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Myosin light chains are not a physiological substrate of AMPK in the control of cell structure changes |
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| Authors: | Laurent Bultot Sandrine Horman Dietbert Neumann Louis Hue |
| Institution: | a Université Catholique de Louvain, Hormone and Metabolic Research Unit, de Duve Institute, Avenue Hippocrate, 75, B-1200 Brussels, Belgium b Université Catholique de Louvain, CARD Unit, Division of Cardiology, Avenue Hippocrate, 55, B-1200 Brussels, Belgium c Institute of Cell Biology, Swiss Federal Institute of Technology (ETH), CH-8093 Zurich, Switzerland d Smooth Muscle Research Group and Department of Biochemistry and Molecular Biology, University of Calgary, Faculty of Medicine, Calgary, Alberta, Canada T2N 4N1. |
| Abstract: | The kinetics of myosin regulatory light chain (MLC) phosphorylation by recombinant AMP-activated protein kinase (AMPK) were compared with commercial AMPK from rat liver and smooth muscle myosin light chain kinase (smMLCK). With identical amounts of activity units, initial rates of phosphorylation of MLC were at least 100-fold less with recombinant AMPK compared to smMLCK, whereas with rat liver AMPK significant phosphorylation was seen. In Madin-Darby Canine Kidney cells, AMPK activation led to an increase in MLC phosphorylation, which was decreased by a Rho kinase inhibitor without affecting AMPK activation. Therefore, MLC phosphorylation during energy deprivation does not result from direct phosphorylation by AMPK.Structured summary
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| Keywords: | ACC acetyl-CoA carboxylase AMPK AMP-activated protein kinase Ca2+/CaM calcium/calmodulin MDCK Madin-Darby Canine Kidney MLC myosin regulatory light chain smMLCK smooth muscle myosin light chain kinase |
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