First Advisor
Jeffrey Singer
Date of Award
2014
Document Type
Thesis
Degree Name
Bachelor of Science (B.S.) in Biology and University Honors
Department
Biology
Subjects
Ubiquitin, Protein binding
DOI
10.15760/honors.48
Abstract
Ubiquitination is a fundamental biochemical process, which controls numerous aspects of protein function, such as degradation, protein-protein interaction and sub cellular localization. Cullin 3 (Cul3) is a ubiquitin ligase that is fundamentally responsible for ubiquitination of proteins and plays a critical role in normal cellular processes. Cul3 has been shown to use substrate adaptors to facilitate the ubiquitination process and many of these substrate adaptors contain BTB domains among other protein-protein interacting domains. A novel BTB domain containing protein is Ctb73. Ctb73 has a BACK and Kelch domain along with a BTB domain. It has not been shown whether Ctb73 is a substrate adaptor for Cul3. The purpose of this experiment is to determine whether Ctb73 binds to Cul3 and if so, through which domain.
Rights
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Persistent Identifier
http://archives.pdx.edu/ds/psu/12466
Recommended Citation
Royer, Lacey, "Cul3 Ubiquitin Ligase and Ctb73 Protein Interactions" (2014). University Honors Theses. Paper 101.
https://doi.org/10.15760/honors.48