Ubiquilin interacts and enhances the degradation of expanded-polyglutamine proteins

被引：35

作者：

Wang, Hongmin ^{[1
]}

Monteiro, Mervyn J. ^{[1
]}

机构：

[1] Univ Maryland, Inst Biotechnol, Ctr Med Biotechnol, Inst Neurodegenerat Dis, Baltimore, MD 21201 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 360卷 / 02期

关键词：

Huntington's disease; polyglutamine; ubiquilin; aggregation; protein turnover;

D O I：

10.1016/j.bbrc.2007.06.097

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：423 / 427

页数：5

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