PKM2 also phosphorylates myosin light chain 2 (MLC2) at Tyr118, primes the binding of Rho-associated protein kinase 2 (ROCK2) to MLC2 and the phosphorylation of ROCK2–MLC2 complex at Ser15, to allow the interaction between myosin II with actin, which is required for the contractile function of the actomyosin complex at the cleavage furrow, completion of the cytokinesis process, and proliferation of tumor cells [16]. This evidence concerns the gene MYL2 and neoplasm.