Lack of Evidence for PKM2 Protein Kinase Activity
Copyright policy )Lack of Evidence for PKM2 Protein Kinase Activity
The role of pyruvate kinase M2 (PKM2) in cell proliferation is controversial. A unique function of PKM2 proposed to be important for the proliferation of some cancer cells involves the direct activity of this enzyme as a protein kinase; however, a detailed biochemical characterization of this activity is lacking. Using [(32)P]-phosphoenolpyruvate (PEP) we examine the direct substrates of PKM2 using recombinant enzyme and in vitro systems where PKM2 is genetically deleted. Labeling of some protein species from [(32)P]-PEP can be observed; however, most were dependent on the presence of ADP, and none were dependent on the presence of PKM2. In addition, we also failed to observe PKM2-dependent transfer of phosphate from ATP directly to protein. These findings argue against a role for PKM2 as a protein kinase.
- Harvard University United States
- Massachusetts Institute of Technology United States
- Dana-Farber Cancer Institute United States
Thyroid Hormones, Pyruvate Kinase, Substrate Specificity, Phosphoenolpyruvate, Mice, Adenosine Triphosphate, Cell Line, Tumor, Animals, Humans, Phosphorylation, Molecular Biology, Cells, Cultured, Cell Proliferation, Membrane Proteins, Cell Biology, Recombinant Proteins, Carrier Proteins, Glycolysis, Protein Kinases, Gene Deletion, Thyroid Hormone-Binding Proteins
Thyroid Hormones, Pyruvate Kinase, Substrate Specificity, Phosphoenolpyruvate, Mice, Adenosine Triphosphate, Cell Line, Tumor, Animals, Humans, Phosphorylation, Molecular Biology, Cells, Cultured, Cell Proliferation, Membrane Proteins, Cell Biology, Recombinant Proteins, Carrier Proteins, Glycolysis, Protein Kinases, Gene Deletion, Thyroid Hormone-Binding Proteins
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