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J. Biol. Chem., Vol. 276, Issue 42, 38341-38344, October 19, 2001

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ACCELERATED PUBLICATION
Regulation of Transcription by AMP-activated Protein Kinase
PHOSPHORYLATION OF p300 BLOCKS ITS INTERACTION WITH NUCLEAR RECEPTORS^*

Wenbo Yang, Yu Holly Hong, Xi-Qiang Shen, Christy Frankowski, Heidi S. Camp, and Todd Leff^§¶

From the  Department of Molecular Sciences, Pfizer Global Research and Development, Ann Arbor, Michigan 48105 and the ^§ Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109

AMP-activated protein kinase (AMP-kinase) modulates many metabolic processes in response to fluctuations in cellular energy status. Although most of its known targets are metabolic enzymes, it has been proposed that AMP-kinase might also regulate gene expression. Here we demonstrate that the transcriptional coactivator p300 is a substrate of AMP-kinase. Phosphorylation of p300 at serine 89 by AMP-kinase dramatically reduced its interaction, in vitro and in vivo, with the nuclear receptors peroxisome proliferator-activated receptor , thyroid receptor, retinoic acid receptor, and retinoid X receptor, but did not affect its interaction with the non-nuclear receptor transcription factors E1a, p53, or GATA4. These findings indicate that the AMP-kinase signaling pathway selectively modulates a subset of p300 activities and represent the first example of a transcriptional component regulated by AMP-kinase. Our results suggest a direct link between cellular energy metabolism and gene expression.

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