Figure 5.MKRN2 inhibits PKM2 by promoting its degradation. Using Co-immunoprecipitation experiments with gastric cells, we showed that MKRN2 was able to coimmunoprecipitate endogenous PKM2 (A). MKRN2 decreased ERK phosphorylation by promoting ubiquitination-mediated degradation of PKM2 (B). In plv-MKRN2 transfected MGC-803 cells, level of PKM2 and ERK phosphorylation significantly decreased (D, F). Knockdown of MKRN2 increased the level of PKM2 and ERK phosphorylation (C, E).
