AMPK as a direct sensor of long-chain fatty acyl–CoA esters

D. Grahame Hardie (Lead / Corresponding author)

Research output: Contribution to journalComment/debatepeer-review

10 Citations (Scopus)
170 Downloads (Pure)


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.
Original languageEnglish
Pages (from-to)799-800
Number of pages2
JournalNature Metabolism
Issue number9
Publication statusPublished - 27 Jul 2020


  • Kinases
  • Metabolism
  • Nutrient signalling

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Physiology (medical)
  • Internal Medicine
  • Cell Biology


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