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Dual specificity phosphatase 3

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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: H1, ACID, MKP-1, Protein-Tyrosine-Phosphatase, ERK
Papers on VHR
New neo-lignan from Acanthopanax senticosus with protein tyrosine phosphatase 1B inhibitory activity.
Cui et al., Jilin, China. In Arch Pharm Res, Oct 2015
All the isolates were evaluated for in vitro inhibitory activity against PTP1B, VHR and PP1.
Perspective: Tyrosine phosphatases as novel targets for antiplatelet therapy.
Rahmouni et al., Los Angeles, United States. In Bioorg Med Chem, Jul 2015
We also introduce VHR (DUSP3), a PTP that we recently identified as a major player in platelet biology and thrombosis.
Focused library with a core structure extracted from natural products and modified: application to phosphatase inhibitors and several biochemical findings.
Sodeoka et al., Wako, Japan. In Acc Chem Res, Jun 2015
The resulting compounds showed dramatically improved cell membrane permeability and inhibitory selectivity and included VHR (vaccinia VH1-related)-selective RE12 and CDC25A/B (cell division cycle 25A/B)-selective RE44.
VHR/DUSP3 phosphatase: structure, function and regulation.
Köhn et al., Heidelberg, Germany. In Febs J, May 2015
VHR/DUSP3 has been implicated in several human cancers, where its tumor-suppressing and -promoting properties have been described.
Combined experimental and bioinformatics analysis for the prediction and identification of VHR/DUSP3 nuclear targets related to DNA damage and repair.
Forti, São Paulo, Brazil. In Integr Biol (camb), 2015
Here, we combined experimental and computational tools to identify new substrates and protein partners of VHR (DUSP3) phosphatase in HeLa cells exposed to genotoxic stress.
Good Outcome for Very High Risk Adult B-cell Acute Lymphoblastic Leukaemia Carrying Genetic Abnormalities t(4;11)(q21;q23) or t(9;22)(q34;q11), if Promptly Submitted to Allogeneic Transplantation, after Obtaining a Good Molecular Remission.
Pioltelli et al., Monza, Italy. In Mediterr J Hematol Infect Dis, 2014
BACKGROUND AND OBJECTIVES: Acute lymphoblastic leukaemia (ALL) carrying t(9;22) or t(4;11) genetic abnormalities represents a very high risk subtype of disease (VHR-ALL).
Removal of a small C-terminal region of JCV and SV40 large T antigens has differential effects on transformation.
Pipas et al., Pittsburgh, United States. In Virology, 2014
When the least conserved region of the LT proteins, the variable linker and host range region (VHR), was removed, changes in T antigen expression and cellular p53 post-translational modifications occurred, but interaction with the pRB pathway was unaffected.
DUSP3/VHR is a pro-angiogenic atypical dual-specificity phosphatase.
Rahmouni et al., Liège, Belgium. In Mol Cancer, 2013
BACKGROUND: DUSP3 phosphatase, also known as Vaccinia-H1 Related (VHR) phosphatase, encoded by DUSP3/Dusp3 gene, is a relatively small member of the dual-specificity protein phosphatases.
Trials and Tribulations with VH Replacement.
Luning Prak et al., Philadelphia, United States. In Front Immunol, 2013
VH replacement (VHR) is a type of antibody gene rearrangement in which an upstream heavy chain variable gene segment (VH) invades a pre-existing rearrangement (VDJ).
[Development of novel types of biologically active compounds based on natural products and biomolecules].
Hirai, Wako, Japan. In Yakugaku Zasshi, 2011
As inhibitors for the dual-specificity protein phosphatase VHR, the neutral phosphate-mimicking core structure was designed based on natural product RK-682.
Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3.
Neish et al., Atlanta, United States. In J Biol Chem, 2011
Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3
Vaccinia H1-related phosphatase is a phosphatase of ErbB receptors and is down-regulated in non-small cell lung cancer.
Chen et al., Taiwan. In J Biol Chem, 2011
VHR expression enhances the signaling of ErbB receptors and may be involved in NSCLC pathogenesis.
Small-Molecule Inhibitors of Vaccinia-H1-Related Phosphatase VHR
Chung et al., Bethesda, United States. In Unknown Journal, 2009
Vaccinia H1-related (VHR) protein tyrosine phosphatase dephosphorylates and thereby inactivates extracellular signal-regulated kinases Erk1/2 and c-Jun N-terminal kinases Jnk1/2.
The mitogen-activated protein kinase phosphatase vaccinia H1-related protein inhibits apoptosis in prostate cancer cells and is overexpressed in prostate cancer.
Saatcioglu et al., Oslo, Norway. In Cancer Res, 2008
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.
High intracellular Zn2+ ions modulate the VHR, ZAP-70 and ERK activities of LNCaP prostate cancer cells.
Abubakar et al., Kuala Lumpur, Malaysia. In Cell Mol Biol Lett, 2007
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.
Cervix carcinoma is associated with an up-regulation and nuclear localization of the dual-specificity protein phosphatase VHR.
Rahmouni et al., Liège, Belgium. In Bmc Cancer, 2007
VHR can be considered as a new marker for cancer progression in cervix carcinoma and potential new target for anticancer therapy
Negative regulation of ERK activity by VRK3-mediated activation of VHR phosphatase.
Kim et al., South Korea. In Nat Cell Biol, 2006
Here, we show that VRK3 suppresses ERK activity through direct binding to one of the MKPs, vaccinia H1-related (VHR), which specifically dephosphorylates and inactivates ERK in the nucleus.
Loss of the VHR dual-specific phosphatase causes cell-cycle arrest and senescence.
Mustelin et al., Los Angeles, United States. In Nat Cell Biol, 2006
VHR is required for cell-cycle progression as it modulates MAP kinase activation in a cell-cycle phase-dependent manner.
Tyrosine phosphorylation of VHR phosphatase by ZAP-70.
Mustelin et al., Los Angeles, United States. In Nat Immunol, 2003
VHR, a Vaccinia virus VH1-related dual-specific protein phosphatase, is phosphorylated at Y138 by ZAP-70.
Crystal structure of the dual specificity protein phosphatase VHR.
Saper et al., Ann Arbor, United States. In Science, 1996
Here, the crystal structure of a human DSP, vaccinia H1-related phosphatase (or VHR), was determined at 2.1 angstrom resolution.
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