M2 pyruvate kinase provides a mechanism for nutrient sensing and regulation of cell proliferation

We show that the M2 isoform of pyruvate kinase (M2PYK) exists in equilibrium between monomers and tetramers regulated by allosteric binding of naturally occurring small-molecule metabolites. Phenylalanine stabilizes an inactive T-state tetrameric conformer and inhibits M2PYK with an IC ₅₀ value of 0...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2013-04, Vol.110 (15), p.5881-5886
Hauptverfasser:	Morgan, Hugh P., O'Reilly, Francis J., Wear, Martin A., O'Neill, J. Robert, Fothergill-Gilmore, Linda A., Hupp, Ted, Walkinshaw, Malcolm D.
Format:	Artikel
Sprache:	eng
Schlagworte:	Allosteric regulation Allosteric Site Amino Acid Sequence Amino acids Biological Sciences Cancer Catalytic Domain Cell growth Cell Line, Tumor Cell Proliferation Cells Cellular metabolism Crystallography, X-Ray Dimerization Enzymes glucose Hormones Humans Inhibitory Concentration 50 Kinases Ligands lysine Metabolites Molecular Sequence Data Monomers neoplasms phenylalanine Phenylalanine - chemistry Protein Conformation Protein isoforms Protein Structure, Tertiary Protein subunits pyruvate kinase Pyruvate Kinase - metabolism Thyroid hormones Triiodothyronine - chemistry Tumors X-radiation
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