Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration

@article{Friedman2007PolyglutamineDM,
  title={Polyglutamine domain modulates the TBP-TFIIB interaction: implications for its normal function and neurodegeneration},
  author={Meyer J. Friedman and Anjali G Shah and Zhi-Hui Fang and Elizabeth M. Ward and Stephen T Warren and Shihua Li and Xiao-Jiang Li},
  journal={Nature Neuroscience},
  year={2007},
  volume={10},
  pages={1519-1528}
}
Expansion of the polyglutamine (polyQ) tract in human TATA-box binding protein (TBP) causes the neurodegenerative disease spinocerebellar ataxia 17 (SCA17). It remains unclear how the polyQ tract regulates normal protein function and induces selective neuropathology in SCA17. We generated transgenic mice expressing polyQ-expanded TBP. These mice showed weight loss, progressive neurological symptoms and neurodegeneration before early death. Expanded polyQ tracts reduced TBP dimerization but… CONTINUE READING

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