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 |
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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. |
doi_str_mv | 10.1074/jbc.M802053200 |
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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.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M802053200</identifier><identifier>PMID: 18426792</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>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</subject><ispartof>The Journal of biological chemistry, 2008-07, Vol.283 (27), p.18505-18512</ispartof><rights>2008 © 2008 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c532t-5c391cf8cd1bd2d5f4e1b5999834ee941602feb8bc8360850a9464a43cdd2de03</citedby><cites>FETCH-LOGICAL-c532t-5c391cf8cd1bd2d5f4e1b5999834ee941602feb8bc8360850a9464a43cdd2de03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18426792$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Horman, Sandrine</creatorcontrib><creatorcontrib>Morel, Nicole</creatorcontrib><creatorcontrib>Vertommen, Didier</creatorcontrib><creatorcontrib>Hussain, Nusrat</creatorcontrib><creatorcontrib>Neumann, Dietbert</creatorcontrib><creatorcontrib>Beauloye, Christophe</creatorcontrib><creatorcontrib>Najjar, Nicole El</creatorcontrib><creatorcontrib>Forcet, Christelle</creatorcontrib><creatorcontrib>Viollet, Benoit</creatorcontrib><creatorcontrib>Walsh, Michael P.</creatorcontrib><creatorcontrib>Hue, Louis</creatorcontrib><creatorcontrib>Rider, Mark H.</creatorcontrib><title>AMP-activated Protein Kinase Phosphorylates and Desensitizes Smooth Muscle Myosin Light Chain Kinase</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><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.</description><subject>Adenosine Triphosphate - chemistry</subject><subject>Adenosine Triphosphate - genetics</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>AMP-Activated Protein Kinases</subject><subject>Animals</subject><subject>Aorta - chemistry</subject><subject>Aorta - enzymology</subject><subject>Benzimidazoles - pharmacology</subject><subject>Calcium - metabolism</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - chemistry</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - genetics</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>Calmodulin - genetics</subject><subject>Calmodulin - metabolism</subject><subject>Cattle</subject><subject>Cells, Cultured</subject><subject>Chickens</subject><subject>Male</subject><subject>Mice</subject><subject>Mice, Knockout</subject><subject>Multienzyme Complexes - chemistry</subject><subject>Multienzyme Complexes - genetics</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Muscle Contraction - drug effects</subject><subject>Muscle Contraction - physiology</subject><subject>Muscle Tonus - drug effects</subject><subject>Muscle Tonus - physiology</subject><subject>Muscle, Smooth - chemistry</subject><subject>Muscle, Smooth - enzymology</subject><subject>Myocytes, Smooth Muscle - chemistry</subject><subject>Myocytes, Smooth Muscle - enzymology</subject><subject>Myosin-Light-Chain Kinase - chemistry</subject><subject>Myosin-Light-Chain Kinase - genetics</subject><subject>Myosin-Light-Chain Kinase - metabolism</subject><subject>Naphthalimides - pharmacology</subject><subject>Phenylephrine - pharmacology</subject><subject>Phosphorylation - drug effects</subject><subject>Potassium Chloride - pharmacology</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Vasoconstriction - drug effects</subject><subject>Vasoconstriction - physiology</subject><subject>Vasoconstrictor Agents - pharmacology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS1ERZeFK0fIAXHLMrbzYR-r5avqrlipVOJmOfakcZXEi50tWv56XGXVnhC-jOT5zdPMe4S8obCiUBcf7xqz2gpgUHIG8IwsKAie85L-fE4WAIzmkpXinLyM8Q7SKyR9Qc6pKFhVS7Yg9mK7y7WZ3L2e0Ga74Cd0Y3blRh0x23U-7jsfjn3qxkyPNvuEEcfoJvcnfVwP3k9dtj1E02O2PfqYZjfutpuydacfdV6Rs1b3EV-f6pLcfPn8Y_0t33z_erm-2OQmbT_lpeGSmlYYSxvLbNkWSJtSSil4gSgLWgFrsRGNEbwCUYKWRVXoghubcAS-JB9m3X3wvw4YJzW4aLDv9Yj-EFUl09UlFf8FGdSiqusHcDWDJvgYA7ZqH9ygw1FRUA8BqBSAegogDbw9KR-aAe0TfnI8Ae9noEs2_XYBVeO86XBQTHDF6kSWSWtJ3s1Yq73St8FFdXPNgHIACTKZkggxE5gcvXcYVDQOR4M2iZpJWe_-teRffcOpVg</recordid><startdate>20080704</startdate><enddate>20080704</enddate><creator>Horman, Sandrine</creator><creator>Morel, Nicole</creator><creator>Vertommen, Didier</creator><creator>Hussain, Nusrat</creator><creator>Neumann, Dietbert</creator><creator>Beauloye, Christophe</creator><creator>Najjar, Nicole El</creator><creator>Forcet, Christelle</creator><creator>Viollet, Benoit</creator><creator>Walsh, Michael P.