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FEBS Lett. 2009 Jan 5;583(1):25-8. doi: 10.1016/j.febslet.2008.11.022. Epub 2008 Dec 4.

Myosin light chains are not a physiological substrate of AMPK in the control of cell structure changes.

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Université Catholique de Louvain, de Duve Institute, Brussels, Belgium.


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.

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