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Sci. Signal., 19 February 2013
Vol. 6, Issue 263, p. pe7
[DOI: 10.1126/scisignal.2003925]

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Allosteric Regulation of PKM2 Allows Cellular Adaptation to Different Physiological States

Dan Y. Gui1*, Caroline A. Lewis1*, and Matthew G. Vander Heiden1,2{dagger}

1 Koch Institute for Integrative Cancer Research at Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
2 Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.

* These authors contributed equally to this work.

Abstract: Pyruvate kinase isoform M2 (PKM2) activity is subject to complex allosteric regulation. Recently, serine and SAICAR (succinylaminoimidazolecarboxamide ribose-5'-phosphate) were identified as previously unrecognized activators of PKM2. These findings add additional complexity to how PKM2 is regulated in cells and support the notion that modulating PKM2 activity enables cells to adapt their metabolic state to specific physiological contexts.

{dagger} Corresponding author. E-mail: mvh{at}mit.edu

Citation: D. Y. Gui, C. A. Lewis, M. G. Vander Heiden, Allosteric Regulation of PKM2 Allows Cellular Adaptation to Different Physiological States. Sci. Signal. 6, pe7 (2013).

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