Molecular and structural architecture of polyQ aggregates in yeast

Medientyp: E-Artikel

Titel: Molecular and structural architecture of polyQ aggregates in yeast

Beteiligte: Gruber, Anselm; Hornburg, Daniel; Antonin, Matthias; Krahmer, Natalie; Collado, Javier; Schaffer, Miroslava; Zubaite, Greta; Lüchtenborg, Christian; Sachsenheimer, Timo; Brügger, Britta; Mann, Matthias; Baumeister, Wolfgang; Hartl, F. Ulrich; Hipp, Mark S.; Fernández-Busnadiego, Rubén

Erschienen: Proceedings of the National Academy of Sciences, 2018

Sprache: Englisch

DOI: 10.1073/pnas.1717978115

ISSN: 0027-8424; 1091-6490

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Beschreibung: Significance How protein aggregation leads to neurodegenerative disorders such as Huntington’s disease remains poorly understood. Here we show that polyglutamine (polyQ) aggregation in yeast results in the formation of amorphous inclusions and less frequent fibrils. This is accompanied by significant changes in proteome composition as well as distortions in mitochondria and lipid droplet morphology that do not arise from direct interactions of these organelles with polyQ inclusions or fibrils. This contrasts with recent observations in mammalian cells, where the same polyQ proteins formed amyloid-like fibrils that distort endoplasmic reticulum membranes. These results demonstrate that the same polyQ expansion protein can adopt different nonnative conformations that utilize distinct mechanisms to target a variety of cellular structures.

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