Serine is a natural ligand and allosteric activator of pyruvate kinase M2
Open accessAbstract
Cancer cells exhibit several unique metabolic phenotypes that are critical for cell growth and proliferation. Specifically, they overexpress the M2 isoform of the tightly regulated enzyme pyruvate kinase (PKM2), which controls glycolytic flux, and are highly dependent on de novo biosynthesis of serine and glycine. Here we describe a new rheostat-like mechanistic relationship between PKM2 activity and serine biosynthesis. We show that serine can bind to and activate human PKM2, and that PKM2 activity in cells is reduced in response to serine deprivation. This reduction in PKM2 activity shifts cells to a fuel-efficient mode in which more pyruvate is diverted to the mitochondria and more glucose-derived carbon is channelled into serine biosynthesis to support cell proliferation.
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The pyruvate kinase activity of PKM2 tetramers can be regulated by the concentration of FBP, serine, and by post-translational modifications including tyrosine phosphorylation.
“The pyruvate kinase activity of the tetramers can be regulated by the concentration of the naturally occurring upstream glycolytic intermediate FBP (Ashizawa et al., 1991; Jurica et al., 1998), serine (Chaneton et al., 2012), as well as by a multitude of post-translational modifications (Wu and Le, 2013) including tyrosine phosphorylation.”
From Pyruvate kinase M2 regulates Hif-1α activity and IL-1β induction and is a critical determinant of the Warburg effect in LPS-activated macrophages (2015) · cites this paper as Chaneton et al., 2012
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- Authors
- Chaneton, B., Hillmann, P., Zheng, L., Martin, A. C. L., Maddocks, O. D. K., Chokkathukalam, A., Coyle, J. E., Jankevics, A., Holding, F. P., Vousden, K. H., Frezza, C., O’Reilly, M., & Gottlieb, E.
- Affiliations
- Cancer Research UK (GB)
- Astex Pharmaceuticals (US)
- University of Glasgow (GB)
- University of Groningen (NL)
- Corresponding author
- O’Reilly, Marc
- Gottlieb, Eyal
- ORCID
- Venue
- Nature
- Published
- 2012-10-14
- Volume
- 491
- Issue
- 7424
- Pages
- 458-462
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3894725
- OpenAlex
- W2039558597
- Cited by
- 661
- References
- 38
- Citations by year
- 2026: 36 · 2025: 44 · 2024: 46 · 2023: 62 · 2022: 36 · 2021: 63 · 2020: 47 · 2019: 45 · 2018: 52 · 2017: 49 · 2016: 52 · 2015: 41 · 2014: 43 · 2013: 40 · 2012: 5
- FWCI
- 13.70
- Type
- journal article
- Language
- en
- Update notices
- correction (2013-04-17)
- Open access
- green
- research.rug.nl
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, other-oa)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion)
- Funders
- Cancer Research UK (A12477)
- Beatson Institute for Cancer Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- PKM2, serine, allosteric activation, serine biosynthesis, glycolysis, cancer metabolism, glucose-derived carbon, mitochondrial metabolism, cell proliferation
- MeSH terms
- Enzyme Activation, Glucose, Glycine, Humans, Ligands, Pyruvate Kinase, Recombinant Proteins, Serine, Pyruvic Acid, Enzyme Activators, Cell Line, Tumor, Cell Proliferation
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