The interplay between the chaperonin TRiC and N-terminal region of Huntingtin mediates Huntington’s Disease aggregation and pathogenesis

  • Koning Shen
  • Judith Frydman
Part of the Research and Perspectives in Alzheimer's Disease book series (ALZHEIMER)


Huntington’s Disease (HD) is a neurodegenerative disorder resulting from an expanded polyglutamine (polyQ) repeat in exon1 of the Huntingtin (Htt) protein. This polyQ expansion causes aggregation of the Htt protein in neuronal cells, which is linked to HD pathogenesis. Recent evidence has shown that Htt aggregation and toxicity are not solely dictated by the polyQ-expanded region but also by sequences flanking the polyQ region, particularly the first N-terminal 17 amino acids of Htt (N17). N17 has been shown to be critical in the Htt aggregation mechanism as well as host many post-translational modifications and interactions with molecular chaperones. Understanding how N17 functions in Htt aggregation and as a general handle for protein quality control will guide design of HD therapeutics.


Protein Quality Control Aggregation Propensity polyQ Protein Hydrophobic Face polyQ Tract 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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© Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  1. 1.Department of Biology and BioX ProgramStanford UniversityStanfordUSA

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