MAPK ERK kinases, also known as MEKs, are a group of enzymes that play a crucial role in cellular signaling pathways. They belong to the family of mitogen-activated protein kinases (MAPKs) and specifically regulate the extracellular signal-regulated kinase (ERK) pathway.
These kinases are responsible for phosphorylating and activating ERKs, a type of MAPK, in response to various extracellular signals. They act as intermediates in a signaling cascade, relaying the information from cell surface receptors to the nucleus, where they influence gene expression and cellular responses.
MEKs are highly conserved among eukaryotes and typically exist as multiple isoforms in mammals. The most well-known isoforms of MEKs are MEK1 and MEK2. They contain conserved domains, including a kinase domain that catalyzes the phosphorylation event, a proline-rich domain, and a regulatory domain that contributes to their specificity and regulation.
Activation of MEKs is triggered by the binding of ligands, such as growth factors or cytokines, to their respective cell surface receptors. This initiates a series of phosphorylation events, leading to the activation of MEKs. Once activated, MEKs phosphorylate ERKs on specific residues, which allows ERKs to translocate to the nucleus and activate various downstream targets involved in cell proliferation, differentiation, survival, and apoptosis.
Dysregulation of the MAPK ERK kinases pathway, including mutations or aberrant activation of MEKs, has been implicated in numerous diseases, including cancer, neurodegenerative disorders, and inflammatory diseases. Due to their importance in cellular signaling, MEKs have become attractive targets for therapeutic interventions, with several MEK
