Signaling Kinase AMPK Activates Stress-Promoted Transcription via Histone H2B Phosphorylation
| Autor: | Benjamin J. Fuerth, Russell G. Jones, David Bungard, Craig B. Thompson, Ping-Yao Zeng, Benoit Viollet, David Carling, Nancy L. Maas, Shelley L. Berger, Brandon Faubert |
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| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: |
Chromatin Immunoprecipitation
Transcription Genetic Cell Survival Amino Acid Motifs RNA polymerase II AMP-Activated Protein Kinases Protein Serine-Threonine Kinases environment and public health Article Cell Line Histones Mice Stress Physiological Cell Line Tumor Histone H2B Serine Humans Animals Phosphorylation Protein kinase A Promoter Regions Genetic Cells Cultured Multidisciplinary biology AMPK Promoter Adaptation Physiological Chromatin Enzyme Activation Biochemistry Amino Acid Substitution Gene Expression Regulation biology.protein Tumor Suppressor Protein p53 Chromatin immunoprecipitation Signal Transduction Transcription Factors |
| Popis: | Regulation of Energy Homeostasis 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 ; published online 17 August; see the Perspective by Hardie ) 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. |
| Databáze: | OpenAIRE |
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