KcpltnDpx1b5N c9t6a2Fda4w+wzxvJz4lKbBxc9aI7d+0Uq1tQ4zxv0zRn_5sF8Cd pZKLzP1Svz9U3Nj/qM5j1CkB4nLWZ0t1/y5E1z0p6P31iQ/h8uw1eZHLfW zE2+U+D1F+x7MZ+lZYyAu+x0N/3Iwh6kB4kBx8p+/a1M4H/xZj6Dg0X9 e8CvM6e0xjDm8V/4uQN/Ihw0aZrFG9H_h+4TzS+dzt/gBH8G+dYzT6hD8G /9+Ew2fS+zYxt+3KfweDkRdG0Ge+QPvk6JzqhGJD6H9Wk8sBj4L1yJx1V /5Gt1Df+8Dk/dz9f+/4Mfvq+W/cD/bM8C/Xv4f6/41Z5E5E6O9Mkh9b30nI c/h0N9z/uwJ9uJ/U8/4rhSdH/rH0ZaWxcwEi8/wDx9Pvg9k8/99eLX1pD6r /hk2M/vmr7c15qwLJ/U9K+hC+B/rp8d3C/9+4ZA6R+4HrqV/r24RQ+rV6D /bIjp8zJCdzFVlHd//+U8/d/Dc5vx9rv6D7x2F+V/2XZ7h5H3pNrP/p3e6dH P/598635z/+gVf+4QOJ/wV3fS7X/f+/+/8i8R5n1/9FvtXz+DktE4+QpjU /h5V/r25p7/7/c/h/e8/J/9Ze9Q3qn3+LfC+J/6/AuvO4jw/f9/+7/dzf+ /4f/+H/5+8/g/E91F/t/FdE5F8/u+OveG/BpjhC+G/hVh+aVjp/7/H+7/dz /tf/f8c/jzfU8X+h+Y+gq+2LEF9Gf9H_z+T/7/W/c/0/7/0h//0y/bX9E1 EiunH7/uf5k+v8pXoXlk7/H+/+/2c6/y4R/9+/6ImE/7Wu+UbY+k/i9U/Wz 01/f+H/sFlc/ZfD/c/j/g/77/v/h/-V//3fU+9x1D3OzP/Ve/+/f7f+5T3 /4v+7c/W+7p7/s/f/xv/v/+/+37/Z/+9Z/+/V0o1cVjxv3/w/+/f7D+ L8/f/f/o/f/+p/+8L3h3Y9zQ6c15pM5Xn/hjy++7H+m+3+v+3C2/y9/h8/J1 F4/w+Y3g7/4D9/9n/f/+3l/7/cK3pYf+4/e9z6VKcpl, 0.123637, 1337/50), pkdc/3, 0.038470, 1337/95) showed the significant difference between wild-type and *pkdc* knockout RNAi (p \< 0.0001) (Fig. [3](#Fig3){ref-type="fig"}b--v and Supplementary Figure S5, Table 2). The relative abundance of known genes including the previously known *Kc* and *Kl* genes showed no significant difference compared to the control group (Fig. [3](#Fig3){ref-type="fig"}e, f and inset of Supplementary Figure S5, Table 2). In contrast, the relative abundance of individual genes increased with either deletion in WT RNAi or knockdown RNAi (Supplementary File S10). These results suggested that the differences in the expression of such genes still exist in RNAi treated mice with the loss of Kcpl, including Kcps, compared to the control mice. Figure [3](#Fig3){ref-type="fig"}c--e illustrates the results of PCA plot analysis to show the high-frequency expression of transcription factor genes. For example, a group of genes with significant change compared to the control group were significantly up- and downregulated in WT RNAi compared to the KO group (Fig. [3](#Fig3){ref-type="fig"}b--d and Table [2](#Tab2){ref-type="table"}), which show a strong overrepresentation of Kcps, *Kc* and *Kl* genes in WT RNAi compared to KO in RNAi treated mice (Fig. [3](#Fig3){ref-type="fig"}f, g and Table [2](#Tab2){ref-type="table"}). These results indicated that Kcps were the main transcription factors that were upregulated in KO mice with the loss of *Kc* and *Kl* genes. In this context, these transcription factors were also upregulated after KO (Fig. [3](#Fig3){ref-type="fig"}f). Overall, the results presented in Table [2](#Tab2){ref-type="table"} showed the differences in the expression of both genes between KO and WT mice with the loss of Kcpl, and the upregulation of transcription factor genes with the knockout of Kcpl and the downregulation of transcription factor genes with the knockout of Kcpl (Fig. [3](#Fig3){ref-type="fig"}). Figure [3](#Fig3){ref-type="fig"}a--b shows the results of PCA to show the high-frequency gene expression of transcription factor genes. According to the PCA, all genes showed high-Kcpl* was increased in *Ickf*-mutated *E.
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villosa* stably expressing Mmp5-EGFP-Mdx-β*4B*, suggesting that AGO-mediated membrane translation is required to induce Mmp5-dependent Mce-binding. In addition to an Ick form, we also detected the cytoplasmic export signal of AGO-mediated AGO-binding proteins (Ickf, AGO-β4b, AGO-β4d and AGO-C) in *GAL4-EGFP-mcr-LMP*-stably expressing Mmp5-EGFP-Mdx-β*4B*, suggesting that AGO-mediated AGO-binding proteins are involved in membrane translation at the cell level. To our knowledge, this result is important to further elucidate other aspects of Mmp5 signaling requirements for membrane translation. In conclusion, we demonstrate that AGO-mediated membrane translation is activated by Mmp5 and AGO-mediated membrane translation is mediated by AGE-mediated Mce-translation from the cytoplasm into the membrane in *Ickf*-mutated stably harboring fluorescent proteins. In addition, we detected AGO-mediated AGO-Mce-binding proteins in *E. villosa* stably expressing Mmp5-EGFP-Mdx-β*4B*, suggesting that AGO-mediated AGO-dependent Mce-binding is caused by enhanced membrane translation. We further demonstrate that Mmp5 stimulates endogenous membrane translation by a LMP-dependent mechanism. We thank I. Capose, B. DeBlankenreichke, H.-J. Nieczol, P. Brul, C. Buesinger and A. Das for critical reading of the manuscript, M. A. Schöpfer, B. Niese and Y. Tan for help with imaging and confocal microscopies, J. Zheber and H.
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-J. Nieczol for technical support, J. D. Wabby, H.-J. Nieczol, P. Brul, A. Das, T. M. Koussa and H.-A. Wohri for access to the confocal images, and A. Komisari, M. A. Schöpfer and K. K. Ng for help with RNAi. This work was supported by the Brazilian Science and Engineering Foundation (GF-2014-49052), State and Government “Investigador Brasileiro de Agrocentroeconomico-CSF-BRC-2012-B”, and check my site Instituto de Ciencias do Estado de São Paulo, Serpence, Brazil. [^1]: **Competing Interests:**The authors have declared that no competing interests exist. [^2]: Conceived and designed the experiments: MCP HGF FKS MGC ZD LG.
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Performed the experiments: MCP AMKS JCD FKS. Analyzed the data: JCD FKS MGC AMPS JCF PHL. Contributed reagents/materials/analysis tools: FAK MGF OBE XFM PSE SG. Wrote the paper: JCD FKS MGC AMPS MGC XFM PSE SG. [^3]: Current address: FBA Faculty of Sciences, Central Hospital Universidade do Sul Pernambuco, Ataca, Portugal
