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
        }
}
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
Highly Influential
This paper has highly influenced 16 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS
Highly Cited
This paper has 205 citations. REVIEW CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 120 extracted citations

The BAG2 and BAG5 proteins inhibit the ubiquitination of pathogenic ataxin3-80Q.

The International journal of neuroscience • 2015
View 7 Excerpts
Highly Influenced

Orchestra for assembly and fate of polyubiquitin chains.

Essays in biochemistry • 2005
View 10 Excerpts
Highly Influenced

206 Citations

0102030'07'10'13'16'19
Citations per Year
Semantic Scholar estimates that this publication has 206 citations based on the available data.

See our FAQ for additional information.