Ontology highlight
ABSTRACT:
SUBMITTER: Nachman E
PROVIDER: S-EPMC7363153 | biostudies-literature | 2020 Jul
REPOSITORIES: biostudies-literature
Nachman Eliana E Wentink Anne S AS Madiona Karine K Bousset Luc L Katsinelos Taxiarchis T Allinson Kieren K Kampinga Harm H McEwan William A WA Jahn Thomas R TR Melki Ronald R Mogk Axel A Bukau Bernd B Nussbaum-Krammer Carmen C
The Journal of biological chemistry 20200528 28
The accumulation of amyloid Tau aggregates is implicated in Alzheimer's disease (AD) and other tauopathies. Molecular chaperones are known to maintain protein homeostasis. Here, we show that an ATP-dependent human chaperone system disassembles Tau fibrils <i>in vitro</i> We found that this function is mediated by the core chaperone HSC70, assisted by specific cochaperones, in particular class B J-domain proteins and a heat shock protein 110 (Hsp110)-type nucleotide exchange factor (NEF). The Hsp ...[more]