The main research objective of our group is to study the complex pathways that are activated in mammalian cells upon their stimulation by growth factors and their role in cancer development. Transduction of signals involved in the regulation of cellular proliferation, differentiation and function in multicellular organisms occurs in many cases through the activation of membrane-spanning receptor protein-tyrosine kinases (RTK). Activation by ligand-binding leads to auto-phosphorylation of receptors, which in turn mediates the formation of specific receptor complexes with several key intracellular signaling enzymes and adaptors, thus producing a variety of second-messengers that propagate further signaling events. These processes require macromolecular interactions that are mediated by conserved functional domains, such as SH2, which interact with phosphotyrosine containing regions, SH3, which bind proline-rich sequences and PH (pleckstrin-homology), which specifically recognize phoshoinositides. Prominent amongst the many signaling cascades initiated by activated growth factor receptors are those involving the phosphoinositide (PI) 3-kinase and the MAP-kinase family of enzymes.
Our laboratory also employs proteomic technologies (mass spectrometry and Biacore biosensor analysis) in order to understand the role of specific signaling pathways in cancer development. Studies in model systems investigate the role of ras mutations, HER2 over-expression and EBV infection in colon cancer progression, breast cancer development and B-lyphocyte transformation, respectively.

We are partners of the TRANSFOG FP6 project.