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Through extensive analysis of the gene expression patterns in cells with activated forms of Ras and Rho families, it was found that Ephexin1 was highly upregulated by H-Ras G12V in NIH3T3 cells. It is phosphorylated by the Src family of kinases and by fibroblast growth factor receptor signaling, leading to the regulation of GEF activity, which in turn regulates actin cytoskeletal dynamics. Ephexin1 is highly expressed in the nervous system during development and is involved in many neurophysiological events. Despite decades of effort, many aspects of the molecular mechanism underlying Ras-induced tumorigenesis and possible therapeutic targeting remain difficult to identify.Įphexin1 is a member of the DbI family of guanine nucleotide exchange factors (GEFs) and serves as a direct link between Eph receptors and the Rho-family of GTPases.
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More recently, new regulatory factors that directly interact with K-Ras were identified and shown to play a crucial role in the full range of K-Ras oncogenic phenotypes. It is well established that canonical Ras signaling is coupled to transcriptional regulation through the activation of the MAPK cascade, which involves the sequential phosphorylation and activation of the serine/threonine kinases RAF, MEK1/2, and ERK1/2. A significant consequence of Ras-mediated signal transduction is the altered expression of a large number of genes. Thus, understanding the mechanisms behind Ras-induced oncogenesis is an important goal in cancer therapy. Mutational activation of K-Ras in these tissues is sufficient to initiate neoplasia in mice. Oncogenic Ras mutations are frequently observed in solid tumor cells and are present in pancreatic cancer, colorectal cancer (CRC), and lung cancer (LC). These data indicate that Ephexin1 plays a critical role in the Ras-mediated CRC and LC and pSer16/18 Ephexin1 might be an effective therapeutic target for CRC and LC. Furthermore, pSer16/18 Ephexin1 is associated with both an increased tumor grade and metastatic cases of CRC and LC, and those that highly express pSer16/18 exhibit poor overall survival rates. Mechanically, Akt phosphorylates Ephexin1 at Ser16 and Ser18 (pSer16/18) and pSer16/18 Ephexin1 then interacts with oncogenic K-Ras to promote downstream MAPK signaling, facilitating tumorigenesis.
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Ephexin1 contributes to the positive regulation of Ras-mediated downstream target genes and promotes Ras-induced skin tumorigenesis. Knockdown of Ephexin1 markedly inhibited the cell growth of CRC and LC cells with oncogenic Ras mutations.
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Here, we show that Ephexin1 is highly expressed in colorectal cancer (CRC) and lung cancer (LC) patient tissues. Ephexin1 was reported to be highly upregulated by oncogenic Ras, but the functional consequences of this remain poorly understood.