Phospho-regulation of the Scaffolding Protein Mid1

Presentation Type

Poster/Portfolio

Presenter Major(s)

Cell and Molecular Biology

Mentor Information

Dawn Clifford Hart, hartdaw@gvsu.edu

Department

Cell and Molecular Biology

Location

Henry Hall Atrium 27

Start Date

13-4-2011 4:00 PM

End Date

13-4-2011 5:00 PM

Keywords

Life Science

Abstract

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.

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Apr 13th, 4:00 PM Apr 13th, 5:00 PM

Phospho-regulation of the Scaffolding Protein Mid1

Henry Hall Atrium 27

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.