Inhibition of Dual-specificity phosphatase 14 (DUSP14) by Ethyl-3,4-dephostatin

摘要

Most cellular functions derived from signal transduction pathways require protein phosphorylation. Protein phosphorylation is processed by opposing activities of protein kinases and protein phosphatases. Dual-specificity phosphatases (DUSPs) are a subclass of protein tyrosine phosphatases (PTP) families that comprises 107 genes in human genome and can dephosphorylate both phospho-tyrosine and phosphoserine/phosphothreonine residues on substrates. Some DUSPs have been reported as key regulators for inactivating mitogen-activated protein kinases (MAP kinase). The three major subfamilies of MAPK in mammalian cells are p38, extracellular signal regulated kinase (ERK), c-Jun N-terminal kinase (INK).