Abstract
Cortical actomyosin networks consist of filamentous actin (F-actin) bundles crosslinked into highly dynamic networks that are linked physically to the extracellular matrix via integrins. These networks play an active role in tissue morphogenesis during development as well as metastasis in cancer, by enabling rapid remodelling of cell shape via F-actin polymerization and interaction with myosin-II motor proteins. Here we investigate a newly discovered isotropic actomyosin network on the dorsal surface of epithelial MDCK cells and characterize its structure and dynamics using computational analysis of timelapse fluorescence microscopy data provided by Lifeact, a highly specific marker for F-actin in living cells. At low cell density, F-actin bundles depolymerise and polymerize continuously, splitting and merging into large bundle clusters. Spatial Temporal Image Correlation Spectroscopy and Optical Flow are used to characterize the oscillatory dynamics of the bundled networks, and reveal characteristic length- and time-scales associated with their motions.
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