at the level of gene expression, protein complex formation, or degradation. Here, we report that ubiquitination also directly regulates the(More)
Ataxin-3, a deubiquitinating enzyme, is the disease protein in spinocerebellar ataxia type 3, one of many neurodegenerative disorders caused by polyglutamine expansion. Little is known about the cellular regulation of ataxin-3. This is an important issue, since growing evidence links disease protein context to pathogenesis in polyglutamine disorders.(More)
Brett J. Winborn, Sue M. Travis, Sokol V. Todi, K. Matthew Scaglione, Ping Xu , Aislinn J. Williams**, Robert E. Cohen, Junmin Peng , and Henry L. Paulson From the Program in Molecular and Cellular Biology, Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242, the Department of Biochemistry, Carver College of Medicine, University of Iowa,(More)
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