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- Anselm Gruber
- Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
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- Daniel Hornburg
- Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
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- Matthias Antonin
- Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
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- Natalie Krahmer
- Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
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- Javier Collado
- Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
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- Miroslava Schaffer
- Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
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- Greta Zubaite
- Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
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- Christian Lüchtenborg
- Heidelberg University Biochemistry Center, 69120 Heidelberg, Germany;
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- Timo Sachsenheimer
- Heidelberg University Biochemistry Center, 69120 Heidelberg, Germany;
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- Britta Brügger
- Heidelberg University Biochemistry Center, 69120 Heidelberg, Germany;
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- Matthias Mann
- Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
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- Wolfgang Baumeister
- Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
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- F. Ulrich Hartl
- Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
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- Mark S. Hipp
- Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
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- Rubén Fernández-Busnadiego
- Department of Structural Molecular Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany;
抄録
<jats:title>Significance</jats:title> <jats:p>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.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 115 (15), 2018-03-26
Proceedings of the National Academy of Sciences