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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.
In PTP1B (show PTPN1 Proteins) and VHR, two new allosteric clusters were identified in each enzyme.
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.
Data suggest levels of gene expression of both DUSP3 (dual specificity phosphatase 3) and PSME3 (proteasome activator subunit 3 (show PSME3 Proteins)) are associated with susceptibility to Staphylococcus aureus infection/sepsis in humans and in mouse disease model.
Our results demonstrate that DUSP3 plays a key and nonredundant role as a regulator of innate immune responses
VHR can dimerize inside cells, and that VHR catalytic activity is reduced upon dimerization.
DUSP3 is a pro-angiogenic atypical dual-specificity phosphatase.
DUSP3 interacting partners are nucleolar proteins involved in processes related to DNA repair and senescence.
we report the first successful site-specific incorporation of sulfotyrisine into VHR through the use of expanding genetic code
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 (show TYR Proteins)(P) proteins in vivo.
DUSP3 phosphatase plays a key role in metastatic growth.
At the molecular level, DUSP3 deletion was associated with estrogen-dependent decreased phosphorylation of ERK1/2 and Akt (show AKT1 Proteins) in peritoneal macrophages stimulated ex vivo by LPS (show TLR4 Proteins); results demonstrate that estrogens may modulate M2-like responses during endotoxemia in a DUSP3-dependent manner
Data suggest levels of gene expression of both Dusp3 (dual specificity phosphatase 3) and Psme3 (proteasome activator subunit 3 (show PSME3 Proteins)) are associated with susceptibility to Staphylococcus aureus infection/sepsis in humans and in mouse disease model.
Platelets from DUSP3-deficient mice displayed a selective impairment of aggregation and granule secretion.
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 maps in a region that contains the BRCA1 locus which confers susceptibility to breast and ovarian cancer. Although DUSP3 is expressed in both breast and ovarian tissues, mutation screening in breast cancer pedigrees and in sporadic tumors was negative, leading to the conclusion that this gene is not BRCA1.
dual specificity phosphatase 3 (vaccinia virus phosphatase VH1-related)
, dual specificity phosphatase 3
, dual specificity protein phosphatase 3
, dual specificity protein phosphatase VHR
, serine/threonine specific protein phosphatase
, vaccinia H1-related phosphatase
, vaccinia virus phosphatase VH1-related