Characterization of the actomyosin binding interface

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The aim of this project is to elucidate the function of actin-based motor proteins in cell adhesion, phagocytosis and filopodia dynamics. Members of at least four different myosin classes appear to be involved in these processes. Initial results show that their motor properties share many features with fast skeletal muscle myosins, which facilitates their production and characterization. Distinct functional features of these myosins can be linked to a small number of changes at the primary sequence level, whose detailed characterization promises to reveal new and important insights about the mechanism of chemo-mechanical coupling and its regulation. In particular, we will test the significance and structural basis of a regulatory mechanism by which physiological changes in the concentration of free Mg2+-ions modulate the motor activity of at least two of these myosins. Together with our partner laboratories in the research unit, we will measure the forces produced by individual myosins and small ensembles of myosins, characterize myosin binding partners, and dissect the role of myosin VII as mediator of interactions between adhesion structures, filamentous actin and microtubules.