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Mechanistic approaches to understand the prion-like propagation of aggregates of the human tau protein

Kumar, H and Udgaonkar, JB (2019) Mechanistic approaches to understand the prion-like propagation of aggregates of the human tau protein. In: Biochimica et Biophysica Acta - Proteins and Proteomics, 1867 (10). pp. 922-932.

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Official URL: https://doi.org/10.1016/j.bbapap.2019.04.004


The dynamic nature of the tau protein under physiological conditions is likely to be critical for it to perform its diverse functions inside a cell. Under some conditions, this intrinsically disordered protein assembles into pathogenic aggregates that are self-perpetuating, toxic and infectious in nature. The role of liquid-liquid phase separation in the initiation of the aggregation reaction remains to be delineated. Depending on the nature of the aggregate, its structure, and its localization, neurodegenerative disorders with diverse clinical features are manifested. The prion-like mechanism by which these aggregates propagate and spread across the brain is not well understood. Various factors (PTMs, mutations) have been strongly associated with the pathological aggregates of tau. However, little is known about how these factors modulate the pathological properties linked to aggregation. This review describes the current progress towards understanding the mechanism of propagation of tau aggregates. © 2019 Elsevier B.V.

Item Type: Journal Article
Publication: Biochimica et Biophysica Acta - Proteins and Proteomics
Publisher: Elsevier B.V.
Additional Information: The copyright for this article belongs to Elsevier B.V.
Keywords: amyloid; protein aggregate; tau protein; intrinsically disordered protein; protein aggregate; tau protein, degenerative disease; fibril; human; liquid phase microextraction; Michaelis Menten kinetics; nonhuman; phase separation; prion; priority journal; protein polymorphism; protein structure; protein transport; Review; chemistry; genetics; metabolism; mutation, Humans; Intrinsically Disordered Proteins; Mutation; Prions; Protein Aggregates; tau Proteins
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 05 Jan 2023 10:02
Last Modified: 05 Jan 2023 10:02
URI: https://eprints.iisc.ac.in/id/eprint/78791

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