AMP-activated Protein Kinase Phosphorylates and Desensitizes Smooth Muscle Myosin Light Chain Kinase

Smooth muscle contraction is initiated by a rise in intracellular calcium, leading to activation of smooth muscle myosin light chain kinase (MLCK) via calcium/calmodulin (CaM). Activated MLCK then phosphorylates the regulatory myosin light chains, triggering cross-bridge cycling and contraction. Her...

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Veröffentlicht in:The Journal of biological chemistry 2008-07, Vol.283 (27), p.18505-18512
Hauptverfasser: Horman, Sandrine, Morel, Nicole, Vertommen, Didier, Hussain, Nusrat, Neumann, Dietbert, Beauloye, Christophe, Najjar, Nicole El, Forcet, Christelle, Viollet, Benoit, Walsh, Michael P., Hue, Louis, Rider, Mark H.
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container_end_page 18512
container_issue 27
container_start_page 18505
container_title The Journal of biological chemistry
container_volume 283
creator Horman, Sandrine
Morel, Nicole
Vertommen, Didier
Hussain, Nusrat
Neumann, Dietbert
Beauloye, Christophe
Najjar, Nicole El
Forcet, Christelle
Viollet, Benoit
Walsh, Michael P.
Hue, Louis
Rider, Mark H.
description Smooth muscle contraction is initiated by a rise in intracellular calcium, leading to activation of smooth muscle myosin light chain kinase (MLCK) via calcium/calmodulin (CaM). Activated MLCK then phosphorylates the regulatory myosin light chains, triggering cross-bridge cycling and contraction. Here, we show that MLCK is a substrate of AMP-activated protein kinase (AMPK). The phosphorylation site in chicken MLCK was identified by mass spectrometry to be located in the CaM-binding domain at Ser815. Phosphorylation by AMPK desensitized MLCK by increasing the concentration of CaM required for half-maximal activation. In primary cultures of rat aortic smooth muscle cells, vasoconstrictors activated AMPK in a calcium-dependent manner via CaM-dependent protein kinase kinase-β, a known upstream kinase of AMPK. Indeed, vasoconstrictor-induced AMPK activation was abrogated by the STO-609 CaM-dependent protein kinase kinase-β inhibitor. Myosin light chain phosphorylation was increased under these conditions, suggesting that contraction would be potentiated by ablation of AMPK. Indeed, in aortic rings from mice in which α1, the major catalytic subunit isoform in arterial smooth muscle, had been deleted, KCl- or phenylephrine-induced contraction was increased. The findings suggest that AMPK attenuates contraction by phosphorylating and inactivating MLCK. This might contribute to reduced ATP turnover in the tonic phase of smooth muscle contraction.
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Indeed, in aortic rings from mice in which α1, the major catalytic subunit isoform in arterial smooth muscle, had been deleted, KCl- or phenylephrine-induced contraction was increased. The findings suggest that AMPK attenuates contraction by phosphorylating and inactivating MLCK. 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subjects Adenosine Triphosphate - chemistry
Adenosine Triphosphate - genetics
Adenosine Triphosphate - metabolism
AMP-Activated Protein Kinases
Animals
Aorta - chemistry
Aorta - enzymology
Benzimidazoles - pharmacology
Calcium - metabolism
Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors
Calcium-Calmodulin-Dependent Protein Kinases - chemistry
Calcium-Calmodulin-Dependent Protein Kinases - genetics
Calcium-Calmodulin-Dependent Protein Kinases - metabolism
Calmodulin - genetics
Calmodulin - metabolism
Cattle
Cells, Cultured
Chickens
Male
Mice
Mice, Knockout
Multienzyme Complexes - chemistry
Multienzyme Complexes - genetics
Multienzyme Complexes - metabolism
Muscle Contraction - drug effects
Muscle Contraction - physiology
Muscle Tonus - drug effects
Muscle Tonus - physiology
Muscle, Smooth - chemistry
Muscle, Smooth - enzymology
Myocytes, Smooth Muscle - chemistry
Myocytes, Smooth Muscle - enzymology
Myosin-Light-Chain Kinase - chemistry
Myosin-Light-Chain Kinase - genetics
Myosin-Light-Chain Kinase - metabolism
Naphthalimides - pharmacology
Phenylephrine - pharmacology
Phosphorylation - drug effects
Potassium Chloride - pharmacology
Protein-Serine-Threonine Kinases - chemistry
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Rats
Rats, Wistar
Vasoconstriction - drug effects
Vasoconstriction - physiology
Vasoconstrictor Agents - pharmacology
title AMP-activated Protein Kinase Phosphorylates and Desensitizes Smooth Muscle Myosin Light Chain Kinase
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