Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 360, Issue 2, Pages 423-427Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2007.06.097
Keywords
Huntington's disease; polyglutamine; ubiquilin; aggregation; protein turnover
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Funding
- NIGMS NIH HHS [R01 GM066287, GM066287, R01 GM066287-04] Funding Source: Medline
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Previously, we showed that overexpression of ubiquilin reduces protein aggregates and toxicity of expanded polyglutarnine proteins. Here, we investigated the mechanism of ubiquilin's protective effect. Immunofluorescence microscopy and immunoprecipitation studies indicated that ubiquilin colocalized and coimmunoprecipitated more with GFP-huntingtin-exon-l-fusion proteins containing a 74-polyglutamine tract than with GFP-huntingtin-fusion proteins containing a 28-polyglutamine tract or with GFP protein alone. Furthermore, overexpression of ubiquilin selectively enhanced the turnover of the expanded GFP-huntingtin-fusion protein. These results suggest that elevating ubiquilin levels could aid in the selective disposal of potentially toxic expanded polyglutarnine proteins that are thought to cause several human diseases. (C) 2007 Elsevier Inc. All rights reserved.
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