Biology is largely controlled by proteins, which are the products of gene expression. Much of our understanding of how proteins mediate biological function and disease comes from three-dimensional structures of stable folded proteins. But more than 60 per cent of proteins contain intrinsically disordered regions (IDRs) that lack folded domains. IDRs are more common in disease-associated proteins and play a critical role in regulatory processes, yet they remain poorly understood.
To shine a light on IDR function, Dr. Julie Forman-Key, Canada Research Chair in Intrinsically Disordered Proteins, is studying the EWS-FLI1 fusion protein, which is associated with cancer development. She and her research team are defining the roles of IDRs and intrinsically disordered proteins in autism spectrum disorder. They are also creating bioinformatic tools for IDR function and disease mutations and applying them to the disorder. Their research will provide insights into how EWS-FLI1 and autism spectrum disorder variants lead to pathology.