Ancient signaling pathways lie at the base of the initiation of immunity, serving to transmit signals from Pattern Recognition Receptors (PRRs) to trigger the activation of anti-microbial defenses. All PRRs, which evolved to detect potentially pathogenic microorganisms, operate by following two cellular rules: 1) these receptors must activate cytosolic signaling with extremely fast kinetics (within seconds of ligand binding) 2) these receptors must survey multiple cellular compartments, yet still recruit a common set of signaling proteins to each location. How does a signaling network develop that has properties of near immediate responsiveness, yet the flexibility to signal from multiple locations?

While most research on immune signal transduction focuses on the effector functions of signaling proteins, we are interested in understanding how these proteins are organized in the cytosol to promote both rapid responses and the flexibility of signaling locale. Using the Toll-like Receptor (TLR) and RIG-I like Receptor (RLR) families of PRRs, we seek to explain the operation of cytosolic signaling proteins that function of antibacterial and antiviral immunity.

Current projects in the lab focus on addressing the following problems:

1. How are RLR and TLR signaling proteins delivered to the appropriate cellular locations to promote signal transduction?

2. What are the biochemical properties of RLR and TLR-induced signaling complexes?

3. How is the innate immune response manipulated by bacterial and viral pathogens?