[정기세미나] 2024학년도 1학기 생명과학과 7차 세미나
- -연사 : 장재락 교수 (아주대학교 의과대학)
- -연제 : Molecular mechanisms of autophagic clearance associated with Alzheimer's disease
- -일시 : 2024.06.03 (월) 10:30 ~
- -장소 : 시대융합관-B12호
첨부파일 (2개)
- 장재락 교수님_Abstract.pdf (104.9 KB)
- 장재락 교수님_CV.pdf (244.7 KB)
Tripartite motif (TRIM) proteins, a large family of E3 ubiquitin ligases, are implicated in various cellular processes, including antiviral defense, tumorigenesis, and protein quality control. While TRIM proteins are known to regulate the ubiquitin-proteasome system, endoplasmic reticulum-associated degradation, and autophagy, the precise mechanisms by which they modulate downstream events remain elusive. In this study, we uncovered a novel role for TRIM22 in the regulation of autophagy. Our findings demonstrated that TRIM22 facilitates autophagosome-lysosome fusion by mediating the interaction between GABARAP family proteins and PLEKHM1, thereby promoting the autophagic clearance of protein aggregates. Notably, this function is independent of TRIM22's E3 ubiquitin ligase activity. Furthermore, we identified a TRIM22 variant associated with early-onset familial Alzheimer's disease that disrupts autophagosome-lysosome fusion and impairs autophagic clearance. These findings highlight TRIM22 as a critical regulator of autophagy, orchestrating autophagosome-lysosome fusion by scaffolding key autophagy-related proteins. Our work suggests that TRIM22 may serve as a potential therapeutic target in neurodegenerative diseases characterized by impaired autophagic clearance, such as Alzheimer's disease.
첨부파일 (2개)
- 장재락 교수님_Abstract.pdf (104.9 KB)
- 장재락 교수님_CV.pdf (244.7 KB)
