Abstract
Spinocerebellar ataxia type 1 (SCA1) is an autosomal-dominant neurodegenerative disorder characterized by ataxia and progressive motor deterioration. SCA1 has been known to associate with elongated polyglutamine tract in ataxin-1, the SCA1 gene product. Using the yeast two-hybrid system, we have found that USP7, a ubiquitin-specific protease, binds to ataxin-1. Further experiments with deletion mutants indicated that the C-terminal region of ataxin-1 was essential for the interaction. Liquid β-galactosidase assay and coimmunoprecipitation experiments revealed that the strength of the interaction between USP7 and ataxin-1 is influenced by the length of the polyglutamine tract in the ataxin-1; weaker interaction was observed in mutant ataxin-1 with longer polyglutamine tract and USP7 was not recruited to the mutant ataxin-1 aggregates in the Purkinje cells of SCA1 transgenic mice. Our results suggest that altered function of the ubiquitin system can be involved in the pathogenesis of spinocerebellar ataxia type 1.
| Original language | English |
|---|---|
| Pages (from-to) | 298-306 |
| Number of pages | 9 |
| Journal | Molecular and Cellular Neuroscience |
| Volume | 20 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2002 Jul 23 |
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ASJC Scopus subject areas
- Molecular Biology
- Cellular and Molecular Neuroscience
- Developmental Neuroscience
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USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product. / Hong, Sunghoi; Kim, Sung J.; Ka, Sojeong; Choi, Inho; Kang, Seong Man.
In: Molecular and Cellular Neuroscience, Vol. 20, No. 2, 23.07.2002, p. 298-306.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product
AU - Hong, Sunghoi
AU - Kim, Sung J.
AU - Ka, Sojeong
AU - Choi, Inho
AU - Kang, Seong Man
PY - 2002/7/23
Y1 - 2002/7/23
N2 - Spinocerebellar ataxia type 1 (SCA1) is an autosomal-dominant neurodegenerative disorder characterized by ataxia and progressive motor deterioration. SCA1 has been known to associate with elongated polyglutamine tract in ataxin-1, the SCA1 gene product. Using the yeast two-hybrid system, we have found that USP7, a ubiquitin-specific protease, binds to ataxin-1. Further experiments with deletion mutants indicated that the C-terminal region of ataxin-1 was essential for the interaction. Liquid β-galactosidase assay and coimmunoprecipitation experiments revealed that the strength of the interaction between USP7 and ataxin-1 is influenced by the length of the polyglutamine tract in the ataxin-1; weaker interaction was observed in mutant ataxin-1 with longer polyglutamine tract and USP7 was not recruited to the mutant ataxin-1 aggregates in the Purkinje cells of SCA1 transgenic mice. Our results suggest that altered function of the ubiquitin system can be involved in the pathogenesis of spinocerebellar ataxia type 1.
AB - Spinocerebellar ataxia type 1 (SCA1) is an autosomal-dominant neurodegenerative disorder characterized by ataxia and progressive motor deterioration. SCA1 has been known to associate with elongated polyglutamine tract in ataxin-1, the SCA1 gene product. Using the yeast two-hybrid system, we have found that USP7, a ubiquitin-specific protease, binds to ataxin-1. Further experiments with deletion mutants indicated that the C-terminal region of ataxin-1 was essential for the interaction. Liquid β-galactosidase assay and coimmunoprecipitation experiments revealed that the strength of the interaction between USP7 and ataxin-1 is influenced by the length of the polyglutamine tract in the ataxin-1; weaker interaction was observed in mutant ataxin-1 with longer polyglutamine tract and USP7 was not recruited to the mutant ataxin-1 aggregates in the Purkinje cells of SCA1 transgenic mice. Our results suggest that altered function of the ubiquitin system can be involved in the pathogenesis of spinocerebellar ataxia type 1.
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UR - http://www.scopus.com/inward/citedby.url?scp=0036311587&partnerID=8YFLogxK
U2 - 10.1006/mcne.2002.1103
DO - 10.1006/mcne.2002.1103
M3 - Article
C2 - 12093161
AN - SCOPUS:0036311587
VL - 20
SP - 298
EP - 306
JO - Molecular and Cellular Neurosciences
JF - Molecular and Cellular Neurosciences
SN - 1044-7431
IS - 2
ER -