The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity
Abstract
Huntington's disease (HD) is an autosomal dominant neurodegenerative disorder caused by polyglutamine expansion in the disease protein, huntingtin. In HD patients and transgenic mice, the affected neurons form characteristic ubiquitin-positive nuclear inclusions (NIs). We have established ecdysone-inducible stable mouse Neuro2a cell lines that express truncated N-terminal huntingtin (tNhtt) with different polyglutamine lengths which form both cytoplasmic and nuclear aggregates in a polyglutamine length- and inducer dose-dependent manner. Here we demonstrate that newly synthesized polyglutamine-expanded truncated huntingtin interacts with members of Hsp40 and Hsp70 families of chaperones in a polyglutamine length-dependent manner. Of these interacting chaperones, only Hdj-2 and Hsc70 frequently (Hdj-2 > Hsc70) co-localize with both the aggregates in the cellular model and with the NIs in the brains of HD exon 1 transgenic mice. However, Hdj-2 and Hsc70 do not co-localize with cytoplasmic aggregates in the brains of transgenic mice despite these chaperones being primarily localized in the cytoplasmic compartment. This strongly suggests that the chaperone interaction and their redistribution to the aggregates are two completely different phenomena of the cellular unfolded protein response. This unfolded protein response is also evident from the dramatic induction of Hsp70 on expression of polyglutamine-expanded protein in the cellular model. Transient overexpression of either Hdj-1 or Hsc70 suppresses the aggregate formation; however, suppression efficiency is much higher in Hdj-1 compared with Hsc70. Overexpression of Hdj-1 and Hsc70 is also able to protect cell death caused by polyglutamine-expanded tNhtt and their combination proved to be most effective.
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Cites
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Nuclear and Neuropil Aggregates in Huntington’s Disease: Relationship to Neuropathology
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Cited by
Regional and cellular gene expression changes in human Huntington's disease brain
Hodges, A., Strand, A. D., Aragaki, A. K., Kuhn, A., Sengstag, T., Hughes, G., Elliston, L. A., Hartog, C., Goldstein, D. R., Thu, D., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl013 · Cited by 804
Molecular Mechanisms and Potential Therapeutical Targets in Huntington's Disease
Zuccato, C., Valenza, M., & Cattaneo, E. (2010) · Physiological Reviews · doi:10.1152/physrev.00041.2009 · Cited by 848
A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease
Brehme, M., Voisine, C., Rolland, T., Wachi, S., Soper, J. H., Zhu, Y., Orton, K., Villella, A., Garza, D., Vidal, M., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.09.042 · Cited by 584
Hsp70 Reduces α-Synuclein Aggregation and Toxicity
Klucken, J., Shin, Y., Masliah, E., Hyman, B. T., & McLean, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400255200 · Cited by 508
Duan, W., Guo, Z., Jiang, H., Ware, M., Li, X.-J., & Mattson, M. P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0536856100 · Cited by 428
Metadata
- Authors
- Jana, N. R.
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2000-08-12
- Volume
- 9
- Issue
- 13
- Pages
- 2009-2018
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2156079900
- Cited by
- 432
- References
- 41
- FWCI
- 8.22
- Type
- journal article
- Language
- en
- Open access
- closed
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- Jana, N. R. (2000). Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicity. Human Molecular Genetics. https://doi.org/10.1093/hmg/9.13.2009
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