Abstract
Dual-specificity phosphatases (DUSPs) are a subset of protein tyrosine phosphatases (PTPs), many of which dephosphorylate the residues of phosphor-serine/threonine and phosphor-tyrosine on mitogen-activated protein kinases (MAPKs), and hence are also referred to as MAPK phosphatases (MKPs). Homologue of Vaccinia virus H1 phosphatase gene clone 5 (HVH-5), also known as DUSP8, is a unique member of the DUSPs family of phosphatases. Accumulating evidence has shown that DUSP8 plays an important role in phosphorylation-mediated signal transduction of MAPK signaling ranging from cell oxidative stress response, cell apoptosis and various human diseases. It is generally believed that DUSP8 exhibits significant dephosphorylation activity against JNK, however, with the deepening of research, plenty of new literature reports that DUSP8 also has effective dephosphorylation activity on p38 MAPK and ERKs, successfully affects the transduction of MAPKs pathway, indicating that DUSP8 presents a unknown diversity of DUSPs family on distinct corresponding dephosphorylated substrates in different biological events. Therefore, the in-depth study of DUSP8 not only throws a new light on the multi-biological function of DUSPs, but also is much valuable for the reveal of complex pathobiology of clinical diseases. In this review, we provide a detail overview of DUSP8 phosphatase structure, biological function and expression regulation, as well as its role in related clinical human diseases, which might be help for the understanding of biological function of DUSP8 and the development of prevention, diagnosis and therapeutics in related human diseases.
Highlights
Protein phosphorylation is a key event that controls cellular responses to external cues [1–3]
By testing DUSP8 and PTPRC for their diagnostic potential through quantitative PCR assay from 138 blood samples with Parkinson’s disease (PD), the results have shown that compared to PD patients and healthy controls, the relative abundance of PTRPC mRNA significantly decreased in progressive supranuclear palsy (PSP) patients, whereas there was no obvious difference in the expression level of DUSP8, suggesting DUSP8 might not be suitable to become a biomarker for assisting to diagnose PD or PSP [67]
Accumulating evidence has shown that DUSP8, a unique member of Dual-specificity phosphatases (DUSPs) family, is emerging as a critical negative regulator for mitogen-activated protein kinases (MAPKs) pathway and involved in cell oxidative stress response and cell apoptosis, as well as the development of various human diseases
Summary
Protein phosphorylation is a key event that controls cellular responses to external cues [1–3]. One of the most widely studied signaling pathways is the mitogen-activated protein kinases (MAPKs) DUSP8, as a emerging phosphatase, involved in the development and progression of multiple human diseases, plays a critical role in negatively regulating the activity via dephosphorylates relevant residues; there is absent of a review to comprehensively summary these findings and its specific significance.
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