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Wiley, FEBS Letters, 1(583), p. 25-28, 2008

DOI: 10.1016/j.febslet.2008.11.022

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

Journal article published in 2008 by Laurent Bultot ORCID, Sandrine Horman, Dietbert Neumann ORCID, Michael P. Walsh, Louis Hue, Mark H. Rider
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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: