Integrated proteomics and phosphoproteomics study reveals the potential tumour suppressive function of PCK2 in hepatocellular carcinoma

binding sites and kinase activity site, which indicate that the phosphorylation of Ser304 may regulate PCK2 activity. HepG2 cell proliferation, invasion and migration were significantly increased when treated with 3-mercaptopicolinic acid, an inhibitor of PCK2, which demonstrated the tumour suppressive activity of PCK2 in HCC. In addition, the low mRNA expression of PCK2 was correlated with poor overall survival of live cancer patients. Overall, our proteomic and phosphoproteomic study revealed the tumour suppressive function of PCK2 in HCC and indicated that activation of its expression or activity may be a potential therapeutic strategy for HCC treatment.