Respuesta :
Akt, a serine or threonine kinase also known as PKB, is essential for controlling a variety of cellular processes, including as EC migration and survival, gene transcription, and protein synthesis important for angiogenesis.
Akt activates mTOR, which in turn regulates protein synthesis and cell growth. p70-S6 kinase-1 and 4E-binding protein 1 are phosphorylated by mTOR, which controls the synthesis of proteins important for angiogenesis. The activation of the highly conserved PI3K-PKB/Akt pathway is carefully regulated by a multistep process. Class 1A PI3Ks bound via their regulatory subunits or adaptor molecules, such as the insulin receptor substrate (IRS) proteins, are directly stimulated by activated receptors. Phosphatidylinositol (3,4)-bisphosphate (PIP2) lipids are converted to phosphatidylinositol (3,4,5)-trisphosphate by the catalytic domain of PI3K as a result of this (PIP3).
When PKB/Akt binds to PIP3 at the plasma membrane, PDK1 can enter the "activation loop" and phosphorylate T308 to partially activate PKB/Akt. By directly phosphorylating and inactivating tuberous sclerosis protein 2 (TSP2) and proline-rich Akt substrate of 40 kDa (PRAS40), this PKB/Akt alteration is sufficient to activate mTORC1 (TSC2). By influencing a variety of downstream components involved in regulating the G1/S and G2/M transitions, growth-factor-activated Akt signaling supports progression through regular, undisturbed cell cycles.
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