SUMO-1 interacts with mutant ataxin-1 and colocalizes to its aggregates in Purkinje cells of SCA1 transgenic mice
- Authors
- Kang, S.; Hong, S.
- Issue Date
- 12월-2010
- Publisher
- PISA UNIV PRESS
- Keywords
- Aggregates; Polyglutamine; Mutant ataxin-1; SCA1; SUMO-1
- Citation
- ARCHIVES ITALIENNES DE BIOLOGIE, v.148, no.4, pp.351 - 363
- Indexed
- SCIE
SCOPUS
- Journal Title
- ARCHIVES ITALIENNES DE BIOLOGIE
- Volume
- 148
- Number
- 4
- Start Page
- 351
- End Page
- 363
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/115148
- ISSN
- 0003-9829
- Abstract
- Spinocerebellar ataxia type 1 (SCA1) is one of several progressive neurodegenerative diseases caused by the expanded polyglutamine tract in ataxin-1, the SCA1 gene product. In SCA1 patients and transgenic mice, the affected neuronal cells contain a large ubiquitin-positive aggregate which is derived from the mutant ataxin-1. Small ubiquitin-like modifier-1 (SUMO-1) is one of the most intriguing ubiquitin-like modifiers being conjugated to target proteins and modulating a number of cellular pathways. Recent findings that the aggregates from several neurodegenerative diseases are SUMO-1-positive prompted us to examine the implication of SUMO-1 in SCA1 pathogenesis. In our yeast two-hybrid experiments using mutant ataxin-1 as bait, we identified a SUMO-1 protein that directly hinds to ataxin-1 protein. Interestingly, we found that most of the mutant ataxin-1-derived aggregates were SUMO-1-positive both in Purkinje cells of SCA1 transgenic mice and in HeLa cells, but not wild-type ataxin-1 in HeLa cells. In addition, the aggregates in Purkinje cells of SCA I transgenic mice were positive against both anti-SUMO-1 and anti-ubiquitin antibodies. These results show that the SUMO-1 protein interacts with mutant ataxin-1 and colocalizes with its aggregates which suggests the involvement of the SUMO-1 system in the pathogenesis of SCA I disease.
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Collections - Graduate School > Department of Life Sciences > 1. Journal Articles
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