Emily Levenson

SMAD4 is member of the TGF-B superfamily of proteins and a large portion of its interaction is  when it binds in a homo- or heteromeric complex with other SMADs. This protein complex transports to the nucleus where it interacts with transcriptional activators. Through this pathway, SMAD4 is involved in many cell functions such as cell differentiation, growth, adhesion, migration, and apoptosis. When mutated, the SMAD complex becomes inactivated and can result in cancer such as pancreatic, head and neck, and colorectal as well as other conditions like juvenile poplyposis and hereditary hemorrhagic telangiectasia. My research focuses on the binding interface between SMAD4 and its SMAD counterpart in order to see how natural occuring mutants affect the protein's dimerization.