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Our research activities concentrate on the question how complex, supramolecular structures are assembled in cells. This includes the following basic aspects:

  • Which protein-protein interactions are the molecular basis for the assembly of complex structures?
  • Which signals regulate their subcellular morphogenesis?
  • Which malfunctions are involved in pathological aberrations of normal assembly?
These questions are addressed in an exemplary fashion primarily with cross-striated muscle cells. Our research focusses on the morphogenesis of the myofibrillar apparatus that is responsible for muscle contraction. The precise regulation of the assembly of actin into thin filaments and myosin into thick filaments relies on interactions with numerous cytoskeletal proteins, which are also necessary to integrate these filaments into contractile units, the sarcomeres. To enable an efficient transduction of the forces developed by the contracting myofibrils, muscle cells need specialized structures that link the contractile machinery to the cell membrane and the extracellular environment. Using various modern techniques of cell biology, molecular biology and protein chemistry, we have recently characterized several proteins involved in the morphogenesis of myofibrils, and elucidated signal transduction pathways that regulate the interactions of these proteins with their ligands. Our current research mainly focusses on the proteins that play a role in the dramatic remodeling of the actin cytoskeleton that accompanies the integration of actin filaments into myofibrils, and their subsequent attachment to the cell membrane. In cooperation with several clinical research groups we analyze the pathophysiological effects of mutations in myofibril-associated proteins that are causative for skeletal and cardiac muscle diseases.
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