| First Author | Hosios AM | Year | 2015 |
| Journal | Mol Cell | Volume | 59 |
| Issue | 5 | Pages | 850-7 |
| PubMed ID | 26300261 | Mgi Jnum | J:228093 |
| Mgi Id | MGI:5705201 | Doi | 10.1016/j.molcel.2015.07.013 |
| Citation | Hosios AM, et al. (2015) Lack of Evidence for PKM2 Protein Kinase Activity. Mol Cell 59(5):850-7 |
| abstractText | 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. |
