The cell surface may be considered as a multi-component composite- an asymmetric lipid bilayer sandwiched between a thin actomyosin cortex and an extracellular matrix. The lipid membrane itself has rich compositional diversity, consisting of a variety of lipids and proteins. In my talk I will provide an overview of how different myosin motors in conjunction with actin dynamics pattern the membrane bilayer into forming distinct domains of specific chemical composition and properties. I will then focus on how the actomyosin cortex subjects diverse transmembrane protein receptors to cortical actin flows, resulting in their sorting based on the affinity of these proteins for the actin cytoskeleton. 

Insights both from theory and validation from our in vitro experiments show that actomyosin activity drives the nano and mesoscale segregation of the distinct actin-binding domains based on their kinetics of (un)binding to actin filaments, emphasizing a new sorting property of this active interface.