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

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.

Pubmed ID: 12062018


  • 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



Publication Data

May 30, 2002

Associated Grants


Mesh Terms

  • Aged
  • Animals
  • Carrier Proteins
  • Cell Death
  • Cell Nucleus
  • Cell Survival
  • Cells, Cultured
  • Cerebellum
  • Disease Models, Animal
  • Female
  • Genes, Regulator
  • Humans
  • Inclusion Bodies
  • Macromolecular Substances
  • Mice
  • Nerve Tissue Proteins
  • Neurons
  • Nuclear Proteins
  • Peptides
  • Protein Structure, Tertiary
  • RNA Polymerase II
  • Spinocerebellar Ataxias
  • Trinucleotide Repeat Expansion