Biology Department Seminar
"Diversity & Specificity in Protein Ubiquitination: The BRCA1/BARD1 Paradigm"
Presented by Rachel Klevit, Department of Biochemistry, University of Washington, Seattle, WA
Tuesday, April 21, 2009, 1:30 pm — Large Conference Room, Bldg. 490
Protein ubiquitination is carried out by a trio of enzyme activities, known as E1, E2, and E3. The human genome encodes 1-2 ubiquitin-activating (E1) enzymes, several dozen ubiquitin-conjugating (E2) enzymes, and perhaps a thousand ubiquitin (E3) ligases. While such a hierarchy implies that numerous E3s must be recognized by a given E2, it is now clear that the reciprocal is also true, that is, that a single E3 can recognize multiple E2s. This relationship begs the question, What dictates the function of an E2/E3 enzyme pair? Studies on the structure and function of the breast cancer-associated E3 ligase, BRCA1/BARD1, and its interactions with E2s and substrates provide insights into the diverse repertoire of ubiquitinated products and their cellular consequences.
Hosted by: Carl Anderson
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