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Differential effects of soluble and aggregating polyQ proteins on cytotoxicity and type-1 myosin-dependent endocytosis in yeast

Journal article
Authors Lisa Larsson Berglund
Xinxin Hao
Beidong Liu
Julie Grantham
Thomas Nyström
Published in Scientific Reports
Volume 7
ISSN 2045-2322
Publication year 2017
Published at Institute of Biomedicine, Department of Microbiology and Immunology
Department of Chemistry and Molecular Biology
Language en
Links doi.org/10.1038/s41598-017-11102-6
Keywords proline-rich region, huntington-disease, saccharomyces-cerevisiae, chaperone proteins, actin cytoskeleton, mutant huntingtin, cag repeat, gene, toxicity, domains
Subject categories Cancer and Oncology

Abstract

Huntington's disease develops when the polyglutamine (polyQ) repeat in the Huntingtin (Htt) protein is expanded to over 35 glutamines rendering it aggregation-prone. Here, using Htt exon-1 as a polyQ model protein in a genome-wide screen in yeast, we show that the normal and soluble Htt exon-1 is toxic in cells with defects in type-1 myosin-dependent endocytosis. The toxicity of Htt is linked to physical interactions with type-1 myosins, which occur via the Htt proline-rich region, leading to a reduction in actin patch polarization and clathrin-dependent endocytosis. An expansion of the polyQ stretch from 25 to 103 glutamines, which causes Htt aggregation, alleviated Htt toxicity in cells lacking Myo5 or other components involved in early endocytosis. The data suggest that the proline-rich stretch of Htt interacts with type-1 myosin/clathrin-dependent processes and demonstrate that a reduction in the activity of such processes may result in a positive selection for polyQ expansions.

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