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Title: Aggregation-prone proteins modulate huntingtin inclusion body formation in yeast
Authors: Kantcheva, Ralitsa B.
Mason, Robert
Giorgini, Flaviano
First Published: 23-Apr-2014
Publisher: Public Library of Science
Citation: PLoS Currents , 2014, 6(1)
Abstract: Huntington's disease (HD) is a fatal neurodegenerative disorder caused by a polyglutamine expansion in the huntingtin (HTT) protein. The expression of mutant HTT in the baker's yeast Saccharomyces cerevisiae recapitulates many of the cellular phenotypes observed in mammalian HD models. Mutant HTT aggregation and toxicity in yeast is influenced by the presence of the Rnq1p and Sup35p prions, as well as other glutamine/asparagine-rich aggregation-prone proteins. Here we investigated the ability of a subset of these proteins to modulate mutant HTT aggregation and to substitute for the prion form of Rnq1p. We find that overexpression of either the putative prion Ybr016wp or the Sup35p prion restores aggregation of mutant HTT in yeast cells lacking the Rnq1p prion. These results indicate that an interchangeable suite of aggregation-prone proteins regulates mutant HTT aggregation dynamics in yeast, which may have implications for mutant HTT aggregation in human cells.
DOI Link: 10.1371/currents.hd.501008f3051342c9a5c0cd0f3a5bf3a4
eISSN: 2157-3999
Version: Publisher Version
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2014, the authors. Available under the terms of the Creative Commons Attribution License ( ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Appears in Collections:Published Articles, Dept. of Genetics

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