Regulation of protein phosphatases and the evolution of cellular signaling

Phosphatases and kinases integrate diverse cellular and environmental cues to precisely and rapidly tune the activity of target proteins by controlling their phosphorylation state. We use genetics, cell biology, enzymology and structural biology to determine how protein phosphatases achieve regulation, specificity, and evolutionary flexibility.

The PP2C family of protein serine/threonine phosphatases is widespread (found throughout the bacterial, plant, and animal kingdoms), highly diversified (some species of bacteria and plants have more than 50 and humans have 20), and has broad impact on biology (controlling diverse processes including stress responses, development, and cell growth and death). We study how phosphatases are regulated, what they sense, how they achieve specificity, and how they evolve in both bacterial and mammalian systems.