| DUSP3 modulates IRES-dependent translation of mRNAs through dephosphorylation of the HNRNPC protein in cells under genotoxic stimulus. | DUSP3 modulates IRES-dependent translation of mRNAs through dephosphorylation of the HNRNPC protein in cells under genotoxic stimulus.
Ferruzo PYM, Boell VK, Russo LC, Oliveira CC, Forti FL. | 06/5/2024 |
| The role of dual-specificity phosphatase 3 in melanocytic oncogenesis. | The role of dual-specificity phosphatase 3 in melanocytic oncogenesis.
Chousakos E, Katsoulas N, Kavantzas N, Stratigos A, Lazaris AC. | 10/8/2022 |
| DUSP3 maintains genomic stability and cell proliferation by modulating NER pathway and cell cycle regulatory proteins. | DUSP3 maintains genomic stability and cell proliferation by modulating NER pathway and cell cycle regulatory proteins.
Russo LC, Farias JO, Forti FL., Free PMC Article | 08/28/2021 |
| Regulation of signal transducer and activator of transcription 3 activation by dual-specificity phosphatase 3. | Regulation of signal transducer and activator of transcription 3 activation by dual-specificity phosphatase 3.
Kim BR, Ha J, Kang E, Cho S., Free PMC Article | 02/13/2021 |
| Allosteric Impact of the Variable Insert Loop in Vaccinia H1-Related (VHR) Phosphatase. | Allosteric Impact of the Variable Insert Loop in Vaccinia H1-Related (VHR) Phosphatase.
Beaumont VA, Reiss K, Qu Z, Allen B, Batista VS, Loria JP., Free PMC Article | 01/23/2021 |
| 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. | Identification of serum miR-1915-3p and miR-455-3p as biomarkers for breast cancer.
Guo J, Liu C, Wang W, Liu Y, He H, Chen C, Xiang R, Luo Y., Free PMC Article | 01/12/2019 |
| 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. | VRK3-mediated nuclear localization of HSP70 prevents glutamate excitotoxicity-induced apoptosis and Aβ accumulation via enhancement of ERK phosphatase VHR activity.
Song H, Kim W, Kim SH, Kim KT., Free PMC Article | 06/9/2018 |
| Data indicated that regulating non-receptor tyrosine kinase FAK and cell migration is a newly revealed function of VHR/DUSP3. | Deficiency in VHR/DUSP3, a suppressor of focal adhesion kinase, reveals its role in regulating cell adhesion and migration.
Chen YR, Chou HC, Yang CH, Chen HY, Liu YW, Lin TY, Yeh CL, Chao WT, Tsou HH, Chuang HC, Tan TH. | 12/9/2017 |
| The loss of DUSP3 activity markedly increases gamma radiation-induced DNA strand breaks, suggesting a potential novel role for DUSP3 in DNA repair. | Loss of DUSP3 activity radiosensitizes human tumor cell lines via attenuation of DNA repair pathways.
Torres TEP, Russo LC, Santos A, Marques GR, Magalhaes YT, Tabassum S, Forti FL. | 11/4/2017 |
| In PTP1B and VHR, two new allosteric clusters were identified in each enzyme. | Leveraging Reciprocity to Identify and Characterize Unknown Allosteric Sites in Protein Tyrosine Phosphatases.
Cui DS, Beaumont V, Ginther PS, Lipchock JM, Loria JP., Free PMC Article | 07/29/2017 |
| 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. | Reduced levels of Dusp3/Vhr phosphatase impair normal spindle bipolarity in an Erk1/2 activity-dependent manner.
Tambe MB, Narvi E, Kallio M. | 05/13/2017 |
| 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. | Dusp3 and Psme3 are associated with murine susceptibility to Staphylococcus aureus infection and human sepsis.
Yan Q, Sharma-Kuinkel BK, Deshmukh H, Tsalik EL, Cyr DD, Lucas J, Woods CW, Scott WK, Sempowski GD, Thaden JT, Rude TH, Ahn SH, Fowler VG Jr., Free PMC Article | 08/15/2015 |
| Our results demonstrate that DUSP3 plays a key and nonredundant role as a regulator of innate immune responses | DUSP3 Genetic Deletion Confers M2-like Macrophage-Dependent Tolerance to Septic Shock.
