The dynamic alterations in the cytoskeletal components actin and intermediate, etc. filaments are required for cell invasion and migration. The actin cytoskeleton is a highly dynamic structure that is governed by a delicate balance of actin filament formation and disassembly. To controlling the activities of key components of the epithelial mesenchymal transition (EMT) could be a viable solution to metastasis. Bioinformatics technologies also allow researchers to investigate the consequences of synthetic mutations or naturally occurring variations of these cytoskeletal proteins. S100A4 is S100 protein family member that interact with a variety of biological target. In study has shown that S100A4 interacts with the tumor suppressor protein p53, indicating that S100A4 may have additional roles in tumor development. The S100A4 and p53 interaction increases after inhibition of MDM2-dependent p53 degradation using Nutlin-3A. The main goal of this research was control of cytoskeletal dynamics in cancer through a combination of, actin and S100A4 protein. The investigate the molecular mechanism behind S100A4 function in (EMT) and indicating that S100A4 is promoting p53 degradation. Understanding the signaling pathways involved would provide a better understanding of the changes that occur during metastasis, which will eventually lead to the identification of proteins that can be targeted for treatment, resulting in lower mortality.