My lab combines biochemical and structural techniques to study kinases and phosphatases that produce soluble inositol phosphate (IP) and membrane-bound phosphatidylinositol (PI) signals in cells. Inositol-based signalling is ubiquitous in human cells and its dysregulation has been linked with disease states. Our goal is to understand how these kinases and phosphatases produce highly specific inositol signals and how they elicit their effects in cells. To do this, we study the structures of IP- and PI- kinases and phosphatases, their catalytic mechanisms, and how their actions are regulated in the cell. We use x-ray crystallography to determine high-resolution structures of these enzymes and protein engineering to correlate the structure of each enzyme with its catalytic function and their downstream effects. Using these approaches we generate a clear understanding of the functions of these kinases and phosphatases and we also obtain high-resolution structures to facilitate inhibitor design efforts to target inositol-based signalling networks.