My research seeks to understand transformations of the actin cytoskeleton that occur in both normal and invasive motility. Of particular interest are the strategies employed by actin binding proteins to promote invasive cell motility associated with metastatic cancer progression. The majority of my laboratory’s efforts are directed at defining the molecular mechanisms involving regulation of F-actin structures by palladin. We use a multi-disciplinary approach that combines biochemistry, mutagenesis, structural biology, and single molecule microscopy to study these problems from the molecular to cellular level. Our work includes defining the structure and function of individual purified proteins and reconstituting more complex multi-component activities and interactions. The Beck Lab also thrives to understand protein function in the context of living cells through multiple collaborations with cell biologists.
