Ethyl-3,4-dephostatin Inhibits Dual-specificity phosphatase 22 (DUSP22) Activity

摘要

Protein phosphorylation is one of the major protein modification processes that play critical roles in a variety of biological processes, including gene expression, proliferation, differentiation, cell cycle arrest, and apoptosis. Protein phosphorylation usually occurs in serine, threonine, or tyrosine residues and is processed by protein kinases. Of those protein kinases, extracellular signal-regulated kinase (ERK), p38, and c-Jun N-terminal kinase (JNK) that are members of mitogen-activated protein kinases (MAPK) family, have diverse roles in cell proliferation, cell survival, cell death, differentiation, development, immune function, gene expression, and other intracellular events. Therefore, regulation of those MAPK family members results in diverse outcome of cell fate. Many of protein tyrosine phosphatases (PTPs) control the activation of MAPKs through dephosphorylation of phosphoserine, phosphothreonine, or phospho-tyrosine residues that are located on the activation loop of MAPKs. The human genome contains 107 PTP genes. Dualspecificity phosphatases (DUSPs) as a heterogeneous group of protein phosphatases belong to a subclass of PTP families and dephosphorylate both phosphotyrosine and phosphoserine/phosphothreonine residues.