A major goal in the lab is to develop novel biochemical reconstitutions of signaling pathways using purified recombinant proteins on supported lipid bilayers. These reconstituted experimental systems are powerful tools for understanding how molecules self-assemble, identifying the minimum set of molecules sufficient for activity, and uncovering new hypotheses to test in cells. 

Mechanical forces and the material property of the environment have profound effects on cell behavior during development, differentiation, and adult physiology. Mechanotransduction is the molecular process by which cells sense and respond to mechanical signals in their environment. Abnormal mechanotransduction can lead to many human diseases including asthma, heart failure, osteoporosis, and cancer. Integrin receptors are critical regulators of mechanotransduction at the plasma membrane. We seek to identify molecules that regulate integrin-dependent mechanotransduction and understand the mechanisms by which integrin clusters respond to changing mechanical signals. 

Liquid-liquid phase separation has emerged as an important mechanism for promoting higher-order molecular assembly in cells. Interactions between multivalent biomolecules can promote the formation of liquid-like droplets that concentrate a specific subset of molecules. We’ve found that many signaling molecules, including actin regulatory proteins and kinases, undergo phase separation in vitro. We seek to understand whether phase separation regulates the activity of these signaling molecules. Furthermore, since phase separation is highly dependent on concentration, we hypothesize that overexpression of these proteins in cancer may drive the aberrant formation of phase-separated signaling puncta.