Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties

Despite the strong evidence linking the aggregation of the Huntingtin protein (Htt) to the pathogenesis of Huntington’s disease (HD), the mechanisms underlying Htt aggregation and neurodegeneration remain poorly understood. Herein, we investigated the ultrastructural properties and protein compositi...

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Bibliographic Details
Published in:	Nature communications Vol. 12; no. 1; pp. 6579 - 27
Main Authors:	Riguet, Nathan, Mahul-Mellier, Anne-Laure, Maharjan, Niran, Burtscher, Johannes, Croisier, Marie, Knott, Graham, Hastings, Janna, Patin, Alice, Reiterer, Veronika, Farhan, Hesso, Nasarov, Sergey, Lashuel, Hilal A.
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 12.11.2021 Nature Publishing Group Nature Portfolio
Subjects:	14/19 14/28 14/35 631/378/1689/1558 631/80/470/2284 82/29 82/58 96/109 Agglomeration Animals Biochemical composition Biochemistry Cell Nucleus - metabolism Composition Cytoplasm - metabolism Cytoskeleton HEK293 Cells Humanities and Social Sciences Humans Huntingtin Huntingtin Protein - chemistry Huntingtin Protein - genetics Huntingtin Protein - metabolism Huntingtin Protein - ultrastructure Huntington Disease - metabolism Huntington's disease Huntingtons disease Inclusion bodies Inclusions Intranuclear Inclusion Bodies - metabolism Lipids Mammalian cells Mice Mice, Inbred C57BL multidisciplinary Neurodegeneration Neurons - metabolism Organelles Pathogenesis Peptides - chemistry Polyglutamine Protein Aggregation, Pathological Protein composition Proteins Proteome Quality control Science Science (multidisciplinary) Toxicity
ISSN:	2041-1723, 2041-1723
Online Access:	Get full text
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