Singh P, Dejager L, Amand M, Theatre E, Vandereyken M, Zurashvili T, Singh M, Mack M, Timmermans S, Musumeci L, Dejardin E, Mustelin T, Van Ginderachter JA, Moutschen M, Oury C, Libert C, Rahmouni S., Free PMC Article | 07/25/2015 |
| VHR can dimerize inside cells, and that VHR catalytic activity is reduced upon dimerization. | Unnatural amino acid mutagenesis reveals dimerization as a negative regulatory mechanism of VHR's phosphatase activity.
Pavic K, Rios P, Dzeyk K, Koehler C, Lemke EA, Köhn M. | 02/28/2015 |
| DUSP3 is a pro-angiogenic atypical dual-specificity phosphatase. | DUSP3/VHR is a pro-angiogenic atypical dual-specificity phosphatase.
Amand M, Erpicum C, Bajou K, Cerignoli F, Blacher S, Martin M, Dequiedt F, Drion P, Singh P, Zurashvili T, Vandereyken M, Musumeci L, Mustelin T, Moutschen M, Gilles C, Noel A, Rahmouni S., Free PMC Article | 01/17/2015 |
| DUSP3 interacting partners are nucleolar proteins involved in processes related to DNA repair and senescence. | Proteomic, cellular, and network analyses reveal new DUSP3 interactions with nucleolar proteins in HeLa cells.
Panico K, Forti FL. | 08/30/2014 |
| we report the first successful site-specific incorporation of sulfotyrisine into VHR through the use of expanding genetic code | A genetically encoded sulfotyrosine for VHR function research.
Zheng Y, Lv X, Wang J., Free PMC Article | 05/10/2014 |
| 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. | Specificity profiling of dual specificity phosphatase vaccinia VH1-related (VHR) reveals two distinct substrate binding modes.
Luechapanichkul R, Chen X, Taha HA, Vyas S, Guan X, Freitas MA, Hadad CM, Pei D., Free PMC Article | 05/11/2013 |
| Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3 | Enteric commensal bacteria induce extracellular signal-regulated kinase pathway signaling via formyl peptide receptor-dependent redox modulation of dual specific phosphatase 3.
Wentworth CC, Alam A, Jones RM, Nusrat A, Neish AS., Free PMC Article | 01/14/2012 |
| VHR expression enhances the signaling of ErbB receptors and may be involved in NSCLC pathogenesis. | Vaccinia H1-related phosphatase is a phosphatase of ErbB receptors and is down-regulated in non-small cell lung cancer.
Wang JY, Yeh CL, Chou HC, Yang CH, Fu YN, Chen YT, Cheng HW, Huang CY, Liu HP, Huang SF, Chen YR., Free PMC Article | 06/18/2011 |
| VHR can be considered as a new marker for cancer progression in cervix carcinoma and potential new target for anticancer therapy | Cervix carcinoma is associated with an up-regulation and nuclear localization of the dual-specificity protein phosphatase VHR.
Henkens R, Delvenne P, Arafa M, Moutschen M, Zeddou M, Tautz L, Boniver J, Mustelin T, Rahmouni S., Free PMC Article | 01/21/2010 |
| 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. | High intracellular Zn2+ ions modulate the VHR, ZAP-70 and ERK activities of LNCaP prostate cancer cells.
Wong PF, Abubakar S., Free PMC Article | 01/21/2010 |
| 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. | The mitogen-activated protein kinase phosphatase vaccinia H1-related protein inhibits apoptosis in prostate cancer cells and is overexpressed in prostate cancer.
Arnoldussen YJ, Lorenzo PI, Pretorius ME, Waehre H, Risberg B, Maelandsmo GM, Danielsen HE, Saatcioglu F. | 01/21/2010 |
| 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. | Cutting edge: selective tyrosine dephosphorylation of interferon-activated nuclear STAT5 by the VHR phosphatase.
Hoyt R, Zhu W, Cerignoli F, Alonso A, Mustelin T, David M., Free PMC Article | 01/21/2010 |
| VHR is required for cell-cycle progression as it modulates MAP kinase activation in a cell-cycle phase-dependent manner. | Loss of the VHR dual-specific phosphatase causes cell-cycle arrest and senescence.
Rahmouni S, Cerignoli F, Alonso A, Tsutji T, Henkens R, Zhu C, Louis-dit-Sully C, Moutschen M, Jiang W, Mustelin T. | 01/21/2010 |