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Acetylation changes tau interactome to degrade tau in Alzheimer’s disease animal and organoid models

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Title
Acetylation changes tau interactome to degrade tau in Alzheimer’s disease animal and organoid models
Author(s)
Heesun Choi; Haeng Jun Kim; Jinhee Yang; Sehyun Chae; Wonik Lee; Sunwoo Chung; Jisoo Kim; Hyunjung Choi; Hyeseung Song; Chang Kon Lee; Jae Hyun Jun; Yong Jae Lee; Kyunghyeon Lee; Semi Kim; Hye-ri Sim; Young Il Choi; Keun Ho Ryu; Jong-Chan Park; Dongjoon Lee; Sun-Ho Han; Daehee Hwang; Jangbeen Kyung; Inhee Mook-Jung
Publication Date
2020-01
Journal
AGING CELL, v.19, no.1, pp.e13081 -
Publisher
WILEY-BLACKWELL
Abstract
© 2019 The Authors. Aging Cell published by the Anatomical Society and John Wiley & Sons Ltd.Alzheimer's disease (AD) is an age-related neurodegenerative disease. The most common pathological hallmarks are amyloid plaques and neurofibrillary tangles in the brain. In the brains of patients with AD, pathological tau is abnormally accumulated causing neuronal loss, synaptic dysfunction, and cognitive decline. We found a histone deacetylase 6 (HDAC6) inhibitor, CKD-504, changed the tau interactome dramatically to degrade pathological tau not only in AD animal model (ADLPAPT) brains containing both amyloid plaques and neurofibrillary tangles but also in AD patient-derived brain organoids. Acetylated tau recruited chaperone proteins such as Hsp40, Hsp70, and Hsp110, and this complex bound to novel tau E3 ligases including UBE2O and RNF14. This complex degraded pathological tau through proteasomal pathway. We also identified the responsible acetylation sites on tau. These dramatic tau-interactome changes may result in tau degradation, leading to the recovery of synaptic pathology and cognitive decline in the ADLPAPT mice
URI
https://pr.ibs.re.kr/handle/8788114/7266
ISSN
1474-9718
Appears in Collections:
Center for Plant Aging Research (식물 노화·수명 연구단) > Journal Papers (저널논문)
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