TY  - JOUR
AU  - Ramirez, Lisa Marie
AU  - Zweckstetter, Markus
TI  - Molecular-level interplay between intrinsically disordered clients and Hsp90.
JO  - Current opinion in chemical biology
VL  - 74
SN  - 1367-5931
CY  - London
PB  - Current Biology Ltd.
M1  - DZNE-2023-00481
SP  - 102304
PY  - 2023
AB  - 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.
KW  - Humans
KW  - HSP90 Heat-Shock Proteins: metabolism
KW  - Molecular Chaperones
KW  - Proteostasis
KW  - Intrinsically Disordered Proteins: metabolism
KW  - Neurodegenerative Diseases
KW  - α-Synuclein (Other)
KW  - α-Synuclein (Other)
KW  - Alzheimer's disease (Other)
KW  - Heat shock protein (Other)
KW  - Hsp90 (Other)
KW  - Structure (Other)
KW  - Tau (Other)
KW  - α-Synuclein (Other)
KW  - HSP90 Heat-Shock Proteins (NLM Chemicals)
KW  - Molecular Chaperones (NLM Chemicals)
KW  - Intrinsically Disordered Proteins (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:37068388
DO  - DOI:10.1016/j.cbpa.2023.102304
UR  - https://pub.dzne.de/record/257684
ER  -