Ubiquilin interacts and enhances the degradation of expanded-polyglutamine proteins
- Institute for Neurodegenerative Diseases, Medical Biotechnology Center, University of Maryland Biotechnology Institute, Room N352, 725 West Lombard Street, Baltimore, MD 21201 (United States)
Previously, we showed that overexpression of ubiquilin reduces protein aggregates and toxicity of expanded polyglutamine 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-1-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 polyglutamine proteins that are thought to cause several human diseases.
- OSTI ID:
- 20991505
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 360, Issue 2; Other Information: DOI: 10.1016/j.bbrc.2007.06.097; PII: S0006-291X(07)01304-6; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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