Journal Article (Review Article) DZNE-2023-00481

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Molecular-level interplay between intrinsically disordered clients and Hsp90.

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2023
Current Biology Ltd. London

Current opinion in chemical biology 74, 102304 () [10.1016/j.cbpa.2023.102304]

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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.

Keyword(s): Humans (MeSH) ; HSP90 Heat-Shock Proteins: metabolism (MeSH) ; Molecular Chaperones (MeSH) ; Proteostasis (MeSH) ; Intrinsically Disordered Proteins: metabolism (MeSH) ; Neurodegenerative Diseases (MeSH) ; α-Synuclein ; α-Synuclein ; Alzheimer's disease ; Heat shock protein ; Hsp90 ; Structure ; Tau ; α-Synuclein ; HSP90 Heat-Shock Proteins ; Molecular Chaperones ; Intrinsically Disordered Proteins

Classification:

Contributing Institute(s):
  1. Translational Structural Biology (AG Zweckstetter)
Research Program(s):
  1. 352 - Disease Mechanisms (POF4-352) (POF4-352)

Appears in the scientific report 2023
Database coverage:
Medline ; BIOSIS Previews ; BIOSIS Reviews Reports And Meetings ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Ebsco Academic Search ; Essential Science Indicators ; IF >= 5 ; JCR ; NationallizenzNationallizenz ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
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Institute Collections > GÖ DZNE > GÖ DZNE-AG Zweckstetter
Document types > Articles > Journal Article
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 Record created 2023-04-24, last modified 2025-04-11


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