Structural Biology of Cell Migration
We are using cell biology and advanced correlative light and cryo-electron microscopy methods to study the structure and function of protein complexes in situ. Specifically, we are interested in the organization and structure of the actin cytoskeleton, the key player in the ability of cells to move. We also study the reciprocal interactions between migratory cells and their three-dimensional environment. If you want to know more about why and how we do it click here
Describing the protein interactions that form pleomorphic and asymmetric viruses represents a considerable challenge to most structural biology techniques. Obtaining a detailed understanding of these interactions is nevertheless important, considering the number of relevant human pathogens that do not follow strict icosahedral or helical symmetry. Cryo-electron tomography and subtomogram averaging methods provide structural insights into complex biological environments and are well suited to go beyond structures of perfectly symmetric viruses. Specifically, we use these methods to understand the structural conservation and diversity in retroviral capsid assemblies and how the small molecule IP6 regulates retrovirus assembly and maturation. To learn more about our efforts to visualize the structure of different viruses and how they help us to take cryo-ET and subtomogram averaging to the next level click here.
We are very thankful to the ERC, Austrian Science Fund (FWF), the ChanZuckerberg Initiative (CZI), FEBS and EMBO for funding our research. We also are thankful to the Austrian Academy of Sciences (OEAW) for supporting Dario Porley through a DOC-fellowship.