Signaling Kinase AMPK Activates Stress-Promoted Transcription via Histone H2B Phosphorylation
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- David Bungard
- Department of Cellular and Developmental Biology, University of Pennsylvania Medical School, Philadelphia, PA 19104, USA.
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- Benjamin J. Fuerth
- Rosalind and Morris Goodman Cancer Research Centre, McGill University, Montreal, Quebec H3G 1Y6, Canada.
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- Ping-Yao Zeng
- Department of Cellular and Developmental Biology, University of Pennsylvania Medical School, Philadelphia, PA 19104, USA.
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- Brandon Faubert
- Rosalind and Morris Goodman Cancer Research Centre, McGill University, Montreal, Quebec H3G 1Y6, Canada.
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- Nancy L. Maas
- Department of Cellular and Developmental Biology, University of Pennsylvania Medical School, Philadelphia, PA 19104, USA.
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- Benoit Viollet
- Institut Cochin, Université Paris Descartes, CNRS (UMR 8104), 75014 Paris, France.
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- David Carling
- Cellular Stress Group, MRC Clinical Sciences Centre, Imperial College, Hammersmith Hospital, London W12 0NN, UK.
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- Craig B. Thompson
- Abramson Cancer Center and Abramson Family Cancer Research Institute, University of Pennsylvania, Philadelphia, PA 19104, USA.
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- Russell G. Jones
- Rosalind and Morris Goodman Cancer Research Centre, McGill University, Montreal, Quebec H3G 1Y6, Canada.
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- Shelley L. Berger
- Department of Cellular and Developmental Biology, University of Pennsylvania Medical School, Philadelphia, PA 19104, USA.
説明
<jats:title>Regulation of Energy Homeostasis</jats:title> <jats:p> 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. <jats:bold> Bungard <jats:italic>et al.</jats:italic> </jats:bold> (p. <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" page="1201" related-article-type="in-this-issue" vol="329" xlink:href="10.1126/science.1191241">1201</jats:related-article> ; published online 17 August; see the Perspective by <jats:bold> <jats:related-article xmlns:xlink="http://www.w3.org/1999/xlink" ext-link-type="doi" issue="5996" page="1158" related-article-type="in-this-issue" vol="329" xlink:href="10.1126/science.1195447">Hardie</jats:related-article> </jats:bold> ) 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. </jats:p>
収録刊行物
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- Science
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Science 329 (5996), 1201-1205, 2010-09-03
American Association for the Advancement of Science (AAAS)
