Abstract
Cellular processes rely on interactions between the lipid membrane, membrane-binding proteins, and intracellular components above the membrane. Specifically, it is known that membrane-bound proteins interact with the cytoskeleton to drive anaphase during cell division and cellular movement. The mechanism underlying these interactions occur and the factors affecting them are still unknown. To better understand the chemo-mechanical coupling of membrane-binding proteins with the cytoskeleton, I study how Min proteins from E. Coli self-organize in the presence of a reconstituted cytoskeleton in vitro. The Min protein system is a chemical reaction-diffusion system that forms patterns, including spots and traveling waves, on a lipid membrane. I study the interactions of Min proteins with the cytoskeleton, using the microtubule-kinesin gliding assay. I observed that the Min protein spots pattern becomes smaller and spiky with the presence of other proteins on the membrane, and that Min proteins can direct microtubule gliding around Min patterns. These results suggest that the self-organization of membrane-binding proteins and the activity of the cytoskeleton are affected by each other. The in vitro characterization of interactions between membrane-bound Min and cytoskeletal microtubules furthers our ability to reconstitute the cell from bottom-up, helping us better understand the mechanisms behind complex cellular processes.