Abstract
Cancer is one of the most diagnosed diseases in developed countries. Inflammation is a common response to different stress situations including cancer and infection. In those processes, the family of mitogen-activated protein kinases (MAPKs) has an important role regulating cytokine secretion, proliferation, survival, and apoptosis, among others. MAPKs regulate a large number of extracellular signals upon a variety of physiological as well as pathological conditions. MAPKs activation is tightly regulated by phosphorylation/dephosphorylation events. In this regard, the dual-specificity phosphatase 10 (DUSP10) has been described as a MAPK phosphatase that negatively regulates p38 MAPK and c-Jun N-terminal kinase (JNK) in several cellular types and tissues. Several studies have proposed that extracellular signal-regulated kinase (ERK) can be also modulated by DUSP10. This suggests a complex role of DUSP10 on MAPKs regulation and, in consequence, its impact in a wide variety of responses involved in both cancer and inflammation. Here, we review DUSP10 function in cancerous and immune cells and studies in both mouse models and patients that establish a clear role of DUSP10 in different processes such as inflammation, immunity, and cancer.
Highlights
The human genome contains a large number of genes that transcribe/translate to four families of protein tyrosine phosphatases (PTP), which are subclassified depending of their substrate, structure, regulation, and function
We should underline that a variety of stress stimuli such as sepsis, injury, chronic inflammation, and viral infection modulates dual-specificity phosphatase 10 (DUSP10) expression
DUSP10 is induced in many types of cancers, and its enhanced expression confers in general a pro-tumorigenic capacity to neoplastic cells for proliferation, migration, and differentiation
Summary
The human genome contains a large number of genes that transcribe/translate to four families of protein tyrosine phosphatases (PTP), which are subclassified depending of their substrate, structure, regulation, and function Of these genes, 61 encode for dual-specificity phosphatase subfamily and 10 of them are catalytically active MAP kinase phosphatases (MKPs), which are able to dephosphorylate dual specificity phospho-Tyrosine (pTyr) and phospho-Threonine (pThr) substrate, and one of them is catalytically inactive MKP [1]. ISteevaenrdal tchherokminaatsien-biimndminugnodpormecaipinitaotfioDnU-mSPas1s0,sweqhuiechnccinongse(CrvHeIsPt-hseeqm) eecxhpaenriimsmenotfs mreovleeacul ltahrerebciongdninitgioonf these factors on regulatory elements of DUSP10 gene (promoter region, as identified by H3K4me binding) [19] In this regard, it has been proposed that DUSP10 gene has a particularity of being regulated by MAPKs, which promote DUSP10 expression, suggesting a negative feedback loop [20]. Current studies have demonstrated that DUSP10 is able to dephosphorylate phospho-Serine (pSer) residue of non-MAPK substrates [15]
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