Regulation of the cell secretome by protein kinase CK2 modulates cell migration and extracellular matrix composition

The protein kinase CK2 is a pleiotropic kinase known for its involvement in numerous cellular processes, although its role in controlling the cell secretome and extracellular matrix (ECM) composition has not been explored in deep. This study used a triple SILAC quantitative proteomic approach to examine how the absence of CK2 affected the cell secretome in C2C12 myoblasts. The analysis of proteins with significant expression changes in CK2-deficient cells suggests an important role of CK2 in shaping the extracellular environment. Functional experiments in different cell lines demonstrated that CK2-dependent alterations in the secretome had significant effects on cell migration, as evidenced by impaired migration properties in wild-type cells exposed to conditioned medium from CK2-deficient cells, supporting the importance of targeting CK2 in pharmacological cancer treatments. Overall, this research contributes to our understanding of CK2's involvement in ECM generation, adding a new piece to the full picture of CK2 cellular functions.