Implication of phosphorylation of the myosin II regulatory light chain in insulin-stimulated GLUT4 translocation in 3T3-F442A adipocytes
In adipocytes, insulin stimulates glucose transport primarily by promoting the translocation of GLUT4 to the plasma membrane. Requirements for Ca(2+)/calmodulin during insulin-stimulated GLUT4 translocation have been demonstrated; however, the mechanism of action of Ca(2+) in this process is unknown...
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| Veröffentlicht in: | Experimental & molecular medicine 2006-04, Vol.38 (2), p.180-189 |
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| creator | Choi, Young Ok Ryu, Hee Jeong Kim, Hye Rim Song, Young Sook Kim, Cheonghwan Lee, Wan Choe, Han Leem, Chae Hun Jang, Yeon Jin |
| description | In adipocytes, insulin stimulates glucose transport primarily by promoting the translocation of GLUT4 to the plasma membrane. Requirements for Ca(2+)/calmodulin during insulin-stimulated GLUT4 translocation have been demonstrated; however, the mechanism of action of Ca(2+) in this process is unknown. Recently, myosin II, whose function in non-muscle cells is primarily regulated by phosphorylation of its regulatory light chain by the Ca(2+)/calmodulin-dependent myosin light chain kinase (MLCK), was implicated in insulin-stimulated GLUT4 translocation. The present studies in 3T3-F442A adipocytes demonstrate the novel finding that insulin significantly increases phosphorylation of the myosin II RLC in a Ca(2+)-dependent manner. In addition, ML-7, a selective inhibitor of MLCK, as well as inhibitors of myosin II, such as blebbistatin and 2,3-butanedione monoxime, block insulin-stimulated GLUT4 translocation and subsequent glucose transport. Our studies suggest that MLCK may be a regulatory target of Ca(2+)/calmodulin and may play an important role in insulin-stimulated glucose transport in adipocytes. |
| doi_str_mv | 10.1038/emm.2006.22 |
| format | Article |
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Requirements for Ca(2+)/calmodulin during insulin-stimulated GLUT4 translocation have been demonstrated; however, the mechanism of action of Ca(2+) in this process is unknown. Recently, myosin II, whose function in non-muscle cells is primarily regulated by phosphorylation of its regulatory light chain by the Ca(2+)/calmodulin-dependent myosin light chain kinase (MLCK), was implicated in insulin-stimulated GLUT4 translocation. The present studies in 3T3-F442A adipocytes demonstrate the novel finding that insulin significantly increases phosphorylation of the myosin II RLC in a Ca(2+)-dependent manner. In addition, ML-7, a selective inhibitor of MLCK, as well as inhibitors of myosin II, such as blebbistatin and 2,3-butanedione monoxime, block insulin-stimulated GLUT4 translocation and subsequent glucose transport. Our studies suggest that MLCK may be a regulatory target of Ca(2+)/calmodulin and may play an important role in insulin-stimulated glucose transport in adipocytes.</description><identifier>ISSN: 1226-3613</identifier><identifier>ISSN: 2092-6413</identifier><identifier>EISSN: 2092-6413</identifier><identifier>DOI: 10.1038/emm.2006.22</identifier><identifier>PMID: 16672772</identifier><language>eng</language><publisher>United States: Springer Nature B.V</publisher><subject>3T3 Cells ; Adipocytes - cytology ; Adipocytes - drug effects ; Adipocytes - metabolism ; Animals ; Azepines - pharmacology ; Calmodulin - antagonists & inhibitors ; Calmodulin - physiology ; Dose-Response Relationship, Drug ; Enzyme Inhibitors - pharmacology ; Glucose Transporter Type 4 - metabolism ; Insulin - pharmacology ; Mice ; Myosin Type II - metabolism ; Myosin-Light-Chain Kinase - antagonists & inhibitors ; Myosin-Light-Chain Kinase - metabolism ; Naphthalenes - pharmacology ; Phosphorylation ; Protein Transport - drug effects</subject><ispartof>Experimental & molecular medicine, 2006-04, Vol.38 (2), p.180-189</ispartof><rights>Copyright Nature Publishing Group Apr 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-b879c8404255b134c257c50e7243d33d80455b9022a7de10ce235889b29909193</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,860,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16672772$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Choi, Young Ok</creatorcontrib><creatorcontrib>Ryu, Hee Jeong</creatorcontrib><creatorcontrib>Kim, Hye Rim</creatorcontrib><creatorcontrib>Song, Young Sook</creatorcontrib><creatorcontrib>Kim, Cheonghwan</creatorcontrib><creatorcontrib>Lee, Wan</creatorcontrib><creatorcontrib>Choe, Han</creatorcontrib><creatorcontrib>Leem, Chae Hun</creatorcontrib><creatorcontrib>Jang, Yeon Jin</creatorcontrib><title>Implication of phosphorylation of the myosin II regulatory light chain in insulin-stimulated GLUT4 translocation in 3T3-F442A adipocytes</title><title>Experimental & molecular medicine</title><addtitle>Exp Mol Med</addtitle><description>In adipocytes, insulin stimulates glucose transport primarily by promoting the translocation of GLUT4 to the plasma membrane. 