Nanometer-scale protein assemblies self organize to shape both crawling and dividing cells. How this occurs is not clear. Therefore, our lab is focused on how the molecular motor driving contractile forces inside of cells, myosin II, assembles. Myosin II-contractility is involved in a whole host of cellular functions required for proper organismal development and the progression of cancer including cell division and cell migration.
Our research is focused on three basic questions: 1) How do the molecular motors generating contractile forces get assembled/disassembled inside of living cells?; 2) How do contractile forces mediate 3-D cellular shape changes during cell motility and cell division?; and 3) How do molecular motors assemble to rebuild contractile systems after cellular injury? To study these problems, my lab uses a combination of high- and super-resolution microscopy, biochemistry, and proteomics. Our ultimate goal is to build a unifying 3-D model of how contractile systems regulate the function of cells in both healthy tissues and during cancer progression.
Super-resolution microscopy techniques used in the Burnette lab: structured illumination microscopy (SIM), photo-activated localization microscopy (PALM), Stochastic Optical Reconstruction Microscopy (STORM) and Scanning Angle Interference Microscopy (SAIM).