Research Description

The actin cytoskeleton plays an essential role in multiple cellular functions, including cytokinesis, vesicular trafficking and the maintenance of cell shape and polarity. To accomplish these functions, the cytoskeleton undergoes constant remodeling into various forms of structural and functional networks, such as lamellipodia, filopodia, stress fibers and focal adhesions. Remodeling of the cytoskeleton is a tightly regulated process, involving hundreds of actin-binding and signaling proteins. The main focus of the research in our lab is to understand the molecular basis for how protein-protein interaction networks bring together cytoskeleton scaffolding, nucleation, elongation, and signaling proteins to accomplish specific cellular functions.

Our primary research tool is protein X-ray crystallography. The atomic “snapshots” resulting from the X-ray crystal structures of proteins provide a wealth of knowledge, but lack information about the dynamic aspects of protein-protein interactions. To obtain this kind of information we also use a host of other approaches, including mutagenesis, bio-informatics, biophysical and biochemical methods.