DUSP6
- Known as:
- DUSP6
- Catalog number:
- 000585A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- DUSP6
Related genes to: DUSP6
- Gene:
- DUSP6 NIH gene
- Name:
- dual specificity phosphatase 6
- Previous symbol:
- -
- Synonyms:
- MKP-3, PYST1
- Chromosome:
- 12q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 1997-03-19
- Date modifiied:
- 2016-01-15
Related products to: DUSP6
Related articles to: DUSP6
- Psoriasis is a chronic inflammatory skin disease characterised by keratinocyte hyperproliferation and immune cell infiltration driven by cytokines such as IL-17A. The dual-specificity phosphatase 6 (DUSP6) is a negative regulator of MAPK signalling and was previously reported to be a key mediator of arthritis severity. Here, we examine the role of DUSP6 in a mouse model of psoriasis. Psoriasis was studied in the imiquimod-induced model (IMQ). The skin of DUSP6+/+ and DUSP6-/- mice was treated with IMQ cream. Disease severity was assessed using well-established clinical and histologic systems. Skin inflammatory genes were quantified by qPCR.DUSP6-/- mice exhibited significantly reduced skin inflammation with lower PASI clinical scores (mean DUSP6-/- 1.8 and DUSP6+/+ 8.4; p < 0.0001). Histologic scores for epidermal thickening, parakeratosis and immune cell infiltration were decreased in the DUSP6-/- mice (p < 0.0005), and mRNA levels of IL1β, IL17A and STAT3 were lower in DUSP6-/- skin (p ≤ 0.05) compared with DUSP6+/+. In conclusion, DUSP6 is required for the development of psoriasis-like skin inflammation in mice. In the absence of DUSP6, mice were protected and had significantly lower levels of pathogenic genes, suggesting a new and central role for DUSP6 in skin inflammation and a potential therapeutic target in psoriasis. - Source: PubMed
Laragione TeresinaHarris CarolynPhelps RobertGulko Percio S - Myocardial infarction (MI) is the most severe clinical manifestation of coronary artery diseases (CVD) and serves as a critical driver of sudden cardiac death and heart failure (HF). Its pathophysiology begins with the abrupt cessation of coronary blood flow, leading to severe ischemia and subsequent cardiomyocyte necrosis. This study aimed to investigate the molecular mechanisms by which METTL14 regulates the progression of MI in mice via the OTUD1/DUSP6 signaling axis. An MI mouse model was established by ligating the left anterior descending (LAD) coronary artery. The progression of MI was evaluated through echocardiography, HE staining, Masson's trichrome staining, TUNEL assay, and assessment of inflammatory cytokines. Mechanistically, Me-RIP, PAR-CLIP Co-IP, and protein stability assays were performed to dissect the interactions within the METTL14/OTUD1/DUSP6 axis. Our results demonstrated that METTL14 was highly expressed in the MI mouse model. Silencing METTL14 significantly reduced the left Ventricular Internal Diameter at end-diastole (LVIDd) and left Ventricular Internal Diameter at end-systole (LVIDs), increased ejection fraction (EF) and fractional shortening (FS), and attenuated histopathological damage, apoptosis, and the levels of inflammatory cytokines (TNF-α and IL-β). Further analysis revealed that METTL14 promotes OTUD1 mRNA stability and expression by modulating its mA modification. In turn, METTL14 influences DUSP6 expression by regulating OTUD1-mediated ubiquitination. Collectively, silencing METTL14 modulates the MI disease process through the OTUD1/DUSP6 signaling axis, suggesting that METTL14 plays a pivotal role in MI progression. These findings indicate that targeting METTL14 may represent a potential therapeutic strategy to alleviate pathological injury, apoptosis, and inflammation during MI. - Source: PubMed
Publication date: 2026/03/30
Wei Cheng-ChengShen Ya-FangZhang Jin-Yu - Of all the skin malignancies, melanoma is the most invasive and challenging to treat. Melanoma patients have a poor prognosis and a high recurrence rate despite advancements in treatment. There is substantial evidence that plant-derived bioactives prevent and treat melanoma effectively. The naturally occurring bioactive compound dalbergin, found in certain species of the genus, such as , is a neoflavanoid that has been studied for its various biological and pharmacological properties, including its anticancer activity. Nevertheless, it is uncertain what mechanism underpins its anti-melanoma therapeutic benefits. This study aims to predict potential target proteins and suggest a possible molecular mechanism for dalbergin against melanoma using multiple systems biology databases and tools. Melanoma targets were identified through online databases and compared to proteins that were anticipated to be affected by dalbergin. Furthermore, pathways such as the MAPK signalling pathway, signal transduction, transcriptional control, and apoptosis regulation were identified using KEGG pathway analysis. Cytoscape was used to build a protein-protein interaction network, and six melanoma-associated hub targets, ERK1, ERK2, MAPK14, PTPN11, CDKN1B, and DUSP6, were identified through network analysis. Molecular docking studies demonstrated strong binding between dalbergin and the selected target proteins, with ERK1 showing the best binding (- 9.7 kcal/mol). Molecular dynamics simulations were performed for over 100 ns after molecular docking to confirm the structural stability of the dalbergin and ERK1/ERK2 complexes. This indicates the rationale for dalbergin as a potential bioactive in melanoma treatment. However, these predictions require confirmation through relevant and experimental studies to verify the precise mechanism, which is a limitation of the present work and a future scope. - Source: PubMed
Publication date: 2026/03/22
Vijh DeepanshiSingh AryamanMansi Khanna LeenaGupta Promila - Apoptosis plays a significant role in osteoporosis (OP), yet a causal relationship between apoptosis gene expressions and OP remains unexplored. This study applies an integrated multi-omics analysis to establish causality between them, offering clinical treatment and prediction insights. - Source: PubMed
Publication date: 2026/03/23
Wang YixiXia LintaoXiao YangWu MingxingZhang RuiRexiti PaerhatiZhang Hui - Mitogen-activated protein kinase (MAPK) phosphatases [MKPs, also known as dual-specificity phosphatases (DUSPs)] regulate MAPKs -key mediators of cellular processes such as proliferation, differentiation, and survival- by dephosphorylating the threonine and tyrosine residues required for MAPK activation. MKP-3/DUSP6 is an ERK-selective phosphatase that has also been reported to regulate the transcription factor FOXO1. The full-length MKP-3 transcript has been shown to encode the MKP-3L protein, whereas alternative splicing gives rise to the shorter isoform MKP-3S. However, the available information regarding the functional differences between these variants is limited. By combining biochemical and bioinformatic approaches, we demonstrate that these isoforms differ significantly in subcellular localization and enzymatic activity. Structural analysis and molecular docking reveal that while MKP-3S retains functional binding domains and recognizes ERK2 similarly to the full-length isoform. However, the absence of critical catalytic motifs in MKP-3S leads to a structural uncoupling where the protein retains its ability to bind ERK2 but fails to induce dephosphorylation, suggesting a non-canonical role as a molecular scaffold. The results obtained demonstrate significant variations in subcellular localization, enzymatic activity, and the capacity to modulate FOXO1 transcriptional activity. This, in turn, affects the expression of genes such as p21. In conclusion, the findings indicate that MKP-3 variants exhibit distinct functional behaviours, which may result in differential regulation of a wide range of cellular processes. - Source: PubMed
Publication date: 2026/03/17
Mori Sequeiros Garcia María MercedesNudler SilvanaBigi María MercedesCohen Sabban Juan ManuelPoderoso CeciliaMaloberti Paula MarianaPaz Cristina