Anastasia Mylona

Protein phosphorylation is an important post-translational protein modification and a major regulatory mechanism of cellular signaling.  Deregulation of phosphorylation pathways commonly underlies disease aetiology. Proteins often get phosphorylated not only at one but at multiple sites by a single protein kinase. Multisite phosphorylation is a key regulatory mechanism in many cellular processes, and has been suggested to provide a precise tool to generate complex functional outputs from single kinase signaling inputs. Our research vision is to understand the mechanism and functional role of multisite phosphorylation in physiology and disease. In particular, we want to understand how multisite phosphorylation controls the activity of transcriptional regulators and subsequently the final biological response and how it can alter the architecture of signaling pathways in diseases like cancer, which may pave the way for novel treatments. For that purpose, we use a novel multidisciplinary methodology pipeline combining structural (time-resolved NMR, X-ray crystallography), biochemical and cell-based in vivo experimental strategies.