Browse our anti-Dual Specificity Phosphatase 3 (DUSP3) Antibodies

Human Dual Specificity Phosphatase 3 (DUSP3) interaction partners

1. Study demonstrated that miR-1915-3p might promote the proliferation and metastasis of breast cancer by repression of DUSP3 and serum miR-1915-3p and miR-455-3p could serve as diagnostic and predictive biomarkers for breast cancer.

2. 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.

3. Data indicated that regulating non-receptor tyrosine kinase FAK and cell migration is a newly revealed function of VHR/DUSP3.

4. The loss of DUSP3 activity markedly increases gamma radiation-induced DNA strand breaks, suggesting a potential novel role for DUSP3 in DNA repair.

5. In PTP1B and VHR, two new allosteric clusters were identified in each enzyme.

6. 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.

7. 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.

8. Our results demonstrate that DUSP3 plays a key and nonredundant role as a regulator of innate immune responses

9. VHR can dimerize inside cells, and that VHR catalytic activity is reduced upon dimerization.

10. DUSP3 is a pro-angiogenic atypical dual-specificity phosphatase.

11. DUSP3 interacting partners are nucleolar proteins involved in processes related to DNA repair and senescence.

12. we report the first successful site-specific incorporation of sulfotyrisine into VHR through the use of expanding genetic code

13. 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.

14. Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3

15. VHR expression enhances the signaling of ErbB receptors and may be involved in NSCLC pathogenesis.

16. VHR, a Vaccinia virus VH1-related dual-specific protein phosphatase, is phosphorylated at Y138 by ZAP-70.

17. VHR is required for cell-cycle progression as it modulates MAP kinase activation in a cell-cycle phase-dependent manner.

18. deregulated expression of BRCA1-IRIS is likely to reduce dependence on normal physiological growth stimuli

19. 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.

20. 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.

Mouse (Murine) Dual Specificity Phosphatase 3 (DUSP3) interaction partners

1. Data indicated that regulating non-receptor tyrosine kinase FAK and cell migration is a newly revealed function of VHR/DUSP3.

2. DUSP3 phosphatase plays a key role in metastatic growth.

3. At the molecular level, DUSP3 deletion was associated with estrogen-dependent decreased phosphorylation of ERK1/2 and Akt in peritoneal macrophages stimulated ex vivo by LPS; results demonstrate that estrogens may modulate M2-like responses during endotoxemia in a DUSP3-dependent manner

4. 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.

5. Platelets from DUSP3-deficient mice displayed a selective impairment of aggregation and granule secretion.

6. Our results demonstrate that DUSP3 plays a key and nonredundant role as a regulator of innate immune responses

7. DUSP3 is a pro-angiogenic atypical dual-specificity phosphatase.

8. Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3