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Molecular-level interplay between intrinsically disordered clients and Hsp90

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

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Citation

Ramirez, L., & Zweckstetter, M. (2023). Molecular-level interplay between intrinsically disordered clients and Hsp90. Current Opinion in Chemical Biology, 74: 102304. doi:10.1016/j.cbpa.2023.102304.


Cite as: https://hdl.handle.net/21.11116/0000-000D-07D3-D
Abstract
Proteostasis is maintained by a network of molecular chaperones, a prominent member of which is the 90-kilodalton heat shock protein Hsp90. The chaperone function of Hsp90 has been extensively reviewed previously, emphasizing its ATPase activity and remodeling of folded client proteins. Experimental evidence implicating Hsp90 in neurodegenerative diseases has bolstered interest in the noncanonical chaperoning of intrinsically disordered protein (IDPs), however the interplay between Hsp90 and its disordered clients remains poorly understood. In this review we describe recent advances that have contributed to our understanding of the intricate mechanisms characterizing Hsp90-mediated chaperoning of the IDPs tau and α-synuclein and survey emerging insights into the modulation of the chaperone-client interplay in the context of neurodegeneration.