Adam Rudner

• In-person event
• 4440Q, Carleton Technology and Training Centre, Carleton University
• 1125 Colonel By Drive, Ottawa, ON, K1S 5B6

• Contact
• Owen Rowland, owen.rowland@carleton.ca

Regulation of Anaphase Onset

Adam Rudner, Ottawa Institute of Systems Biology, Univ. of Ottawa

Faculty Host: Owen Rowland

Cancer • Chromosomal disorders • Proteins • Yeast • Cellular Proteomics

The exit from mitosis in eukaryotes is triggered by the regulated destruction of anaphase regulators by the Anaphase Promoting Complex (APC), a multi-subunit ubiquitin ligase. In yeast, the APC is composed of thirteen subunits and its activity is regulated by the binding of activating subunits, the presentation of its substrates, and by its phosphorylation. The cyclin dependent kinase, Cdk1, phosphorylates the APC and this phosphorylation is required for its activation during mitosis. In an effort to determine if phosphorylation regulates other aspects of APC function we are determining the complete phosphoproteome of the APC using mass spectrometry. To date we have identified many new phosphorylation sites on eight of the thirteen subunits. We are now using stable isotope labeling by amino acids in cell culture (SILAC) and absolute quantification (AQUA) to identify which sites are regulated during the cell cycle and in response to changes in cell physiology, as well to determine which kinases and phosphatases regulate APC phosphorylation.