The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation
Open accessAbstract
Aggregation of proteins containing polyglutamine (polyQ) expansions characterizes many neurodegenerative disorders, including Huntington's disease. Molecular chaperones modulate the aggregation and toxicity of the huntingtin (Htt) protein by an ill-defined mechanism. Here we determine how the chaperonin TRiC suppresses Htt aggregation. Unexpectedly, TRiC does not physically block the polyQ tract itself, but rather sequesters a short Htt sequence element, N-terminal to the polyQ tract, that promotes the amyloidogenic conformation. The residues of this element essential for rapid Htt aggregation are directly bound by TRiC. Our findings illustrate how molecular chaperones, which recognize hydrophobic determinants, can prevent aggregation of polar polyQ tracts associated with neurodegenerative diseases. The observation that short endogenous sequence elements can accelerate the switch of polyQ tracts to an amyloidogenic conformation provides a novel target for therapeutic strategies.
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Citations
Cites
Unfolding the role of protein misfolding in neurodegenerative diseases
Soto, C. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1007 · Cited by 1,506
Progressive disruption of cellular protein folding in models of polyglutamine diseases
Gidalevitz, T., Ben-Zvi, A., Ho, K. H., Brignull, H. R., & Morimoto, R. I. (2006) · Science · doi:10.1126/science.1124514 · Cited by 643
Cited by
Huntington's disease: from molecular pathogenesis to clinical treatment
Ross, C. A., & Tabrizi, S. J. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70245-3 · Cited by 1,743
Bates, G. P., Dorsey, R., Gusella, J. F., Hayden, M. R., Kay, C., Leavitt, B. R., Nance, M., Ross, C. A., Scahill, R. I., Wetzel, R., et al. (2015) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2015.5 · Cited by 1,641
Cellular Strategies of Protein Quality Control
Chen, B., Retzlaff, M., Roos, T., & Frydman, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004374 · Cited by 502
Self-citationSun, Z., Diaz, Z., Fang, X., Hart, M. P., Chesi, A., Shorter, J., & Gitler, A. D. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000614 · Cited by 458
Protein aggregates in Huntington's disease
Arrasate, M., & Finkbeiner, S. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2011.12.013 · Cited by 383
Metadata
- Authors
- Tam, S., Spiess, C., Auyeung, W., Joachimiak, L., Chen, B., Poirier, M. A., & Frydman, J.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2009-11-15
- Volume
- 16
- Issue
- 12
- Pages
- 1279-1285
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2060354977
- Cited by
- 245
- References
- 2
- FWCI
- 7.78
- Type
- journal article
- Language
- en
- Open access
- green
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- Tam, S., Spiess, C., Auyeung, W., Joachimiak, L., Chen, B., Poirier, M. A., & Frydman, J. (2009). The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1700
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