Title: Investigating Multimodal Activation of Cellular Signaling Pathways Through Lipids

Abstract: Key signaling molecules, receptor tyrosine kinases (RTKs) are a clinically important family of receptors that act as key regulators of a wide range of biological functions and as such, play a role in the development of various diseases. All RTKs are membrane proteins that share a single-pass transmembrane helix that links and extracellular domain with an intracellular kinase domain. Structurally, how a single helix promotes the large diversity of signaling processes mediated by RTKs has long been a question of interest, and classically, RTKs are considered to be activated by ligand-induced dimerization. However, in recent years it has become clear that RTKs utilize a wide variety of mechanisms to promote activation and signaling and a subfamily of RTKs, TAM receptors, appear to have unique requirements for activation and offer a great system to study some of these alternative mechanisms. Preliminary data from my lab suggests that TAM receptors are capable of forming ligand-independent dimers and may form high order oligomers, or clusters, during activation that are driven by interactions with membrane lipids. My lab works to gain new insights from cellular and structural studies into the dependence of TAM receptors on the membrane lipid, phosphatidylserine, in the activation of TAM receptors and other important drivers of cellular phagocytosis during signaling.

Host: Christa Baker