Speaker
Description
In many signaling pathways, receptors are spatially organized at the plasma membrane into signaling clusters with a specific composition. Phase separation driven by protein interactions can promote clustering of many types of receptors, including the LAT receptor, Nephrin receptor, and integrin receptor. We use biochemical reconstitutions and cellular experiments to study compositionally complex phase separated signaling clusters. Through recent studies of the cell-cell adhesion receptor nephrin and the cell-matrix adhesion receptor integrin, we’ve gained insight into how phase separation promotes receptor clustering and the ways in which membranes can influence phase separation. Additionally, we’ve found that molecular activity can be regulated by phase separation. Arp2/3-dependent actin polymerization and kinase autophosphorylation are both dramatically increased in phase-separated compartments. Thus, phase separation can contribute to molecular organization and the regulation of signaling pathways at the plasma membrane. However, many questions remain about how classical physical theories can be applied to understand the multicomponent, heterogenous, and often nonequilibrium cellular phase separation.
