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Folding away the bad guys

Nature Reviews Neuroscience volume 7, pages 832–833 (2006)Cite this article

TRiC can direct this protein away from forming the toxic aggregates that characterize the devastating pathology of Huntington's disease.

The correct folding of newly synthesized proteins is regulated by a pathway that involves heat-shock proteins and chaperonins, such as TRiC (also known as CCT). Three groups have identified a new substrate for TRiC — Huntingtin (HTT) — and show that TRiC can direct this protein away from forming the toxic aggregates that characterize the devastating pathology of Huntington's disease.

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References

ORIGINAL RESEARCH PAPERS

  1. Kitamura, A. et al. Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state. Nature Cell Biol. 8, 1163–1169 (2006)

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  2. Behrends, C. et al. Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Mol. Cell 23, 887–897 (2006)

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  3. Tam, S. et al. The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nature Cell Biol. 8, 1155–1162 (2006)

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FURTHER READING

  1. Young, J. C. et al. Pathways of chaperone-mediated protein folding in the cytosol. Nature Rev. Mol. Cell Biol 5, 781–791 (2004)

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  1. Associate Editor, Nature Reviews Molecular Cell Biology,

    James Pickett

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  1. James Pickett
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Pickett, J. Folding away the bad guys. Nat Rev Neurosci 7, 832–833 (2006). https://doi.org/10.1038/nrn2034

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  • DOI: https://doi.org/10.1038/nrn2034

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