MAP2K1 (phospho-Ser217) Antibody
- Known as:
- MAP2K1 (phosphorilated-Ser217) Antibody
- Catalog number:
- abx000140
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- MAP2K1 (phospho-Ser217) Antibody
Related genes to: MAP2K1 (phospho-Ser217) Antibody
- Gene:
- LAMTOR3 NIH gene
- Name:
- late endosomal/lysosomal adaptor, MAPK and MTOR activator 3
- Previous symbol:
- MAP2K1IP1, MAPKSP1
- Synonyms:
- MP1, MAPBP, Ragulator3
- Chromosome:
- 4q23
- Locus Type:
- gene with protein product
- Date approved:
- 2001-05-22
- Date modifiied:
- 2016-10-05
- Gene:
- MAP2K1 NIH gene
- Name:
- mitogen-activated protein kinase kinase 1
- Previous symbol:
- PRKMK1
- Synonyms:
- MEK1, MAPKK1
- Chromosome:
- 15q22.31
- Locus Type:
- gene with protein product
- Date approved:
- 1993-11-05
- Date modifiied:
- 2019-04-23
Related products to: MAP2K1 (phospho-Ser217) Antibody
Related articles to: MAP2K1 (phospho-Ser217) Antibody
- Mesenchymal-type cancers after epithelial mesenchymal transition (EMT) were recently shown to acquire chemoresistance through expressing EMT specific transcription factors. However, druggable (or actionable) target(s) for chemoresistance in mesenchymal-type lung cancers remain unidentified. Here, we used a public clinical genomic database and mesenchymal lung cancer cells (MLCC) model derived from the A549 lung adenocarcinoma cell line to demonstrate that BCL2 expression, which is highly induced in mesenchymal-type lung cancers, as a predictor of poor prognosis in mesenchymal lung cancer patients and association with acquired chemoradioresistance. Thereby, combination treatment with BH3 mimetics, such as ABT-263 and ABT-737, clearly attenuated chemoresistance in MLCCs. BCL2 expression in MLCCs was induced by ERK1 activity through the upregulation of the MEK1/ERK1 scaffold protein MEK partner-1 (MP1). Interfering with the MEK1/MP1/ERK1 axis using a MEK1 inhibitor or MP1 depletion repressed BCL2 expression and sensitized MLCCs to chemoradiotherapy. Taken together, our results suggest that targeting druggable proteins in the MEK1/MP1/ERK1/BCL2 axis, such as MEK1 or BCL2, with currently available FDA approved drugs is a currently feasible approach to improve clinical outcomes of mesenchymal lung cancer patients. - Source: PubMed
Publication date: 2017/06/10
Kwon Ok-SeonHong Soon-KiKwon Soo-JungGo Young-HyunOh EnselCha Hyuk-Jin - The extracellular signal-regulated kinase (ERK) cascade regulates proliferation, differentiation, and survival in multicellular organisms. Scaffold proteins regulate intracellular signaling by providing critical spatial and temporal specificity. The scaffold protein MEK1 (mitogen-activated protein kinase and ERK kinase 1) partner (MP1) is localized to late endosomes by the adaptor protein p14. Using conditional gene disruption of p14 in mice, we now demonstrate that the p14-MP1-MEK1 signaling complex regulates late endosomal traffic and cellular proliferation. This function its essential for early embryogenesis and during tissue homeostasis, as revealed by epidermis-specific deletion of p14. These findings show that endosomal p14-MP1-MEK1 signaling has a specific and essential function in vivo and, therefore, indicate that regulation of late endosomal traffic by extracellular signals is required to maintain tissue homeostasis. - Source: PubMed
Teis DavidTaub NicoleKurzbauer RobertHilber Dianade Araujo Mariana EErlacher MiriamOffterdinger MartinVillunger AndreasGeley StephanBohn GeorgKlein ChristophHess Michael WHuber Lukas A - Eukaryotic cells use the extracellular signal regulated kinase (ERK) cascade to connect cell-surface receptors to intracellular targets. Although various signals are routed through the ERK pathway, cells respond accordingly to a given stimulus. To regulate proper signal transduction, scaffolds and adaptors are employed to organize specific signaling units. The scaffold protein MP1 (MEK1 partner) assembles a scaffold complex in the ERK cascade. We show that p14 functions as an adaptor protein, which is required and sufficient to localize MP1 to endosomes. Reduction of MP1 or p14 protein levels by siRNAi results in defective signal transduction. Therefore, our results suggest that the endosomal localization of the p14/MP1-MAPK scaffold complex is crucial for signal transduction. - Source: PubMed
Teis DavidWunderlich WinfriedHuber Lukas A