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Thesis

In Situ Architecture and Cellular Interactions of PolyQ Inclusions

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Bäuerlein,  Felix Jan Benedict
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Bäuerlein, F. J. B. (2018). In Situ Architecture and Cellular Interactions of PolyQ Inclusions. PhD Thesis, Technische Universität, Fakultät für Physik, München.


Cite as: https://hdl.handle.net/21.11116/0000-0003-B907-5
Abstract
Expression of many disease-related aggregation-prone proteins results in cytotoxicity and the formation of large intracellular inclusion bodies (IBs). To gain insight into the role of IBs in pathology and their in situ structure inside cells, we employed advanced cryo-electron tomography methods and analyzed IBs formed by polyglutamine-expanded huntingtin exon 1 within their intact cellular context in mouse neurons and human cells. Interactions with IBs' fibrils lead to membrane deformation, the local impairment of ER organization, and profound alterations in ER membrane dynamics and thus contribute to the deleterious cellular effects of protein aggregation.