Abstract
Spinocerebellar ataxia type 1 (SCA1) is an autosomal-dominant neurodegenerative disorder characterized by ataxia and progressive motor deterioration. SCA1 is associated with an elongated polyglutamine tract in ataxin-1, the SCA1 gene product. Using the yeast two-hybrid system and co-immunoprecipitation experiments, we have found that p80 coilin, coiled body-specific protein, binds to ataxin-1. In further experiments with deletion mutants, we found that the C-terminal regions of ataxin-1 and p80 coilin were essential for this interaction. In HeLa cells that have been co-transfected with ataxin-1 and p80 coilin, the p80 coilin protein co-localizes with ataxin-1 aggregates in the nucleoplasm. However, immunohistochemical analysis and immunofluorescence assays showed that mutant ataxin-1 aggregates do not redistribute p80 coilin's dot-like structures in the Purkinje cells of SCA1 transgenic mice. This feature of the interaction between ataxin-1 and p80 coilin suggests that p80 coilin might be implicated in altering the function of ataxin-1.
| Original language | English |
|---|---|
| Pages (from-to) | 35-42 |
| Number of pages | 8 |
| Journal | Biochimica et Biophysica Acta - Molecular Basis of Disease |
| Volume | 1638 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2003 May 20 |
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Keywords
- Coiled body
- p80 coilin
- Polyglutamine
- SCA1
- Yeast two-hybrid
ASJC Scopus subject areas
- Molecular Biology
- Molecular Medicine
- Biophysics
Cite this
p80 coilin, a coiled body-specific protein, interacts with ataxin-1, the SCA1 gene product. / Hong, Sunghoi; Ka, Sojeong; Kim, Sungjo; Park, Yongjae; Kang, Seong Man.
In: Biochimica et Biophysica Acta - Molecular Basis of Disease, Vol. 1638, No. 1, 20.05.2003, p. 35-42.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - p80 coilin, a coiled body-specific protein, interacts with ataxin-1, the SCA1 gene product
AU - Hong, Sunghoi
AU - Ka, Sojeong
AU - Kim, Sungjo
AU - Park, Yongjae
AU - Kang, Seong Man
PY - 2003/5/20
Y1 - 2003/5/20
N2 - Spinocerebellar ataxia type 1 (SCA1) is an autosomal-dominant neurodegenerative disorder characterized by ataxia and progressive motor deterioration. SCA1 is associated with an elongated polyglutamine tract in ataxin-1, the SCA1 gene product. Using the yeast two-hybrid system and co-immunoprecipitation experiments, we have found that p80 coilin, coiled body-specific protein, binds to ataxin-1. In further experiments with deletion mutants, we found that the C-terminal regions of ataxin-1 and p80 coilin were essential for this interaction. In HeLa cells that have been co-transfected with ataxin-1 and p80 coilin, the p80 coilin protein co-localizes with ataxin-1 aggregates in the nucleoplasm. However, immunohistochemical analysis and immunofluorescence assays showed that mutant ataxin-1 aggregates do not redistribute p80 coilin's dot-like structures in the Purkinje cells of SCA1 transgenic mice. This feature of the interaction between ataxin-1 and p80 coilin suggests that p80 coilin might be implicated in altering the function of ataxin-1.
AB - Spinocerebellar ataxia type 1 (SCA1) is an autosomal-dominant neurodegenerative disorder characterized by ataxia and progressive motor deterioration. SCA1 is associated with an elongated polyglutamine tract in ataxin-1, the SCA1 gene product. Using the yeast two-hybrid system and co-immunoprecipitation experiments, we have found that p80 coilin, coiled body-specific protein, binds to ataxin-1. In further experiments with deletion mutants, we found that the C-terminal regions of ataxin-1 and p80 coilin were essential for this interaction. In HeLa cells that have been co-transfected with ataxin-1 and p80 coilin, the p80 coilin protein co-localizes with ataxin-1 aggregates in the nucleoplasm. However, immunohistochemical analysis and immunofluorescence assays showed that mutant ataxin-1 aggregates do not redistribute p80 coilin's dot-like structures in the Purkinje cells of SCA1 transgenic mice. This feature of the interaction between ataxin-1 and p80 coilin suggests that p80 coilin might be implicated in altering the function of ataxin-1.
KW - Coiled body
KW - p80 coilin
KW - Polyglutamine
KW - SCA1
KW - Yeast two-hybrid
UR - http://www.scopus.com/inward/record.url?scp=0038664243&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0038664243&partnerID=8YFLogxK
U2 - 10.1016/S0925-4439(03)00038-3
DO - 10.1016/S0925-4439(03)00038-3
M3 - Article
C2 - 12757932
AN - SCOPUS:0038664243
VL - 1638
SP - 35
EP - 42
JO - Biochimica et Biophysica Acta - Molecular Basis of Disease
JF - Biochimica et Biophysica Acta - Molecular Basis of Disease
SN - 0925-4439
IS - 1
ER -