MAP2K6 (phospho-Ser207) Antibody
- Known as:
- MAP2K6 (phosphorilated-Ser207) Antibody
- Catalog number:
- abx000154
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- MAP2K6 (phospho-Ser207) Antibody
Related genes to: MAP2K6 (phospho-Ser207) Antibody
- Gene:
- MAP2K6 NIH gene
- Name:
- mitogen-activated protein kinase kinase 6
- Previous symbol:
- PRKMK6
- Synonyms:
- MEK6, MKK6, SAPKK3, MAPKK6
- Chromosome:
- 17q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 1997-11-11
- Date modifiied:
- 2016-01-15
Related products to: MAP2K6 (phospho-Ser207) Antibody
Related articles to: MAP2K6 (phospho-Ser207) Antibody
- Chicken coccidiosis inflicts severe economic losses on the poultry industry. The mechanisms underlying Eimeria tenella (E. tenella) invasion, colonization, and damage to host cells remain incompletely elucidated. This study was designed to elucidate EtMIC2-interacting proteins and the mechanism that EtMIC2 regulates E. tenella invasion and host cell apoptosis. His pull-down-MS and KEGG enrichment results showed apoptosis-related proteins including ITGAV (Integrin alpha-V), PlexinB2, MAP2K6, GNA11, TRK, CASP7, PAK1, and RAP1b. Only the interaction model between EtMIC2 and ITGAV met the AlphaFold2 thresholds (pLDDT > 70, pTM+ipTM > 0.75). The CO-IP results showed that in the primary host cells (CECs) of E. tenella, protein bands corresponding to EtMIC2 (50 kDa) and ITGAV (135 kDa) were successfully detected in the IP group. Blue colony growth on SD/-Ade,-His,-Leu,-Trp/X-α-Gal plates for the group pGBKT7-EtMIC2 or pGBKT7-EtMIC2-3 (153-1029 bp) or pGBKT7-EtMIC2-5 (855-1029 bp) co-transformed with pGADT7-ITGAV in Yeast Two-Hybrid assay. Green fluorescence was observed in DF-1 cells pBiFC-EtMIC2-VN173 or pBiFC-EtMIC2-3-VN173 or pBiFC-EtMIC2-5-VN173 were co-transfected with pBiFC-ITGAV-VC155 in Bimolecular fluorescence complementation. The addition of EtMIC2 protein significantly increased (P < 0.05) E. tenella infection rate, gene expression and protein activity of ITGAV, FAK, PLC, PKC, p65, PI3K, Akt, ERK, and Bcl2, and reduced host cell Caspase 3 activity, apoptosis rate, gene expression and protein activity of JNK, p38, Bax, and Caspase 3. Knockdown of ITGAV produced the opposite effects. The function of EtMIC2 was prevented following the knockdown of ITGAV. The above finding indicate that the EtMIC2 855-1029 bp (285-342 aa) region interacts with ITGAV, leading to the upregulation of ITGAV, FAK, PLC, PKC, p65, PI3K, Akt, ERK, and Bcl2, while downregulating JNK, p38, Bax, and Caspase 3, thereby promoting E. tenella invasion and inhibiting host cell apoptosis. - Source: PubMed
Publication date: 2026/04/09
Cui Kai-LingGuo Lu-LuLei XuanChen Ying-YingLiu Kui-HaoDuan Bu-TingZhang Hong-HuiLv Xiao-LingZheng Ming-Xue - Despite significant advancements in atopic dermatitis (AD) treatment, the underlying pathogenesis remains unclear. Understanding flare and remission mechanisms is essential for understanding disease course, evaluating treatment and developing therapeutic strategies. Although biomarkers show promise for assessing disease severity, their identification, validation and clinical utility demand further research. - Source: PubMed
Publication date: 2026/04/20
Olydam Jill IsabelleLitman ThomasNijsten TamarHoof IlkaKoopmann WittePardo Luba MilenaHijnen DirkJan - The mitogen-activated protein kinase (MAPK) pathway widely regulates development and cancer. However, the subcellular localization and function of the secondary kinases in the MAPK pathway remain unclear. Here, we identified mitogen-activated protein kinase kinase 6 or 3 (MKK6/MKK3) as tumor suppressors that could significantly activate mitophagy and suppress tumor growth in lung adenocarcinoma (LUAD). Mechanistically, among MKK1-7, only MKK6/MKK3 exhibited subcellular organellar localization in mitochondria and autophagosome interaction site. The function of MKK6 in mitophagy and tumorigenicity was dependent on its kinase activity, but not through p38. MKK6 directly phosphorylated BCL2L13 at serine 426, enhancing the interaction between BCL2L13 and LC3B, which, in turn, promoted mitophagy, inhibited oxidative phosphorylation (OXPHOS), and prevented tumor growth. Our studies not only revealed that MKK6-BCL2L13 phosphorylation at the interorganellar site can affect mitochondrial quality in tumorigenicity but also might provide a potential therapeutic strategy for LUAD treatment. - Source: PubMed
