Date of Presentation
5-2-2024 12:00 AM
College
Rowan-Virtua School of Osteopathic Medicine
Poster Abstract
Regulation of proteasomes is important for adaptation to cellular stress. Previous studies have shown that following starvation stress, proteasomes are targeted for destruction by autophagy. However, how cells control proteasomes in response to nitrogen starvation remains unclear. This study delves into the intricate interplay between Med13, proteaphagy, and stress response regulation, aiming to elucidate their roles in cellular survival mechanisms. It focused on the highly conserved Cdk8 kinase module (CKM) of the Mediator complex a that plays a pivotal involvement in cellular signaling and gene regulation under stress conditions. During the investigation, we asked if the degradation of specific proteasome subunits was dependent upon Med13, a member of the CKM. The results suggest a novel role of Med13 in the degradation of the Rpn8 proteasome subunit, shedding light on its specific impact on proteasome dynamics during stress. Moving forward, the research endeavors to validate and refine these initial findings through further experimentation and analysis. Replication of experiments and additional time courses, particularly focusing on the Rpn11 subunit, are planned to bolster the observed effects of Med13 on specific proteasome subunits. Furthermore, the exploration of Med13's involvement in proteaphagy under different stress conditions, such as carbon starvation, promises to broaden our understanding of stress-induced cellular responses. In conclusion, this research underscores the critical role of Med13 in cellular survival mechanisms during nitrogen starvation and its potential implication in proteasome degradation. These findings contribute significantly to the comprehension of stress response regulation and hold promise for future investigations into proteaphagy and related cellular processes.
Keywords
Proteaphagy, Proteasome dynamics, Autophagy genes, Cell survival, Med13
Disciplines
Laboratory and Basic Science Research | Medical Molecular Biology | Medicine and Health Sciences | Molecular Biology
Document Type
Poster
Included in
Laboratory and Basic Science Research Commons, Medical Molecular Biology Commons, Molecular Biology Commons
The Role of Med13 in Proteaphagy
Regulation of proteasomes is important for adaptation to cellular stress. Previous studies have shown that following starvation stress, proteasomes are targeted for destruction by autophagy. However, how cells control proteasomes in response to nitrogen starvation remains unclear. This study delves into the intricate interplay between Med13, proteaphagy, and stress response regulation, aiming to elucidate their roles in cellular survival mechanisms. It focused on the highly conserved Cdk8 kinase module (CKM) of the Mediator complex a that plays a pivotal involvement in cellular signaling and gene regulation under stress conditions. During the investigation, we asked if the degradation of specific proteasome subunits was dependent upon Med13, a member of the CKM. The results suggest a novel role of Med13 in the degradation of the Rpn8 proteasome subunit, shedding light on its specific impact on proteasome dynamics during stress. Moving forward, the research endeavors to validate and refine these initial findings through further experimentation and analysis. Replication of experiments and additional time courses, particularly focusing on the Rpn11 subunit, are planned to bolster the observed effects of Med13 on specific proteasome subunits. Furthermore, the exploration of Med13's involvement in proteaphagy under different stress conditions, such as carbon starvation, promises to broaden our understanding of stress-induced cellular responses. In conclusion, this research underscores the critical role of Med13 in cellular survival mechanisms during nitrogen starvation and its potential implication in proteasome degradation. These findings contribute significantly to the comprehension of stress response regulation and hold promise for future investigations into proteaphagy and related cellular processes.