The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation
Open accessAbstract
CNS neurons are endowed with the ability to recover from cytotoxic insults associated with the accumulation of proteinaceous aggregates in mouse models of polyglutamine disease, but the cellular mechanism underlying this phenomenon is unknown. Here, we show that autophagy is essential for the elimination of aggregated forms of mutant huntingtin and ataxin-1 from the cytoplasmic but not nuclear compartments. Human orthologs of yeast autophagy genes, molecular determinants of autophagic vacuole formation, are recruited to cytoplasmic but not nuclear inclusion bodies in vitro and in vivo . These data indicate that autophagy is a critical component of the cellular clearance of toxic protein aggregates and may help to explain why protein aggregates are more toxic when directed to the nucleus.
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Citations
Cites
LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.
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Protein aggregation and neurodegenerative disease
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Impairment of the Ubiquitin-Proteasome System by Protein Aggregation
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Self-citationDavies, S. W., Turmaine, M., Cozens, B. A., DiFiglia, M., Sharp, A. H., Ross, C. A., Scherzinger, E., Wanker, E. E., Mangiarini, L., & Bates, G. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80513-9 · Cited by 2,181
Aggresomes: A Cellular Response to Misfolded Proteins
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Self-citationInclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
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LC3 conjugation system in mammalian autophagy
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Glutamine Repeats and Neurodegeneration
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Cited by
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Selective autophagy mediated by autophagic adapter proteins
Johansen, T., & Lamark, T. (2011) · Autophagy · doi:10.4161/auto.7.3.14487 · Cited by 1,730
Regulation of Mammalian Autophagy in Physiology and Pathophysiology
Ravikumar, B., Sarkar, S., Davies, J. E., Futter, M., Garcia-Arencibia, M., Green-Thompson, Z. W., Jimenez-Sanchez, M., Korolchuk, V. I., Lichtenberg, M., Luo, S., et al. (2010) · Physiological Reviews · doi:10.1152/physrev.00030.2009 · Cited by 1,727
The roles of intracellular protein-degradation pathways in neurodegeneration
Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625
Sarkar, S., Davies, J. E., Huang, Z., Tunnacliffe, A., & Rubinsztein, D. C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609532200 · Cited by 1,142
Metadata
- Authors
- Iwata, A., Christianson, J. C., Bucci, M., Ellerby, L. M., Nukina, N., Forno, L. S., & Kopito, R. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-09-02
- Volume
- 102
- Issue
- 37
- Pages
- 13135-13140
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1977645267
- Cited by
- 318
- References
- 45
- FWCI
- 9.74
- Type
- journal article
- Language
- en
- Open access
- green
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- Iwata, A., Christianson, J. C., Bucci, M., Ellerby, L. M., Nukina, N., Forno, L. S., & Kopito, R. R. (2005). Increased susceptibility of cytoplasmic over nuclear polyglutamine aggregates to autophagic degradation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0505801102
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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