PerspectiveCellular Metabolism

Allosteric Regulation of PKM2 Allows Cellular Adaptation to Different Physiological States

Science Signaling  19 Feb 2013:
Vol. 6, Issue 263, pp. pe7
DOI: 10.1126/scisignal.2003925

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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.

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