11. Dezember 2020
Ksrp Key Agreement
With its involvement in the Wnt signal transduction pathway and tumorgenese, β-catenin is a widely studied protein. However, the vast majority of studies have focused on controlling protein degradation β-catenin after signal-induced phosphorylation [17-19]. Silanes Lopez et al.  identified β-catenin-mRNA as a target of AER-BP HuR in colon cancer cells, which led to the hypothesis that the β catenin is encoded by an unstable m RNA. Our results show that mrna RNA β-Catenin is unstable in unsponsored cells and refers to an unforeseen mechanism to regulate β-catenin expression in its mRNA turnover through the activation of ACT PI3K. Knock-down experiments show that KSRP controls t1/2 and stationary β-catenin-mRNA content, which increases β-catenine protein levels and improves the triage procedure of catenin-dependent journalists β. In particular, knock-down KFP had no effect on the rate of protein degradation β-catenine. While this manuscript was in preparation, a report by Thiele et al.  described the existence of another tear in the human UTR 3″ β-catenin-mRNA that could influence its stability. However, we exclude that mouse-β-mRNA catenin type 3″UTR isoforms are available in cells of 3-1 and C2C12 (Figure S4 and unpublished data).
Surprisingly, Thiele et al.  reported that AREs are stabilizing elements in human 3″UTR β-mrna catenin. Our results suggest that transcription β-catenin is unstable in four different cell lines (T3-1, HIRc-B, C2C12, as shown in this report, and 293T, unpublished data) and that mouse-β staln 3″ UTR gives instability to a reporter. These data contradict the general view that AREs are destabilizing elements in unsusclected cells (verified in [1-3]). In order to assess the contribution of the PI3K/AKT signaling pathway to myomir induction during the differentiation of C2C12 myoblasts, we continuously exposed myoblast-induced myoblasts to LY294002 (LY) of myoblasts induced by the differentiation medium. LY was able to alter DM-induced expression of myogen differentiation markers (Figure S1a, and Serra et al.31) and strongly inhibit the expression of miR-1a, miR-133b and miR-206 (members of the myomiR10, 11) DM-induced family (Figure 1a). It is important that comparative analysis of primary and mature NMNs showed that LY particularly impairs myomiR maturation (Figures 1a and b). ACTION inhibitors are the main effects of the PI3K.32 low team since the relative contribution of the two ACT isoforms (Act1 and Act2) expressed in IN C2C12 is still in discussion course We either reduced isoform prior to exposure to DM (additional figure S1b) and obtained an inhibition of the expression of myogeneist differentiation markers (additional figure S1c and Serra et al.31). Silencing experiments have shown that act1 and act2 are necessary for DM-induced maturation of miR-1a, miR-133b and miR-206 (compare expression of mature and primary miRNA in figures 1c and d). Consistent with an AKT role in myomiR maturation, the expression of a constituent myristolic form of act2 (myr-AKT230) strengthened the expression of MyomiRs in DM-grown C2C12 cells without affecting the expression of corresponding pri-miRNAs (figures 1st and f).