Date of Presentation
5-6-2021 12:00 AM
College
School of Osteopathic Medicine
Poster Abstract
The ubiquitin–proteasome system (UPS) and autophagy pathways are distinct, highly conserved proteolytic systems that play important roles in maintaining cellular homeostasis in response to environmental cues [1]. The goal of this project is to identify the E3 ligase that mediates the degradation of cyclin C following nitrogen starvation in yeast using quantitative Western blot analysis of cyclin C-myc following nitrogen starvation in mutants of known Ubc4/5 interacting E3 ligases. No potential E3 ligases were identified as stable after 4 hours of nitrogen starvation, suggesting redundancy in function.
Keywords
yeasts, Cyclin C, ligases, E3, nitrogen starvation
Disciplines
Cell Biology | Medical Cell Biology | Medical Microbiology | Medicine and Health Sciences | Molecular Biology | Physiological Processes
Document Type
Poster
Included in
Cell Biology Commons, Medical Cell Biology Commons, Medical Microbiology Commons, Molecular Biology Commons, Physiological Processes Commons
Identification of the E3 Ligase that Directs the Degradation of Proteins that Control Cell Fate Decisions in Yeast
The ubiquitin–proteasome system (UPS) and autophagy pathways are distinct, highly conserved proteolytic systems that play important roles in maintaining cellular homeostasis in response to environmental cues [1]. The goal of this project is to identify the E3 ligase that mediates the degradation of cyclin C following nitrogen starvation in yeast using quantitative Western blot analysis of cyclin C-myc following nitrogen starvation in mutants of known Ubc4/5 interacting E3 ligases. No potential E3 ligases were identified as stable after 4 hours of nitrogen starvation, suggesting redundancy in function.