Fig. 2

The activity of PKM2 is dependent upon its oligomerization states. The PKM2 tetramer exhibits high levels of pyruvate kinase activity and can accelerate the transformation of PEP to pyruvate, thereby increasing the glycolytic flux and ATP production rates. Whereas PKM2 in dimeric form exhibits lower levels of pyruvate kinase activity, and can be phosphorylated at Tyr105, Tyr 328, Thr328 or Pro403/408 sites and then translocate into nucleus to act as a co-activator for some transcription factors, such as HIF-1α, β-catenin/c-Myc, NF-κB and STAT3, leading to tumor progression