Molecular-level interplay between intrinsically disordered clients and Hsp90.
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| Název: | Molecular-level interplay between intrinsically disordered clients and Hsp90. |
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| Autoři: | Ramirez, Lisa Marie, Zweckstetter, Markus |
| Zdroj: | Current opinion in chemical biology 74, 102304 (2023). doi:10.1016/j.cbpa.2023.102304 |
| Informace o vydavateli: | Current Biology Ltd. |
| Rok vydání: | 2023 |
| Témata: | info:eu-repo/classification/ddc/570, Humans, HSP90 Heat-Shock Proteins: metabolism, Molecular Chaperones, Proteostasis, Intrinsically Disordered Proteins: metabolism, Neurodegenerative Diseases, Alzheimer's disease, Heat shock protein, Hsp90, Structure, Tau, α-Synuclein |
| Geografické téma: | DE |
| Popis: | 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. |
| Druh dokumentu: | article in journal/newspaper |
| Jazyk: | English |
| Relation: | info:eu-repo/semantics/altIdentifier/issn/1879-0402; info:eu-repo/semantics/altIdentifier/issn/1367-5931; info:eu-repo/semantics/altIdentifier/pmid/pmid:37068388; https://pub.dzne.de/record/257684 |
| Dostupnost: | https://pub.dzne.de/record/257684 https://pub.dzne.de/search?p=id:%22DZNE-2023-00481%22 |
| Rights: | info:eu-repo/semantics/closedAccess |
| Přístupové číslo: | edsbas.125AFEB6 |
| Databáze: | BASE |
Nájsť tento článok vo Web of Science | Abstrakt: | 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. |
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