</creator><creator>Hue, Louis</creator><creator>Rider, Mark H.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20080704</creationdate><title>AMP-activated Protein Kinase Phosphorylates and Desensitizes Smooth Muscle Myosin Light Chain Kinase</title><author>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.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c532t-5c391cf8cd1bd2d5f4e1b5999834ee941602feb8bc8360850a9464a43cdd2de03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Adenosine Triphosphate - chemistry</topic><topic>Adenosine Triphosphate - genetics</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>AMP-Activated Protein Kinases</topic><topic>Animals</topic><topic>Aorta - chemistry</topic><topic>Aorta - enzymology</topic><topic>Benzimidazoles - pharmacology</topic><topic>Calcium - metabolism</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - antagonists & inhibitors</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - chemistry</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - genetics</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</topic><topic>Calmodulin - genetics</topic><topic>Calmodulin - metabolism</topic><topic>Cattle</topic><topic>Cells, Cultured</topic><topic>Chickens</topic><topic>Male</topic><topic>Mice</topic><topic>Mice, Knockout</topic><topic>Multienzyme Complexes - chemistry</topic><topic>Multienzyme Complexes - genetics</topic><topic>Multienzyme Complexes - metabolism</topic><topic>Muscle Contraction - drug effects</topic><topic>Muscle Contraction - physiology</topic><topic>Muscle Tonus - drug effects</topic><topic>Muscle Tonus - physiology</topic><topic>Muscle, Smooth - chemistry</topic><topic>Muscle, Smooth - enzymology</topic><topic>Myocytes, Smooth Muscle - chemistry</topic><topic>Myocytes, Smooth Muscle - enzymology</topic><topic>Myosin-Light-Chain Kinase - chemistry</topic><topic>Myosin-Light-Chain Kinase - genetics</topic><topic>Myosin-Light-Chain Kinase - metabolism</topic><topic>Naphthalimides - pharmacology</topic><topic>Phenylephrine - pharmacology</topic><topic>Phosphorylation - drug effects</topic><topic>Potassium Chloride - pharmacology</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Vasoconstriction - drug effects</topic><topic>Vasoconstriction - physiology</topic><topic>Vasoconstrictor Agents - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Horman, Sandrine</creatorcontrib><creatorcontrib>Morel, Nicole</creatorcontrib><creatorcontrib>Vertommen, Didier</creatorcontrib><creatorcontrib>Hussain, Nusrat</creatorcontrib><creatorcontrib>Neumann, Dietbert</creatorcontrib><creatorcontrib>Beauloye, Christophe</creatorcontrib><creatorcontrib>Najjar, Nicole El</creatorcontrib><creatorcontrib>Forcet, Christelle</creatorcontrib><creatorcontrib>Viollet, Benoit</creatorcontrib><creatorcontrib>Walsh, Michael P.</creatorcontrib><creatorcontrib>Hue, Louis</creatorcontrib><creatorcontrib>Rider, Mark H.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Horman, Sandrine</au><au>Morel, Nicole</au><au>Vertommen, Didier</au><au>Hussain, Nusrat</au><au>Neumann, Dietbert</au><au>Beauloye, Christophe</au><au>Najjar, Nicole El</au><au>Forcet, Christelle</au><au>Viollet, Benoit</au><au>Walsh, Michael P.</au><au>Hue, Louis</au><au>Rider, Mark H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>AMP-activated Protein Kinase Phosphorylates and Desensitizes Smooth Muscle Myosin Light Chain Kinase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2008-07-04</date><risdate>2008</risdate><volume>283</volume><issue>27</issue><spage>18505</spage><epage>18512</epage><pages>18505-18512</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>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.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18426792</pmid><doi>10.1074/jbc.M802053200</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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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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