Recombinant Human Dual specificity protein phosphatase 3 (DUSP3)

1. 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. PMID: 27941812
2. Data indicated that regulating non-receptor tyrosine kinase FAK and cell migration is a newly revealed function of VHR/DUSP3. PMID: 28759036
3. The loss of DUSP3 activity markedly increases gamma radiation-induced DNA strand breaks, suggesting a potential novel role for DUSP3 in DNA repair. PMID: 28389334
4. In PTP1B and VHR, two new allosteric clusters were identified in each enzyme. PMID: 28625849
5. 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. PMID: 27423135
6. 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. PMID: 24901344
7. Our results demonstrate that DUSP3 plays a key and nonredundant role as a regulator of innate immune responses PMID: 25876765
8. VHR can dimerize inside cells, and that VHR catalytic activity is reduced upon dimerization. PMID: 24798147
9. DUSP3 is a pro-angiogenic atypical dual-specificity phosphatase. PMID: 24886454
10. DUSP3 interacting partners are nucleolar proteins involved in processes related to DNA repair and senescence. PMID: 24245651
11. we report the first successful site-specific incorporation of sulfotyrisine into VHR through the use of expanding genetic code PMID: 23918168
12. 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. PMID: 23322772
13. Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3 PMID: 21921027
14. VHR expression enhances the signaling of ErbB receptors and may be involved in NSCLC pathogenesis. PMID: 21262974
15. VHR, a Vaccinia virus VH1-related dual-specific protein phosphatase, is phosphorylated at Y138 by ZAP-70. PMID: 12447358
16. VHR is required for cell-cycle progression as it modulates MAP kinase activation in a cell-cycle phase-dependent manner. PMID: 16604064
17. deregulated expression of BRCA1-IRIS is likely to reduce dependence on normal physiological growth stimuli PMID: 17278098
18. 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. PMID: 17785772
19. 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. PMID: 18311544
20. VHR can be considered as a new marker for cancer progression in cervix carcinoma and potential new target for anticancer therapy PMID: 18505570
21. VHR has a direct role in the inhibition of JNK-dependent apoptosis in LNCaP cells and may therefore have a role in prostate cancer progression. PMID: 19010898

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HGNC: 3069

OMIM: 600183

KEGG: hsa:1845

STRING: 9606.ENSP00000226004

UniGene: Hs.181046