Lack of Evidence for PKM2 Protein Kinase Activity
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Lack of evidence.pdf
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1.02 MB
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Checksum (MD5)
5deb647e0882337cb3860a2ab534e2a4
Author(s)
Hosios, Aaron Marc
Fiske, Brian Prescott
Gui, Dan Yi
Vander Heiden, Matthew G.
Date Issued
August 2015
Journal
Molecular Cell
Publisher
Elsevier
Citation
Hosios, Aaron M. et al. “Lack of Evidence for PKM2 Protein Kinase Activity.” Molecular Cell 59.5 (2015): 850–857.
Version
Author's final manuscript
Abstract
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 [32P]-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 [32P]-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.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Koch Institute for Integrative Cancer Research at MIT
Terms of Use
Creative Commons Attribution-NonCommercial-NoDerivs License
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DOI of Published Version
https://doi.org/10.1016/j.molcel.2015.07.013
