AKT (PKB or Rac) is a serine/threonine kinase located at the core node of the PI3K/AKT/mTOR signaling pathway (PAM pathway), regulating basic functions such as transcription, translation, proliferation, growth, and apoptosis of cells. AKT has three subtypes: Akt1, Akt2, and Akt3. The PH domain (pleckstrin homology domain) of AKT specifically binds to PIP2 and PIP3, allowing AKT to be localized on the cell membrane. Subsequently, the kinase domain transfers the phosphate group of ATP to the substrate threonine for phosphorylation.

Epidermal growth factor receptor (EGFR) is the most classic target in the field of anti-tumor therapy. EGFR is widely distributed on the surface of mammalian epithelial cells, fibroblasts, glial cells, keratinocytes, and other cells. EGFR signaling pathway plays an important role in physiological processes such as cell growth, proliferation, and differentiation. EGFR mutations or overexpression generally trigger tumors. EGFR is a glycoprotein, belonging to the tyrosine kinase receptor type, with a cell membrane penetration and a molecular weight of 170KDa. EGFR is located on the surface of the cell membrane and is activated by binding to ligands, including EGF and TGFα. After activation, EGFR transforms from monomers to dimers, although there is also evidence that dimers exist before activation. EGFR may also be activated by aggregating with other members of the ErbB receptor family, such as ErbB2/Her2/neu.

The PI3K-Akt signaling pathway (phosphatidylinositol 3-kinase-protein kinase B signaling pathway) is a very important intracellular signaling pathway, which refers to the intracellular signaling pathway composed of PI3K and protein Akt. It plays a key role in numerous physiological processes of cells, such as cell growth, proliferation, survival, metabolism, migration, and angiogenesis. The abnormal activation of this pathway is closely related to the occurrence and development of various diseases, especially cancer.