When the ligands such as growth factor bind to the RTKs, two RTKs monomer get close and form a dimer, which leads to activation of the intracellular tyrosine kinase domain and auto phosphorylation by each monomers.

This receptor have three functional domains: an extracellular ligand binding domain, a transmembrane domain and an intracellular tyrosine kinase domain. RTKs are the high-affinity cell surface receptors for many polypeptide growth factors, cytokines, and hormones. The key molecules involved in this signaling pathway are receptor tyrosine kinase (RTKs), phosphatidylinositol 3-kinase (PI3K), phosphatidylinositol-4,5-bisphosphate (PIP2), phosphatidylinositol-3,4,5-bisphosphate (PIP3) and AKT/protein kinase B. Then, several researches suggested that membrane phospholipids generated by PI3K were an integral element required for PKB/Akt activation. In 1995 Richard Roth and his colleagues reported that Akt was activated by insulin. An enzyme termed phosphatidylinositol 3-kinase (PI3K) had been isolated in 1990 by the group of Cantley. These three cloning papers established PKB/Akt as a novel phospho-protein kinase that was widely expressed, and paved the way for future experiments into the role of PKB/Akt in diverse cellular processes. In 1991, three independent research teams identified genes corresponding to PKB/Akt. And this cell-derived oncogenic sequence were isolated and named akt. The origins of PKB/Akt research can be traced back to the discovery in 1977, by Staal and co-workers, which is a previously undescribed oncogene in a virus termed ATK8. Key proteins involved are phosphatidylinositol 3-kinase (PI3K) and Akt/Protein Kinase B. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates.

PI3K-Akt Pathway is an intracellular signal transduction pathway that promotes metabolism, proliferation, cell survival, growth and angiogenesis in response to extracellular signals.

State of survival growth kit