cancer, cytoskeleton, cell division, phosphorylation events
Cancer is a disease of improper and uncontrolled cell division. Both human and fission yeast cells divide using an actomyosin ring which constricts to physically divide the cell in two, making fission yeast an ideal model for understanding this process. The scaffolding protein, Mid1, is essential for medial placement of the contractile ring; cells lacking Mid1 form disorganized rings and divide asymmetrically. Our previous research has shown multiple intracellular kinases directly phosphorylate Mid1. This project illuminates the role of these phosphorylation events. To understand phospho-regulation of Mid1, phosphorylation sites are mutated to prevent modification by such kinases. Mid1 mutants divide faster than wild-type cells. However, when treated with cytoskeletal destabilizing agents the cells cannot continue with division. Current studies focus on highlighting the role of specific phosphorylation sites and the effects of compromising the cytoskeleton in mutant cells.
Phelan, Jennifer, "Phospho-regulation of the Anillin-related Scaffolding Protein, Mid1" (2011). Honors Projects. Paper 106.