Mutational Analysis of the Interactions between the Cytoskeletal Protein WHAMM and Membranes
My research project involves investigating a cytoskeletal protein named WHAMM- WASP homolog associated with actin, membranes, and microtubules. The cytoskeleton is a crucial component of the cell that facilitates protein transportation, structural support, and ultimately the movement and division of cells. It does so through actin polymerization, which is the formation of filaments using actin molecules. An important stimulator of actin polymerization is the Arp 2/3 complex. It is regulated by nucleation-promoting factors, one such example being WHAMM. My project focuses primarily on the WMD domain of WHAMM, which is responsible for the proteins binding to phospholipids on membranes. Using computational studies, I will deduce which residues are essential for membrane binding. I will then introduce point mutations at these sites using biochemical experiments to verify if the membrane binding ability of WHAMM has been abolished. In doing so, I explore the specifics of how WHAMM targets proteins to specific organelles in cells.
Message to Sponsor
- Major: Molecular & Cell Biology, Applied Mathematics
- Mentor: Matthew Welch, Molecular & Cell Biology