The Diaphanous-related formin protein family plays a key role in intracellular cytoskeletal regulation. Due to their farreaching importance, these proteins must be highly regulated themselves. With recent exploration of regulatory processes of mDia2, a formin protein found in mammals, the established mechanism of control appears to be more complex than previously thought. This project examines the possibility of phosphorylation at critical sites near the protein regions that regulate formin function. Here, we outline our initial screen for discovering these specific residues within mDia2 and their potential for phosphorylation using site-directed mutagenesis.