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  Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity

Sakahira, H., Breuer, P., Hayer-Hartl, M. K., & Hartl, F. U. (2002). Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proceedings of the National Academy of Sciences of the United States of America, 99(Suppl. 4), 16412-16418.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-6DAF-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-6DB0-A
Genre: Journal Article
Alternative Title : Proc. Natl. Acad. Sci. U. S. A.

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 Creators:
Sakahira, H.1, Author              
Breuer, P.1, Author              
Hayer-Hartl, M. K.2, Author              
Hartl, F. U.1, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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 Abstract: The formation of insoluble protein aggregates in neurons is a hallmark of neurodegenerative diseases caused by proteins with expanded polyglutamine (polyQ) repeats. However, the mechanistic relationship between polyQ aggregation and its toxic effects on neurons remains unclear. Two main hypotheses have been put forward for how polyQ expansions may cause cellular dysfunction. In one model neurotoxicity results from the ability of polyQ-expanded proteins to recruit other important cellular proteins with polyQ stretches into the aggregates. In the other model, aggregating polyQ proteins partially inhibit the ubiquitin-proteasome system for protein degradation. These two mechanisms are not exclusive but may act in combination. In general, protein misfolding and aggregation are prevented by the machinery of molecular chaperones. Some chaperones such as the members of the Hsp70 family also modulate polyQ aggregation and suppress its toxicity. These recent findings suggest that an imbalance between the neuronal chaperone capacity and the production of potentially dangerous polyQ proteins may trigger the onset of polyQ disease.

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Language(s): eng - English
 Dates: 2002-12-10
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41120
ISI: 000179894800007
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Alternative Title : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Pages: - Volume / Issue: 99 (Suppl. 4) Sequence Number: - Start / End Page: 16412 - 16418 Identifier: ISSN: 0027-8424