Ubiquitin ligase and deubiquitin enzyme in Alzheimer's disease function study
- VernacularTitle:泛素连接酶和去泛素化酶在阿尔茨海默病中的作用研究
- Author:
Yu-qing WANG
1
;
Zhi-tao HOU
1
;
Song-zhe LI
1
;
Zhi-hua HAO
1
;
Jing CHEN
1
Author Information
- Publication Type:Journal Article
- Keywords: Alzheimer's disease; beta-amyloid protein; Tau protein; ubiquitination; ubiquitin ligases; deubiquitylases
- From: Chinese Pharmacological Bulletin 2025;41(3):427-433
- CountryChina
- Language:Chinese
- Abstract: Alzheimer's disease(AD)is a multifactorial condi-tion characterized by the accumulation of toxic proteins and asso-ciated neurodegeneration.AD is distinguished by the pathologi-cal aggregation of amyloid beta(Aβ)and Tau proteins.The in-teraction between Aβ and Tau can further induce neuroinflamma-tion,mitochondrial autophagy dysfunction,and endoplasmic retic-ulum stress,exacerbating synaptic damage and neuronal death.Neuronal cells are particularly susceptible to protein misfolding due to an imbalance between protein production and degrada-tion.The ubiquitin/26S proteasome system(UPS),a major pathway for protein degradation in eukaryotic cells,plays a cruci-al role in recognizing misfolded or damaged proteins within the nervous system.In UPS,the levels of ubiquitin are tightly regu-lated by both ubiquitin ligases(E3s)and deubiquitylases(DUBs).This article reviews the involvement and mechanisms of E3s and DUBs in the pathogenesis of AD,aiming to provide novel research strategies for its treatment.
