Protein degradation, Arabidopsis thaliana, selective protein degradation, cullin ring ligase, ubiquitin, CRL, CRL3
Cell and Developmental Biology | Life Sciences
Protein degradation is a highly regulated process in eukaryotic organisms, and plays a major role in general cell function. One of the key events in selective protein degradation is the addition of ubiquitin (Ub) to the target protein which signals the cell to degrade that protein using the proteasome. This allows the cell to recycle components of proteins that are no longer functioning or necessary for cellular function. E3 ligase protein complexes select specific target proteins for degradation and adds Ub to them, but in order for the E3 ligase complex to become active, Rub (related to ubiquitin) must be covalently ligated to the Cullin protein of the E3 complex. This project investigates the impact that exogenous Abscisic Acid (ABA) has on the ratio of Rubbylated (active) to unRubbylated (inactive) Cullin3 proteins present in Arabidopsis thaliana. Investigating this question allows for further understanding of how a plant's developmental cues can impact its rates of protein degradation.
Baker, Gloria A., "Impact of Abscisic Acid on Rates of Ubiquitin Mediated Selective Protein Degradation in A. thaliana" (2022). Honors Projects. 885.