The HSP40 family chaperone isoform DNAJB6b prevents neuronal cells from tau aggregation
Journal
BMC biology
Journal Volume
21
Journal Volume
21
Journal Issue
1
Journal Issue
1
Pages
293
Start Page
293
ISSN
17417007
Date Issued
2023-12-18
Author(s)
Chang, Ya-Lan
Yang, Chan-Chih
Huang, Yun-Yu
Chen, Yi-An
Yang, Chia-Wei
Liao, Chia-Yu
Li, Hsun
Abstract
Alzheimer's disease (AD) is the most common neurodegenerative disorder with clinical presentations of progressive cognitive and memory deterioration. The pathologic hallmarks of AD include tau neurofibrillary tangles and amyloid plaque depositions in the hippocampus and associated neocortex. The neuronal aggregated tau observed in AD cells suggests that the protein folding problem is a major cause of AD. J-domain-containing proteins (JDPs) are the largest family of cochaperones, which play a vital role in specifying and directing HSP70 chaperone functions. JDPs bind substrates and deliver them to HSP70. The association of JDP and HSP70 opens the substrate-binding domain of HSP70 to help the loading of the clients. However, in the initial HSP70 cycle, which JDP delivers tau to the HSP70 system in neuronal cells remains unclear.
Subjects
Alzheimer’s disease; Cochaperone; DNAJB6b; J-domain proteins; Tau
SDGs
Type
journal article