MAP kinase tyrosine phosphatase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: MAP kinase tyrosine phosphate + H2O = MAP kinase tyrosine + phosphate. [GOC:mah]

MAP kinase tyrosine phosphatase activity refers to the enzymatic activity of proteins that specifically remove phosphate groups from tyrosine residues within MAP kinases. MAP kinases, also known as mitogen-activated protein kinases, are a family of serine/threonine protein kinases that play critical roles in signal transduction pathways involved in cellular responses to various stimuli, including growth factors, stress, and hormones. The dephosphorylation of tyrosine residues within MAP kinases by MAP kinase tyrosine phosphatases is a crucial regulatory mechanism that terminates MAP kinase signaling and ensures proper signal duration. This process involves the formation of a transient complex between the phosphatase and the MAP kinase substrate. The phosphatase then utilizes a catalytic mechanism involving a conserved cysteine residue in its active site to remove the phosphate group from the tyrosine residue. This dephosphorylation event reverts the MAP kinase to its inactive state, effectively shutting down the downstream signaling cascade. The precise regulation of MAP kinase activity by MAP kinase tyrosine phosphatases is essential for maintaining cellular homeostasis and preventing aberrant signaling that can lead to pathological conditions. These phosphatases are involved in various cellular processes, including cell growth, differentiation, apoptosis, and immune responses.'
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Proteins (2)

Compounds (3)