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Science 332 (6036): 1387-1388

Copyright © 2011 by the American Association for the Advancement of Science

ADaPting to Energetic Stress

Michelle L. Bland, and Morris J. Birnbaum

The movement of muscles, the repolarization of neuronal membranes, and the synthesis of cellular building blocks such as proteins and lipids are powered by energy derived from the hydrolysis of adenosine 5'-triphosphate (ATP). Each day, these processes lead to the turnover of 40 kg of ATP in the average adult human being. ATP is indispensable for life, and sophisticated mechanisms for assessing cellular energy status have evolved and been conserved across all eukaryotes. Adenosine 5'-monophosphate (AMP)–activated protein kinase (AMPK; SNF1 in yeast) is a key enzyme that regulates cell energetics. As the name suggests, AMP has long been believed to be the specific metabolite regulating AMPK activity. Oakhill et al. on page 1433 in this issue (1) and a recent report by Xiao et al. (2) propose an alternative model in which the concentration of intracellular adenosine 5'-diphosphate (ADP) signals the energy status of the cell to AMPK, prompting reevaluation of the pathways that govern adaptation to energetic stress.

Institute for Diabetes, Obesity and Metabolism, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.

E-mail: birnbaum{at}

Myc-induced AMPK-phospho p53 pathway activates Bak to sensitize mitochondrial apoptosis.
A. I. Nieminen, V. M. Eskelinen, H. M. Haikala, T. A. Tervonen, Y. Yan, J. I. Partanen, and J. Klefstrom (2013)
PNAS 110, E1839-E1848
   Abstract »    Full Text »    PDF »
AMPK protects proximal tubular cells from stress-induced apoptosis by an ATP-independent mechanism: potential role of Akt activation.
W. Lieberthal, L. Zhang, V. A. Patel, and J. S. Levine (2011)
Am J Physiol Renal Physiol 301, F1177-F1192
   Abstract »    Full Text »    PDF »

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