MAP kinase tyrosine/serine/threonine phosphatase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: MAP kinase serine/threonine/tyrosine phosphate + H2O = MAP kinase serine/threonine/tyrosine + phosphate. [GOC:mah, PMID:12184814]

MAP kinase tyrosine/serine/threonine phosphatase activity is a critical regulatory mechanism in cellular signaling pathways. It specifically removes phosphate groups from tyrosine, serine, and threonine residues within MAP kinases, which are key components of signaling cascades that regulate a diverse range of cellular processes. These processes include cell proliferation, differentiation, survival, and stress responses. The removal of phosphate groups by MAP kinase phosphatases deactivates MAP kinases, effectively terminating their signaling activity. This dephosphorylation event is essential for maintaining a balance in cellular signaling and preventing uncontrolled activation of MAP kinase pathways, which can lead to pathological conditions such as cancer. The specificity of MAP kinase phosphatases for MAP kinases ensures that they are not involved in the regulation of other signaling pathways. This specificity is achieved through the presence of specific binding sites and active sites within the phosphatase that recognize and interact with the MAP kinase substrates. These phosphatases often work in concert with other signaling molecules to fine-tune MAP kinase activity in response to specific stimuli. Understanding the molecular function of MAP kinase tyrosine/serine/threonine phosphatase activity is crucial for comprehending the complexity of cellular signaling and for developing therapeutic strategies targeting these enzymes in disease.'
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Proteins (2)

Compounds (3)