|Research Group Leader:||Yvonne Groemping|
|Phone:||+49 7071 601-340|
|Fax:||+49 7071 601-349|
The process of transduction of an extracellular signal from the plasma membrane to specific sites inside the cell requires the controlled formation of multi protein networks. Crucial for the formation of such networks are reversible protein-protein interactions. Adaptor and scaffold proteins play an important role in facilitating and protein-protein interactions and thus the formation of protein networks. These classes of proteins can recruit binding partners to a specific location and regulate interactions between different signal transduction proteins. Adaptor proteins usually consist of different protein-protein and protein-lipid interaction modules like the SH (src homology) 2 and 3 domains that bind a short target sequence within the binding partner. Lipid-interaction modules like the PH (pleckstrin homology) or PX (phox homology) domains bind phosphatidylinositides and determine the localizations of the adaptor protein. By this means adaptor proteins can amplify a receptor-mediated signal and facilitate coupling of the signal to different signal transduction pathways.
We are interested in how these adaptor proteins function to interact with different binding partners in the process of signal transduction and endocytosis. We use a wide range of methods such as molecular biology, fluorescence spectroscopy, microcalorimetry and structural techniques like x-ray crystallography. Aim of our research is to understand the coordination of different signal transduction pathways and principles of substrate recognition and specificity of adaptor proteins.