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our results indicate that Nodal regulated dusp4 plays a repressive role in mesendoderm induction.
dusp4 is essential for early development; knockout of dusp4 revealed a specific loss of sox17 (show SOX17 Proteins), establishing a new class of endoderm specification defect.
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 (show SGCB Proteins)-7901 and HGC-27) and underlying molecular mechanisms
Study revealed that DUSP4 expression was apparently downregulated in the deep region of colorectal cancer (CRC (show CALR Proteins)) tissues compared with the superficial region, and that ERK (show EPHB2 Proteins) phosphorylation was conversely increased in the deep region relative to the superficial region. Also, downregulation of DUSP4 in CRC (show CALR Proteins) might promote cell proliferation and invasiveness through activation of ERK (show EPHB2 Proteins).
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.
Our findings demonstrate a genetic mechanism by which pancreatic precursor lesions progress to invasive carcinomas and highlight DUSP4 as a novel invasion suppressor
DUSP4 is crucial in regulating corticosteroid sensitivity.
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).
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.
Low DUSP4 expression levels predict recurrence and mortality in triple-negative breast cancer patients
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.
MKP-1 (show DUSP1 Proteins) and MKP-2 stability is regulated by ERK (show EPHB2 Proteins)-mediated phosphorylation through a degradation pathway independent of polyubiquitination
domain-mapping results showed that both the substrate-interacting and the phosphatase domains of DUSP4 (show DUSP9 Proteins) were required for its optimal interaction with STAT5 (show STAT5A Proteins), while the coiled-coil domain of STAT5 (show STAT5A Proteins) appeared to hinder this interaction
MKP-2 knock-out mice show deficits in working memory and spatial reference.
DUSP4 (show DUSP9 Proteins) is crucial for neuronal differentiation and functions in the neurogenesis of embryonic stem cells.
Loss of MKP-2 expression is associated with enhanced susceptibility to parasite infection.
LH/hCG (show CGA Proteins) tightly regulates MKP-2 expression, which modulates the induction of CYP11A1 (show CYP11A1 Proteins) by 8Br-cAMP.
Dusp1 (show DUSP1 Proteins) and Dusp4 (show DUSP9 Proteins) are cardioprotective genes that play a critical role in the heart by dampening p38 MAPK (show MAPK14 Proteins) signaling that would otherwise reduce contractility and induce cardiomyopathy.
Loss of MKP-2 regulates early inflammation in acute lung injury.
Increased DUSP4 (show DUSP9 Proteins) expression in activated T cells in the elderly in part accounts for defective adaptive immune responses.
protein deficiency enhances CD25 (show IL2RA Proteins) expression and CD4 (show CD4 Proteins)+ T-cell proliferation without impeding T-cell development
The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates ERK1, ERK2 and JNK, is expressed in a variety of tissues, and is localized in the nucleus. Two alternatively spliced transcript variants, encoding distinct isoforms, have been observed for this gene. In addition, multiple polyadenylation sites have been reported.
dual specificity protein phosphatase 4
, dual specificity phosphatase 4
, MAP kinase phosphatase 2
, VH1 homologous phosphatase 2
, dual specificity protein phosphatase hVH2
, mitogen-activated protein kinase phosphatase 2
, serine/threonine specific protein phosphatase