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

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 aggregates. Transient overexpression of CHIP increases the ubiquitination and the rate of degradation of polyglutamine-expanded huntingtin or ataxin-3. Finally, we show that overexpression of CHIP suppresses the aggregation and cell death mediated by expanded polyglutamine proteins and the suppressive effect is more prominent when CHIP is overexpressed along with Hsc70.

Pubmed ID: 15664989

Authors

  • Jana NR
  • Dikshit P
  • Goswami A
  • Kotliarova S
  • Murata S
  • Tanaka K
  • Nukina N

Journal

The Journal of biological chemistry

Publication Data

March 25, 2005

Associated Grants

None

Mesh Terms

  • Animals
  • Apoptosis
  • Cell Line
  • Drosophila Proteins
  • Mice
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • Peptides
  • Proteasome Endopeptidase Complex
  • Protein Folding
  • Repressor Proteins
  • Transcription Factors
  • Ubiquitin
  • Ubiquitin-Protein Ligases