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Nuclear HSP70 leads to enhancement of vaccinia H1-related phosphatase (VHR) activity via protein-protein interaction rather than its molecular chaperone activity, thereby suppressing excessive ERK activation. Downregulation of either VRK3 or HSP70 rendered cells vulnerable to glutamate-induced apoptosis.
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Data indicated that regulating non-receptor tyrosine kinase FAK and cell migration is a newly revealed function of VHR/DUSP3.
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The loss of DUSP3 activity markedly increases gamma radiation-induced DNA strand breaks, suggesting a potential novel role for DUSP3 in DNA repair.
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In PTP1B and VHR, two new allosteric clusters were identified in each enzyme.
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In the phosphatase-silenced cells, the normal bipolar spindle structure was restored by chemical inhibition of Erk1/2 and ectopic overexpression of Dusp3. We propose that at M phase Dusp3 keeps Erk1/2 activity in check to facilitate normal mitosis.
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Data suggest levels of gene expression of both DUSP3 (dual specificity phosphatase 3) and PSME3 (proteasome activator subunit 3) are associated with susceptibility to Staphylococcus aureus infection/sepsis in humans and in mouse disease model.
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Our results demonstrate that DUSP3 plays a key and nonredundant role as a regulator of innate immune responses
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VHR can dimerize inside cells, and that VHR catalytic activity is reduced upon dimerization.
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DUSP3 is a pro-angiogenic atypical dual-specificity phosphatase.
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DUSP3 interacting partners are nucleolar proteins involved in processes related to DNA repair and senescence.
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we report the first successful site-specific incorporation of sulfotyrisine into VHR through the use of expanding genetic code
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Proteins containing the class II motifs are efficient VHR substrates in vitro, suggesting that VHR may act on a novel class of yet unidentified Tyr(P) proteins in vivo.
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Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3
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VHR expression enhances the signaling of ErbB receptors and may be involved in NSCLC pathogenesis.
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VHR, a Vaccinia virus VH1-related dual-specific protein phosphatase, is phosphorylated at Y138 by ZAP-70.
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VHR is required for cell-cycle progression as it modulates MAP kinase activation in a cell-cycle phase-dependent manner.
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deregulated expression of BRCA1-IRIS is likely to reduce dependence on normal physiological growth stimuli
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Small dual-specificity phosphatase VHR selectively dephosphorylates tyrosine-phosphorylated interferon-alpha- and beta-activated transcription factor STAT5, leading to the subsequent inhibition of STAT5 function.
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Results highlight the importance of a high intracellular Zn(2+) content and the VHR/ZAP-70/ERK1,2-associated pathways in the modulation of LNCaP prostate cancer cell growth.
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VHR can be considered as a new marker for cancer progression in cervix carcinoma and potential new target for anticancer therapy