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Our studies suggest that MLCK may be a regulatory target of Ca(2+)/calmodulin and may play an important role in insulin-stimulated glucose transport in adipocytes.</description><subject>3T3 Cells</subject><subject>Adipocytes - cytology</subject><subject>Adipocytes - drug effects</subject><subject>Adipocytes - metabolism</subject><subject>Animals</subject><subject>Azepines - pharmacology</subject><subject>Calmodulin - antagonists & inhibitors</subject><subject>Calmodulin - physiology</subject><subject>Dose-Response Relationship, Drug</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Glucose Transporter Type 4 - metabolism</subject><subject>Insulin - pharmacology</subject><subject>Mice</subject><subject>Myosin Type II - metabolism</subject><subject>Myosin-Light-Chain Kinase - antagonists & inhibitors</subject><subject>Myosin-Light-Chain Kinase - metabolism</subject><subject>Naphthalenes - pharmacology</subject><subject>Phosphorylation</subject><subject>Protein Transport - 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Academic</collection><jtitle>Experimental & molecular medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Choi, Young Ok</au><au>Ryu, Hee Jeong</au><au>Kim, Hye Rim</au><au>Song, Young Sook</au><au>Kim, Cheonghwan</au><au>Lee, Wan</au><au>Choe, Han</au><au>Leem, Chae Hun</au><au>Jang, Yeon Jin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Implication of phosphorylation of the myosin II regulatory light chain in insulin-stimulated GLUT4 translocation in 3T3-F442A adipocytes</atitle><jtitle>Experimental & molecular medicine</jtitle><addtitle>Exp Mol Med</addtitle><date>2006-04-30</date><risdate>2006</risdate><volume>38</volume><issue>2</issue><spage>180</spage><epage>189</epage><pages>180-189</pages><issn>1226-3613</issn><issn>2092-6413</issn><eissn>2092-6413</eissn><abstract>In adipocytes, insulin stimulates glucose transport primarily by promoting the translocation of GLUT4 to the plasma membrane. Requirements for Ca(2+)/calmodulin during insulin-stimulated GLUT4 translocation have been demonstrated; however, the mechanism of action of Ca(2+) in this process is unknown. Recently, myosin II, whose function in non-muscle cells is primarily regulated by phosphorylation of its regulatory light chain by the Ca(2+)/calmodulin-dependent myosin light chain kinase (MLCK), was implicated in insulin-stimulated GLUT4 translocation. The present studies in 3T3-F442A adipocytes demonstrate the novel finding that insulin significantly increases phosphorylation of the myosin II RLC in a Ca(2+)-dependent manner. In addition, ML-7, a selective inhibitor of MLCK, as well as inhibitors of myosin II, such as blebbistatin and 2,3-butanedione monoxime, block insulin-stimulated GLUT4 translocation and subsequent glucose transport. Our studies suggest that MLCK may be a regulatory target of Ca(2+)/calmodulin and may play an important role in insulin-stimulated glucose transport in adipocytes.</abstract><cop>United States</cop><pub>Springer Nature B.V</pub><pmid>16672772</pmid><doi>10.1038/emm.2006.22</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 3T3 Cells Adipocytes - cytology Adipocytes - drug effects Adipocytes - metabolism Animals Azepines - pharmacology Calmodulin - antagonists & inhibitors Calmodulin - physiology Dose-Response Relationship, Drug Enzyme Inhibitors - pharmacology Glucose Transporter Type 4 - metabolism Insulin - pharmacology Mice Myosin Type II - metabolism Myosin-Light-Chain Kinase - antagonists & inhibitors Myosin-Light-Chain Kinase - metabolism Naphthalenes - pharmacology Phosphorylation Protein Transport - drug effects |
| title | Implication of phosphorylation of the myosin II regulatory light chain in insulin-stimulated GLUT4 translocation in 3T3-F442A adipocytes |
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