The high-concentration of phosphocholine noticed in neoplastic cells is born in large part to the growth factor activated Ras and PI3K supplier Dabrafenib signaling cascades which stimulate choline kinase via the Rho GTPases. Phosphocholine serves as a vital metabolic tank for the main phospholipid component of membranes, the production of phosphatidylcholine and substrate for the production of lipid second messengers. Particularly, phosphatidic acid, produced in the bosom of phosphatidylcholine by the Ras and PI3K target phospholipase D2, has emerged as a key upstream and downstream activator of Ras signaling. Phosphatidic acid initiates and amplifies Ras signaling by: recruiting the guanine nucleotide exchange factor Sos and the serine/threonine kinase Raf 1 to the plasma membrane, stimulating endosome formation required for MAP kinase activation, and activating the mammalian target of rapamycin kinase. Taken together, these studies claim that phosphocholine might be an important metabolic centre not merely for membrane phospholipid synthesis but additionally for the amplification of neoplastic signaling cascades needed for growth and survival. In a previous research, we demonstrated that the steady state concentration of phosphocholine Metastatic carcinoma is enhanced in H RasV12 changed human epithelial cells in accordance with normal human epithelial cells. We then found that siRNA silencing of choline kinase expression in HeLa cells abrogated the high concentration of phosphocholine, which in turn reduced phosphatidic acid and signaling through both the PI3K/AKT trails and MAPK. That simultaneous reduction in survival signaling triggered a marked decline in the anchorage independent survival of HeLa cells in soft agar and athymic mice. Essentially, combination therapies targeting both PI3K/AKT and MAPK signaling pathways may be a more efficient method p53 ubiquitination than single pathway interruption in patients with advanced level cancers. Provided that selective inhibition of choline kinase disrupted both pathways, we predicted that small molecule antagonists of choline kinase could have activity against a broad range of human cancers propagated with a combination of signaling pathway variations. In today’s research, we performed a screen for small molecule inhibitors of choline kinase utilizing the recently solved crystal structure of choline kinase. We identified a lead compound that is selectively cytotoxic to transformed epithelial cells relative to typical epithelial cells, prevents choline kinase activity and the steady-state concentration of phosphocholine in transformed cells, decreases ERK and AKT activating phosphorylations, and suppresses the growth of xenografts in vivo. These studies suggest that in silico screening of available ingredient sources has great utility for the recognition of small molecule antagonists of metabolic enzymes.