One of the primary functions of AMP-activated protein kinase (AMPK) is to regulate the metabolic pathways in response to reduced cellular energy charge. Most of the known targets of the kinase are cytoplasmic enzymes involved in both catabolic and anabolic metabolism. In addition, activation of AMPK in many cells results in changes in the pattern of gene expression. Although some of these effects are undoubtedly secondary responses to modified cellular metabolism, it is possible that in addition to its well-characterized function in the cytoplasm, AMPK also directly phosphorylates and regulates proteins involved in gene transcription. There are now several examples of transcription factors, cofactors and components of the transcriptional core machinery that are directly phosphorylated and regulated by AMPK. Here I review these examples and discuss the significance of AMPK activity in the nucleus.
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February 2003
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Conference Article|
February 01 2003
AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins
T. Leff
T. Leff
1
Center for Integrative Metabolic and Endocrine Research and the Department of Pathology, Wayne State University School of Medicine, 540 E. Canfield, Detroit, MI 48201, U.S.A.
1e-mail tleff@med.wayne.edu
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Publisher: Portland Press Ltd
Online ISSN: 1470-8752
Print ISSN: 0300-5127
Copyright 2003 Biochemical Society
2003
Biochem Soc Trans (2003) 31 (1): 224–227.
Citation
T. Leff; AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins. Biochem Soc Trans 1 February 2003; 31 (1): 224–227. doi: https://doi.org/10.1042/bst0310224
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