The Effect of Anillin on Actomyosin Network Dynamics

The actin crosslinking protein, anillin, has been shown to autonomously constrict actin rings without the presence of motors. This contractililty is reminiscent of actomyosin contraction, which requires a careful balance of connectivity and force-generation. Here, we investigate the effect of anillin crosslinking on global contractility of actomyosin networks. We use fluorescence confocal microscopy to image actomyosin network dynamics and use differential dynamic microscopy and spatial image autocorrelation to quantify the rate of contraction and degree of restructuring. We show that increasing the concentration of anillin slows the rate of global network contraction while at the same time enhancing local bundling and restructuring.