Publication date: 2026/03/24
Xing GuangsuoHuang YileLiu XiwenLi LinpengLiu ZichaoWu YiZhou YanshuangDing YingzheChen BaodanXue GuanruLi ZijingHao ZhihongLiu YangFan WenhuiDing HaolinLiang ShanHe JingcaiWang JunweiZhang JianQin DajiangWang WumingLu GangChan Wai-YeeRan PixinJu HuaiqiangDong MingLiang WenhuaLiu XingguoChen Keshi - The MAPK p38α is associated with skeletal muscle's development, differentiation and functionality. But, as it is overactive in muscle diseases and aging, it was proposed to be a pivotal promoter of these processes as well. It is not clear how p38α is involved in these disparate activities, in particular whether its chronic activation alone is sufficient to cause them. We established a mouse model designed to study the effects of p38α per se in skeletal muscle. p38α activation is achieved by inducible expression, in muscle, of an intrinsically active variant, p38α. Two weeks following expression muscle degeneration and necrotic changes were observed, accompanied with elevation of p53, caspase 3, and γH2AX; and, intriguingly, suppression of the p38's substrates MK2 and MK3 and its activator MKK6. At later timepoints the tissue recovered, apoptotic markers disappeared, but MK2, MK3, and MKK6 remained suppressed, perhaps as a response that restrains p38α-mediated damage and allows recovery. Induction of p38α in young mice (2 months old) caused milder effects, but MK2, MK3, and MKK6 were suppressed. The p38α effects were associated with altered level of ∼2000 mRNA molecules. For 1700 genes, the effect was transient and for ∼300 constant. Stress-induced activation of p38α in C2C12 myoblasts was also associated with MK2 downregulation, but with constant elevation of apoptotic markers. Thus, chronic activation of p38α per se in skeletal muscle is sufficient to cause damage reminiscent of aging effects, but cannot impose full-scale and lasting aging phenotype. The tissue recovers while suppressing the p38α pathway. - Source: PubMed
Publication date: 2026/03/04
Gilad NechamaDarlyuk-Saadon IlonaMohanam Manju PayiniEngelberg David - Due to a lack of information related to molecular changes in heroin use, we aimed to examine heroin-dependent alterations in different regions of the post-mortem human brain. Tissues were obtained from males (n = 24 heroin users, n = 24 controls) through the Turkish Forensic Medicine Institute after structured verbal interviews with the relatives of the deceased to gather history of substance use. Following toxicological confirmation of heroin use, the hippocampus, putamen, and caudate nucleus were dissected from the left hemispheres. Proteomic analyses were performed using a high-resolution liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) system. Label-free quantitative analysis revealed significant differential expression of 87 proteins in the hippocampus, 121 proteins in the putamen, and 80 proteins in the caudate nucleus compared to controls. These differentially expressed proteins (DEPs) were subsequently used to construct protein-protein interaction (PPI) networks using the STRING database, revealing significantly enriched and highly interconnected interaction networks in all three regions. Gene Ontology (GO) enrichment analysis of DEPs consistently identified extracellular exosome, extracellular space, and vesicle as the top three cellular components. Molecular function enrichment further indicated alterations in signaling, binding, and stress-related processes. The expression of TST, RYR2, ACTBL2, and RPS27 decreased, whereas the expression of COL4A2, OGN, PMP2, and MAP2K6 increased in the hippocampus. In the putamen, the most prominent increases were observed in DNM2 and MADD expression. In the caudate nucleus, the expressions of RPS6KA2, TMED10, and NBEA proteins decreased, whereas HPX protein expression increased. Overall, these alterations promote oxidative stress and molecular changes linked to neurodegeneration, which likely contribute to impaired neuronal function and synaptic plasticity. - Source: PubMed
Publication date: 2026/02/21
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