AMPK is a crucial sensor of the cellular energetic state and is also activated during glucose starvation. A new study reports that AMP-activated protein kinase (AMPK) is activated by interaction with long-chain fatty acyl–CoA esters, which appear to be the long-sought endogenous AMPK ligands that bind the allosteric drug and metabolite (ADaM) site.
References
Lin, S. C. & Hardie, D. G. Cell Metab. 27, 299–313 (2018).
Hardie, D. G., Schaffer, B. E. & Brunet, A. Trends Cell Biol. 26, 190–201 (2016).
Pinkosky, S. L. et al. Nat. Metab. https://doi.org/10.1038/s42255-020-0245-2 (2020).
Winder, W. W. & Hardie, D. G. Am. J. Physiol. 277, E1–E10 (1999).
Cool, B. et al. Cell Metab. 3, 403–416 (2006).
Myers, R. W. et al. Science 357, 507–511 (2017).
Cokorinos, E. C. et al. Cell Metab. 25, 1147–1159.e1110 (2017).
Hawley, S. A. et al. Science 336, 918–922 (2012).
Langendorf, C. G. & Kemp, B. E. Cell Res. 25, 5–6 (2015).
Carling, D., Zammit, V. A. & Hardie, D. G. FEBS Lett. 223, 217–222 (1987).
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Hardie, D.G. AMPK as a direct sensor of long-chain fatty acyl–CoA esters. Nat Metab 2, 799–800 (2020). https://doi.org/10.1038/s42255-020-0249-y
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DOI: https://doi.org/10.1038/s42255-020-0249-y
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