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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
Identification Of The E3 Ligase That Directs The Degradation Of Proteins That Control Cell Fate Decisions In Yeast, Prasanna Tati, Stephen D Willis, Katrina F. Cooper
Identification Of The E3 Ligase That Directs The Degradation Of Proteins That Control Cell Fate Decisions In Yeast, Prasanna Tati, Stephen D Willis, Katrina F. Cooper
Rowan-Virtua Research Day
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.
Cyclin C Determines Cell Fate In Response To Oxidative Stress And Proteasome Inhibition, David C. Stieg
Cyclin C Determines Cell Fate In Response To Oxidative Stress And Proteasome Inhibition, David C. Stieg
Graduate School of Biomedical Sciences Theses and Dissertations
In response to various sources of cellular stress, the coordination of intracellular events is necessary to elicit the appropriate molecular response. In particular, the reprogramming of gene expression by stress-specific transcription factors drives the activation of signaling pathways, triggering either cell survival or regulated cell death pathways. The Cdk8 kinase module (CKM) is a highly conserved transcriptional regulatory complex with a role in this decision. The CKM is composed of Cdk8, its activating partner cyclin C, and two scaffold proteins, Med12 and Med13. The CKM is a detachable subunit of the Mediator complex, which interacts with RNA polymerase II to …