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Background:MEK1 and MEK2, also known as MAPK or Erk kinases, are dual-specificity protein kinases. Their primary role is to phosphorylate and activate downstream MAPK proteins, including ERK1/2 (Extracellular Signal-Regulated Kinase 1/2). Upon stimulation by growth factors, hormones, or stress, MEK1 undergoes activation and phosphorylation. This activated form of MEK1 then transmits signals to ERK1/2 through phosphorylation, ultimately leading to their activation. Once activated, ERK1/2 can enter the cell nucleus and play a crucial role in regulating various cellular physiological processes, such as gene expression, cell cycle progression, cell proliferation, cell migration, and cell survival. In typical conditions, MEK1 is phosphorylated at two conserved serine residues, namely Ser218 and Ser222. Additionally, MEK1 can also be phosphorylated at the Ser298 site by pAK1. This phosphorylation event helps facilitate signal transduction from Raf to MEK1 and Erk2.
