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Papers In Press, published online ahead of print June 24, 2005
J. Biol. Chem, 10.1074/jbc.M503824200
Submitted on April 8, 2005
Revised on June 23, 2005
Accepted on June 24, 2005

The Ca++/calmoldulin-dependent protein kinase kinases are AMP-activated protein kinase kinases

Rebecca L. Hurley, Kristin A. Anderson, Jeanne M. Franzone, Bruce E. Kemp, Anthony R. Means, and Lee A. Witters

Department of Medicine and Biochemistry, Dartmouth Medical School, Hanover, NH 03755-3833

Corresponding Author: lee.a.witters{at}dartmouth.edu

The AMP-activated protein kinase (AMPK) is an important regulator of cellular metabolism in response to metabolic stress and to other regulatory signals. AMPK activity is absolutely dependent upon phosphorylation of AMPKaThr172 in its activation loop by one or more AMPK kinases (AMPKK). The tumor suppressor kinase, LKB1, is a major AMPKK present in a variety of tissues and cells, but several lines of evidence point to the existence of other AMPKKs. We have employed three cell lines deficient in LKB1 to study AMPK regulation and phosphorylation, HeLa, A549 and murine embryo fibroblasts (MEFs) derived from LKB-/- mice. In HeLa and A549 cells, mannitol, 2-deoxyglucose and ionomycin, but not AICAR, treatment activates AMPK by aThr172 phosphorylation. These responses, as well as the downstream effects of AMPK on the phosphorylation of acetyl-CoA carboxylase (ACC), are largely inhibited by the Ca++/calmodulin-dependent protein kinase kinase (CaMKK) inhibitor, STO-609. AMPKK activity in HeLa cell lysates measured in vitro is totally inhibited by STO-609 with an IC50 comparable to that of the known CaMKK isoforms, CaMKKa and CaMKKß. Furthermore, 2-deoxyglucose and ionomycin-stimulated AMPK activity, aThr172 phosphorylation and ACC phosphorylation are substantially reduced in HeLa cells transfected with siRNAs specific for CaMKKa and CaMKKß. Lastly, the activation of AMPK in response to ionomycin and 2-deoxyglucose is not impaired in LKB1-/- MEFs. These data indicate that the CaMKKs function in intact cells as AMPKKs, predicting wider roles for these kinases in regulating AMPK activity in vivo.


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