USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product

Sunghoi Hong, Sung J. Kim, Sojeong Ka, Inho Choi, Seong Man Kang

Research output: Contribution to journalArticle

50 Citations (Scopus)

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 languageEnglish
Pages (from-to)298-306
Number of pages9
JournalMolecular and Cellular Neuroscience
Volume20
Issue number2
DOIs
Publication statusPublished - 2002 Jul 23

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Ubiquitin-Specific Proteases
Spinocerebellar Ataxias
Genes
Galactosidases
Two-Hybrid System Techniques
Purkinje Cells
Ataxia
Ubiquitin
Ataxin-1
Neurodegenerative Diseases
Transgenic Mice

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience
  • Developmental Neuroscience

Cite this

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 journalArticle

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