Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes.

@article{Jana2005CochaperoneCA,
  title={Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes.},
  author={Nihar R Jana and Priyanka Tiwari Dikshit and Anand Goswami and Svetlana Kotliarova and Shigeo Murata and Keiji Tanaka and Nobuyuki Nukina},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 12},
  pages={
          11635-40
        }
}

• Nihar R Jana, Priyanka Tiwari Dikshit, +4 authors Nobuyuki Nukina
• Published 2005 in The Journal of biological chemistry

A major hallmark of the polyglutamine diseases is the formation of neuronal intranuclear inclusions of the disease proteins that are ubiquitinated and often associated with various chaperones and proteasome components. But, how the polyglutamine proteins are ubiquitinated and degraded by the proteasomes are not known. Here, we demonstrate that CHIP (C terminus of Hsp70-interacting protein) co-immunoprecipitates with the polyglutamine-expanded huntingtin or ataxin-3 and associates with their… CONTINUE READING

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