Browse our anti-DUSP4 (DUSP4) Antibodies

Zebrafish Dual Specificity Phosphatase 4 (DUSP4) interaction partners

1. our results indicate that Nodal regulated dusp4 plays a repressive role in mesendoderm induction.

2. dusp4 is essential for early development; knockout of dusp4 revealed a specific loss of sox17, establishing a new class of endoderm specification defect.

Human Dual Specificity Phosphatase 4 (DUSP4) interaction partners

1. This study was aimed to investigate the correlation of dual-specificity phosphatase 4 (DUSP4) expression with clinicopathologic features and overall survival in patients with GC and explore the effects of sanguinarine on tumour growth and invasion in GC cells (SGC-7901 and HGC-27) and underlying molecular mechanisms

2. Study revealed that DUSP4 expression was apparently downregulated in the deep region of colorectal cancer (CRC) tissues compared with the superficial region, and that ERK phosphorylation was conversely increased in the deep region relative to the superficial region. Also, downregulation of DUSP4 in CRC might promote cell proliferation and invasiveness through activation of ERK.

3. Results show that DUSP4 gene is under-expressed in ER-negative breast cancer and is deleted in approximately 50 % of breast cancers. Induced DUSP4 expression suppresses both in vitro and in vivo growths of breast cancer cells suggesting that DUSP4 is a critical regulator of the growth and invasion of triple-negative breast cancer cells.

4. Our findings demonstrate a genetic mechanism by which pancreatic precursor lesions progress to invasive carcinomas and highlight DUSP4 as a novel invasion suppressor

5. DUSP4 is crucial in regulating corticosteroid sensitivity.

6. Data indicate that normalization of dual-specific phosphatase 4 (DUSP4) expression using a specific siRNA improved CD4(+) T-cell activity in idiopathic CD4 lymphopenia (ICL).

7. Ectopic expression of wild-type DUSP4, but not of a phosphatase-deficient mutant, dephosphorylates c-JUN N-terminal kinase (JNK) and induces apoptosis in DLBCL cells.

8. Low DUSP4 expression levels predict recurrence and mortality in triple-negative breast cancer patients

9. Data suggest that MKP-2 rather than MKP-1 is tamoxifen-regulated and that the elevated expression of MKP-2 in MCF7-TAMR cells potentially functions to restore tamoxifen sensitivity.

10. MKP-1 and MKP-2 stability is regulated by ERK-mediated phosphorylation through a degradation pathway independent of polyubiquitination

11. Instead, autophagic cell death was the major consequence, and our investigation of mechanisms suggested it is mediated via the dual specificity phosphatase-4 (DUSP4) dependent ERK inactivation pathway

12. DUSP4 attenuates ERK signaling and reduces cell viability, suggesting that the novel crosstalk between NFkappaB and mitogen activated protein kinase pathways contributes to cell survival.

13. DUSP1, DUSP4, and DUSP5 differentially modulate endothelial MAPK signaling pathways downstream of Tie-2 receptors.

14. Enforced expression of DUSP4 reduced the CD44(+)/CD24(-) population in multiple BLBC cell lines in a MEK-dependent manner, limiting tumor formation of claudin-low SUM159PT cells in mice.

15. high DUSP4 expression was associated with a worse overall survival and with clinical characteristics typical for BRAF mutant patients

16. There was no significant correlation between DUSP4 expression and KRAS mutation.

17. Increased DUSP4 expression is associated with papillary thyroid carcinoma.

18. MKP2 is a negative regulator of VRK1-mediated histone H3 phosphorylation.

19. DUSP4 functions as part of a negative feedback mechanism in the control of the duration and magnitude of nuclear ERK activation during intestinal tumorigenesis.

20. High DUSP4 is associated with microsatellite instability in colorectal cancer and causes increased cell proliferation.

Mouse (Murine) Dual Specificity Phosphatase 4 (DUSP4) interaction partners

1. Signalling via ERK1/2 and tuning by its negative regulator DUSP4 are critical elements of the vasoactive intestinal peptide-directed circadian re-programming.

2. we show that the H222P amino acid substitution in lamin A enhances its binding to ERK1/2 and increases sequestration at the nuclear envelope. Finally, we show that genetic deletion of Dusp4 has beneficial effects on heart function and prolongs survival in LmnaH222P/H222P mice. These results further establish Dusp4 as a key contributor to the pathogenesis of LMNA cardiomyopathy and a potential target for drug therapy.

3. Data provide evidence that repression of the ERK inhibitor DUSP4 by BMI1 is dependent on a more accessible chromatin configuration in G4 MB cells with low CHD7 expression.

4. study suggests that MKP-2 is essential to the pathogenic response of EAE, and it acts mainly via regulating the important antigen presenting DC function and T cell activation.

5. SALL4 associated with the NuRD co-repressor and repressed expression of the tumor suppressor genes Foxl1 and Dusp4.

6. domain-mapping results showed that both the substrate-interacting and the phosphatase domains of DUSP4 were required for its optimal interaction with STAT5, while the coiled-coil domain of STAT5 appeared to hinder this interaction

7. MKP-2 knock-out mice show deficits in working memory and spatial reference.

8. DUSP4 is crucial for neuronal differentiation and functions in the neurogenesis of embryonic stem cells.

9. MKP-1 and MKP-2 stability is regulated by ERK-mediated phosphorylation through a degradation pathway independent of polyubiquitination

10. Loss of MKP-2 expression is associated with enhanced susceptibility to parasite infection.

11. LH/hCG tightly regulates MKP-2 expression, which modulates the induction of CYP11A1 by 8Br-cAMP.

12. Dusp1 and Dusp4 are cardioprotective genes that play a critical role in the heart by dampening p38 MAPK signaling that would otherwise reduce contractility and induce cardiomyopathy.

13. Loss of MKP-2 regulates early inflammation in acute lung injury.

14. Increased DUSP4 expression in activated T cells in the elderly in part accounts for defective adaptive immune responses.

15. protein deficiency enhances CD25 expression and CD4+ T-cell proliferation without impeding T-cell development

16. a critical non-redundant role for MKP-2 in regulating cell cycle progression and apoptosis.

17. These data support a mechanism by which MKP-2 targets ERK deactivation, thereby decreasing MKP-1 and thus removing the negative inhibition of MKP-1 on cytokine production.

18. E2F-1 is a transcriptional activator of MKP-2 and MKP-2 is an essential cell death mediator in the E2F-1 pathway

19. MKP-2 may play a crucial role in oncogenic signaling downstream of mutant RET, leading to deregulation of cell cycle.

20. Mediates transforming growth factor beta-dependent apoptosis by linking SMAD3 to the modulation of extracellular signal-regulated mitogen-activated protein kinase activity and pro-apoptotic events.