Abstract
The mammalian AMP-activated protein kinase (AMPK) is a serine/threonine kinase complex that regulates cellular energy homeostasis. However, the mechanisms by which AMPK mediates transcriptional responses to metabolic perturbations has been unclear. Bungard et al. (p. [1201][1]; published online 17 August; see the Perspective by [Hardie][2] ) have found that AMPK activated transcription directly on chromatin, combined with phosphorylation of histone H2B at Serine-36. Both signals colocalized at genes regulated in the pathway, and both the enzyme and phosphorylation were required for the direct transcription of stress-responsive genes. [1]: /lookup/doi/10.1126/science.1191241 [2]: /lookup/doi/10.1126/science.1195447
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