The three isoforms of Akt share a high degree of structural similarity and sequence homology. The present model shows that Akt is activated through the phosphatidylinositol 3 kinase pathway on growth factor stimulation. The services and products of PI3K, specifically phosphatidyl inositol triphosphate, bind to the Pleckstrin homology histone deacetylase HDAC inhibitor domain of Akt and goal Akt to the plasma membrane where it is phosphorylated on two key residues: Thr308 in the activation loop by PDK1 and Ser473 in the hydrophobic motif of the C terminal tail by putative PDK2. Planned candidates of PDK2 contain PDK1, integrin linked kinase, Akt it self, DNA PKcs, and recently, the mammalian target of rapamycin rictor complex. Phosphorylation on both Ser473 and Thr308 is necessary for complete activation of Akt. Several substrates for Akt have been identified, including I?B kinase kinase, caspase 9, forkhead transcription factors, Bad, glycogen synthase kinase 3, MDM2, p21cip1/WAF1, TSC2, and so on. Among these, forkhead transcription factors, and Bad, caspase 9 facilitate pyrazine apoptosis, and the phosphorylation by Akt abolishes their proapoptotic activities. PI3K Akt transduces mitogenic signals from growth factors and promotes G1/S transition. Through multiple components, Akt downregulates p27, an important Cdk inhibitor that ceases cells in lateG1 until cells are prepared for DNA synthesis. Akt pathway also regulates the transition at G2/M. Either PI3K inhibitors or the lack of Akt in Akt1 null ES cells were reported to produce a delay in G2/M transition. The Akt pathway has been demonstrated to determine mitotic entry along with its mitogenic functions at the G1/S transition. Inhibition of PI3K in a delay in the progression through G2/M, which can be recovered by overexpressing Akt. PTEN null ES cells were shown to transportation faster through the section. natural product library Overexpressing a dominant negative mutant of Akt also arrests cells in G2/M. Eventually, PI3K Akt route adjusts mitotic access through controlling the time of Cdc2 initial. Wee1 and Myt1 are two kinases that phosphorylate Cdc2 at Thr14/ Tyr15 and inhibit Cdc2 kinase activity. Akt phosphorylates and downregulates Myt1 in the border. In addition, Akt was proven to phosphorylateWEE1Hu at Ser642, which often supplies the binding site for 14. That 14 3 joining translocates WEE1Hu in to the cytoplasm and, thus, prevents its inhibitory phosphorylation on Cdc2. Akt also prevents Plk1 destruction through CHFR and promotes mitotic entry under normal conditions and after DNA damage. Aurora kinases are serine/threonine kinases that regulate mitotic activities, ranging from centrosome maturation, mitotic spindle formation, chromosome segregation to cytokinesis. The three members of Aurora kinase family in metazoans reveal substantial structure and sequence similarities. However, they show different localizations and functions during mitosis. Aurora A localizes to centrosomes and is vital for centrosome duplication and growth.