The morphology and elasticity of adhered cells is closely related to the structure of the cytoskeletal meshwork and the way that actomyosin fibers interact with each other to form the network, which is mediated by the activity of myosin Ⅱ. Therefore the interaction between minifilaments (assembled by non-muscle myosin Ⅱ) is important to the cell-level cytoskeletal remodeling through mechanosensing. However, at present it is still difficult to precisely obtain the experimental data of myosin Ⅱ in vivo because the invasive measurement would disturb the cellular local structure and physiological activities, and the non-invasive measurement couldn't provide information about myosin Ⅱ activity accurately. In this paper, we developed and applied new images analysis methods, such as protein fluorescent image tracking and image correlation spectroscopy, to quantify the kinetics of disassembly and reassembly of actomyosin networks and compared them to studies by other groups. This analysis suggested the following processes contribute to the assembly of cortical actomyosin and stress fibers: random myosin mini-filament assembly and disassembly along the cortex; myosin mini-filament aligning and contraction; stabilization of cortical myosin upon increasing contractile tension. We found that the number of myosin Ⅱ and focal adhesions are very important to the formation and stability of the typeⅠ, Ⅱ and Ⅲ actomyosin network in HeLa cells, and the activity of myosin Ⅱ, which determines the dynamics of the actomyosin network reorganization, can be quantified through STICS (spatial temporal image correlation spectroscopy). The formation of typeⅠ, Ⅱ, and Ⅲ actomyosin networks was explained through a mechanical model by adjusting the parameters of myosin Ⅱ activities and number density. The STICS method used in this study can be applied to evaluate the activity of other proteins in live cells.