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Sirtuin type 1 (SIRT1) is a potent NAD+ dependent deacetylase that deacetylates histone and nonhistone proteins to regulate gene expression and protein activity. Emerging evidences have indicated that SIRT1 plays a significant role in diverse cellular processes including cell growth, differentiation, development, and physiological function in muscle cells; however the signaling mechanisms involved remain to be established. In order to investigate its potential role in muscle biological processes, we administrated C2C12 cells which were isolated from skeletal muscle tissue of dystrophic mice with SIRT1 activator resveratrol (REV), inhibitor nicotinamide (NAM) and Wnt inhibitor FH535. By CCK-8, BrdU assay, real-time PCR and Western blot, we investigated whether the SIRT1 has a function in C2C12 cells by promoting beta-catenin accumulation. Our results demonstrate that SIRT1 increases cell proliferation of C2C12 myoblast in a SIRT1-dependent manner. And SIRT1 significantly up-regulates the expression of cyclin D1, C-myc and Dvl2 in vitro as well as stimulates the accumulation of the Wnt/beta-catenin. In conclusion, this study indicates that SIRT1 promotes the proliferation of C2C12 myoblast cells, at least partly via Wnt signaling pathway.

Receptor-interacting protein kinase 4 (RIPK4) is required for epidermal differentiation and is mutated in Bartsocas-Papas syndrome. RIPK4 binds to protein kinase C, but its signaling mechanisms are largely unknown. Ectopic RIPK4, but not catalytically inactive or Bartsocas-Papas RIPK4 mutants, induced accumulation of cytosolic beta-catenin and a transcriptional program similar to that caused by Wnt3a. In Xenopus embryos, Ripk4 synergized with coexpressed Xwnt8, whereas Ripk4 morpholinos or catalytic inactive Ripk4 antagonized Wnt signaling. RIPK4 interacted constitutively with the adaptor protein DVL2 and, after Wnt3a stimulation, with the co-receptor LRP6. Phosphorylation of DVL2 by RIPK4 favored canonical Wnt signaling. Wnt-dependent growth of xenografted human tumor cells was suppressed by RIPK4 knockdown, suggesting that RIPK4 overexpression may contribute to the growth of certain tumor types.