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Interaction between mutant ataxin-1 and PQBP-1 affects transcription and cell death.

Authors:
Okazawa H, Rich T, Chang A, Lin X, Waragai M, Kajikawa M, Enokido Y, Komuro A, Kato S, Shibata M, Hatanaka H, Mouradian MM, Sudol M, Kanazawa I
Affiliation:
Journal:
Neuron

Abstract

PQBP-1 was isolated on the basis of its interaction with polyglutamine tracts. In this study, using in vitro and in vivo assays, we show that the association between ataxin-1 and PQBP-1 is positively influenced by expanded polyglutamine sequences. In cell lines, interaction between the two molecules induces apoptotic cell death. As a possible mechanism underlying this phenomenon, we found that mutant ataxin-1 enhances binding of PQBP-1 to the C-terminal domain of RNA polymerase II large subunit (Pol II). This reduces the level of phosphorylated Pol II and transcription. Our results suggest the involvement of PQBP-1 in the pathology of spinocerebellar ataxia type 1 (SCA1) and support the idea that modified transcription underlies polyglutamine-mediated pathology.

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