Abstract
Pyruvate kinase M2 (PKM2), the final rate-limiting enzyme in glycolysis, exists in a dynamic population of monomer, dimer and tetramer that determine its pyruvate kinase activity. However, the roles of oncoproteins, such as the cancerous inhibitor of protein phosphatase PP2A (CIP2A) that is overexpressed in most human malignancies, in PKM2 dimer-tetramer switching remain largely unknown.
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