Cells actively probe the mechanical properties of their environment and adapt their physiological state accordingly. For this fundamental task, they exert forces on their environment using their actomyosin machinery. This machinery consists of protein fibers consisting of dynamically assembling and dissembling actin units, so called actin stress fibers, on which motor proteins act to generate forces. This machinery is also used to react to external forces applied to cells. Transduction of forces from the actomyosin complexes to the extracellular space occurs via adaptive multi-protein complexes, so called focal adhesions. Focal adhesions re-structure depending on biochemical and mechanical signals. The distance of the extracellular matrix to the actomyosin fibers is determined by the structure of these complexes. Monitoring this distance reveals cellular adaptions to force. Here, we use metal induced energy transfer (MIET) to monitor the distance of the extracellular matrix to focal adhesions for understanding force transduction through focal adhesions. We manipulate the cells either with drugs influencing cellular force generation or using an atomic force microscope. We find that high forces lead to a multistep-restructuring of focal adhesions, rendering force transduction more efficient.
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