Role of aberrant phase separation in pathological protein aggregation

Chakraborty, Pijush; Zweckstetter, Markus

doi:10.1016/j.sbi.2023.102678

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Role of aberrant phase separation in pathological protein aggregation

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Chakraborty, Pijush
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;
Research Group of Protein Structure Determination using NMR, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Zweckstetter, Markus
Department of NMR Based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;
Research Group of Protein Structure Determination using NMR, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Citation

Chakraborty, P., & Zweckstetter, M. (2023). Role of aberrant phase separation in pathological protein aggregation. Current Opinion in Structural Biology, 82: 102678. doi:10.1016/j.sbi.2023.102678.

Cite as: https://hdl.handle.net/21.11116/0000-000D-BFD0-1

Abstract

Neurodegenerative diseases are associated with the pathological deposition of many different intrinsically disordered proteins or proteins with intrinsically disordered regions. Recent evidence suggests that these proteins can undergo liquid-liquid phase separation and also form membrane-less organelles in cells. Additionally, the biomolecular condensates formed by these proteins may undergo liquid-to-solid phase transition thereby maturating to amyloid fibrils, oligomeric species, or amorphous aggregates and contributing to the pathology of several neurodegenerative diseases. Here we discuss the role of phase separation of the neuronal proteins tau, α-synuclein, fused in sarcoma (FUS), and the transactive response DNA-binding protein of 43 kDa (TDP-43) that are associated with neurodegeneration in the context of pathological protein aggregation.