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

Onglets principaux

Bultot, Laurent [UCL] Horman, Sandrine [UCL] Neumann, Dietbert Walsh, Michael P Hue, Louis [UCL] Rider, Mark H. [UCL]

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:

Type de document Article de périodique (Journal article) – Journal Article, Research Support, Non-U.S. Gov't
Type d'accès Accès restreint
Année de publication 2008
Information sur le périodique "FEBS letters" - Vol. 583, no. 1, p. 25-8 (2009)
Peer reviewed oui
issn 0014-5793
Statut de la publication Publié
Affiliations UCL - MD/BICL - Département de biochimie et de biologie cellulaire
MESH Subject rho-Associated Kinases - antagonists & inhibitors - metabolism ; Substrate Specificity ; Rats ; Protein Kinases - genetics - metabolism ; Protein Kinase Inhibitors - pharmacology ; Phosphorylation ; Myosin Light Chains - metabolism ; Humans ; Dogs ; Cell Line ; Animals ; 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine - analogs & derivatives - pharmacology
Liens
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Référence bibliographique Bultot, Laurent ; Horman, Sandrine ; Neumann, Dietbert ; Walsh, Michael P ; Hue, Louis ; et. al. Myosin light chains are not a physiological substrate of AMPK in the control of cell structure changes.. In: FEBS letters, Vol. 583, no. 1, p. 25-8 (2009)
Permalien http://hdl.handle.net/2078.1/20713