title: Allosteric regulation of PKM2 allows cellular adaptation to different physiological states.
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.
authors: Koch Institute for Integrative Cancer Research at Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
authors: Dan Y
authors: DY
authors: Gui
authors: Caroline A
authors: CA
authors: Lewis
authors: Matthew G
authors: MG
authors: Vander Heiden
mesh_terms: D000222:Adaptation, Physiological; D000494:Allosteric Regulation; D002352:Carrier Proteins / Q000502:physiology*; D006801:Humans; D008565:Membrane Proteins / Q000502:physiology*; D013963:Thyroid Hormones / Q000502:physiology*; D000097810:Thyroid Hormone-Binding Proteins
chemical_list: D002352:Carrier Proteins; D008565:Membrane Proteins; D013963:Thyroid Hormones; D000097810:Thyroid Hormone-Binding Proteins