Protein kinase B (c-Akt) is a multifunctional mediator of phosphatidylinositol 3-kinase (PI-3K) activation. It is involved in various cellular processes, including cell survival, growth, and metabolism. The AKT gene was first identified in mice, where it was associated with leukaemias and lymphomas. Human homologues, AKT1 and AKT2, were later cloned and found to be amplified in various cancers. AKT1 is primarily expressed in the brain, thymus, heart, and lung, while AKT2 is more restricted to the brain and testes. The expression of AKT is tightly connected with terminal differentiation of various cell types. PKB is activated by various stimuli, including growth factors, cytokines, and hormones. Activation of PKB is mediated by PI-3K, which generates phosphoinositides that bind to the PH domain of PKB. This binding leads to the phosphorylation of PKB, which is essential for its activation. The phosphorylation of PKB is regulated by two sites, Thr308 and Ser473, which are phosphorylated by PDK1 and PDK2, respectively. PKB is a multimeric protein that exists in three isoforms: α, β, and γ. The PH domain of PKB mediates its interaction with other proteins, playing a role in its regulation. PKB is involved in various biological functions, including the regulation of glucose transport, glycogen synthesis, and protein synthesis. It also plays a role in anti-apoptotic signaling by inhibiting caspase activity and promoting the expression of Bcl-2 and c-Myc. PKB is also involved in cell survival pathways, where it helps to prevent apoptosis by inhibiting the activation of caspases. It is involved in cytokine-mediated survival, where it helps to protect cells from apoptosis induced by cytokine deprivation. PKB is also involved in cell-cycle progression, where it regulates the activation of E2F, a key regulator of cell-cycle progression. The activation of PKB is complex and involves multiple signaling pathways. It is regulated by various kinases, including PDK1 and PDK2, which phosphorylate specific sites on PKB. The activation of PKB is also influenced by the presence of specific phosphoinositides, which bind to the PH domain of PKB. The regulation of PKB is critical for various cellular processes, including cell survival, growth, and metabolism. The study of PKB has provided important insights into the mechanisms of cell survival and the regulation of various cellular processes.Protein kinase B (c-Akt) is a multifunctional mediator of phosphatidylinositol 3-kinase (PI-3K) activation. It is involved in various cellular processes, including cell survival, growth, and metabolism. The AKT gene was first identified in mice, where it was associated with leukaemias and lymphomas. Human homologues, AKT1 and AKT2, were later cloned and found to be amplified in various cancers. AKT1 is primarily expressed in the brain, thymus, heart, and lung, while AKT2 is more restricted to the brain and testes. The expression of AKT is tightly connected with terminal differentiation of various cell types. PKB is activated by various stimuli, including growth factors, cytokines, and hormones. Activation of PKB is mediated by PI-3K, which generates phosphoinositides that bind to the PH domain of PKB. This binding leads to the phosphorylation of PKB, which is essential for its activation. The phosphorylation of PKB is regulated by two sites, Thr308 and Ser473, which are phosphorylated by PDK1 and PDK2, respectively. PKB is a multimeric protein that exists in three isoforms: α, β, and γ. The PH domain of PKB mediates its interaction with other proteins, playing a role in its regulation. PKB is involved in various biological functions, including the regulation of glucose transport, glycogen synthesis, and protein synthesis. It also plays a role in anti-apoptotic signaling by inhibiting caspase activity and promoting the expression of Bcl-2 and c-Myc. PKB is also involved in cell survival pathways, where it helps to prevent apoptosis by inhibiting the activation of caspases. It is involved in cytokine-mediated survival, where it helps to protect cells from apoptosis induced by cytokine deprivation. PKB is also involved in cell-cycle progression, where it regulates the activation of E2F, a key regulator of cell-cycle progression. The activation of PKB is complex and involves multiple signaling pathways. It is regulated by various kinases, including PDK1 and PDK2, which phosphorylate specific sites on PKB. The activation of PKB is also influenced by the presence of specific phosphoinositides, which bind to the PH domain of PKB. The regulation of PKB is critical for various cellular processes, including cell survival, growth, and metabolism. The study of PKB has provided important insights into the mechanisms of cell survival and the regulation of various cellular processes.