CaMKII-Mediated Phosphorylation of the Myosin Motor Myo1c Is Required for Insulin-Stimulated GLUT4 Translocation in Adipocytes
The unconventional myosin Myo1c has been implicated in insulin-regulated GLUT4 translocation to the plasma membrane in adipocytes. We show that Myo1c undergoes insulin-dependent phosphorylation at S701. Phosphorylation was accompanied by enhanced 14-3-3 binding and reduced calmodulin binding. Recomb...
Gespeichert in:
| Veröffentlicht in: | Cell metabolism 2008-11, Vol.8 (5), p.384-398 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 398 |
|---|---|
| container_issue | 5 |
| container_start_page | 384 |
| container_title | Cell metabolism |
| container_volume | 8 |
| creator | Yip, Ming Fai Ramm, Georg Larance, Mark Hoehn, Kyle L. Wagner, Mark C. Guilhaus, Michael James, David E. |
| description | The unconventional myosin Myo1c has been implicated in insulin-regulated GLUT4 translocation to the plasma membrane in adipocytes. We show that Myo1c undergoes insulin-dependent phosphorylation at S701. Phosphorylation was accompanied by enhanced 14-3-3 binding and reduced calmodulin binding. Recombinant CaMKII phosphorylated Myo1c in vitro and siRNA knockdown of CaMKIIδ abolished insulin-dependent Myo1c phosphorylation in vivo. CaMKII activity was increased upon insulin treatment and the CaMKII inhibitors CN21 and KN-62 or the Ca
2+ chelator BAPTA-AM blocked insulin-dependent Myo1c phosphorylation and insulin-stimulated glucose transport in adipocytes. Myo1c ATPase activity was increased after CaMKII phosphorylation in vitro and after insulin stimulation of CHO/IR/IRS-1 cells. Expression of wild-type Myo1c, but not S701A or ATPase dead mutant K111A, rescued the inhibition of GLUT4 translocation by siRNA-mediated Myo1c knockdown. These data suggest that insulin regulates Myo1c function via CaMKII-dependent phosphorylation, and these events play a role in insulin-regulated GLUT4 trafficking in adipocytes likely involving Myo1c motor activity. |
| doi_str_mv | 10.1016/j.cmet.2008.09.011 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69852267</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1550413108002969</els_id><sourcerecordid>69852267</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3791-5fb87dc4a262254061603cacaf388e24a4607daca07335e283ef8e63b44f1ad23</originalsourceid><addsrcrecordid>eNp9kE1r3DAQhkVISdIkf6CH4lNudkcflm3IJSxtarpLS7s5C608ZrXY1kaSC3vpb6-2u5BbTzMj3vcBPYR8oFBQoPLTrjAjxoIB1AU0BVB6QW5ow1leCQaXaS9LyAXl9Jq8D2EHwCVv-BW5pg0IWVZwQ_4s9Opb2-Yr7KyO2GU_ti7st84fBh2tmzLXZ3GL2erggp2ylYvOHw9qsjZkP_F1tj61-vTaTmEe7JT_inach3-w5-XLWmRrr6cwOHMCJspTZ_fOHCKGO_Ku10PA-_O8JS9fPq8XX_Pl9-d28bTMDa8ampf9pq46IzSTjJUCJJXAjTa653WNTGghoerSDRXnJbKaY1-j5Bsheqo7xm_Jw4m79-51xhDVaIPBYdATujko2dQlY7JKQXYKGu9C8Nirvbej9gdFQR2tq506WldH6woalayn0sczfd6M2L1VzppT4PEUwPTH3xa9CsbiZJJ0jyaqztn_8f8CzRyT7A</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69852267</pqid></control><display><type>article</type><title>CaMKII-Mediated Phosphorylation of the Myosin Motor Myo1c Is Required for Insulin-Stimulated GLUT4 Translocation in Adipocytes</title><source>MEDLINE</source><source>Cell Press Free Archives</source><source>ScienceDirect Journals (5 years ago - present)</source><source>EZB-FREE-00999 freely available EZB journals</source><creator>Yip, Ming Fai ; Ramm, Georg ; Larance, Mark ; Hoehn, Kyle L. ; Wagner, Mark C. ; Guilhaus, Michael ; James, David E.</creator><creatorcontrib>Yip, Ming Fai ; Ramm, Georg ; Larance, Mark ; Hoehn, Kyle L. ; Wagner, Mark C. ; Guilhaus, Michael ; James, David E.</creatorcontrib><description>The unconventional myosin Myo1c has been implicated in insulin-regulated GLUT4 translocation to the plasma membrane in adipocytes. We show that Myo1c undergoes insulin-dependent phosphorylation at S701. Phosphorylation was accompanied by enhanced 14-3-3 binding and reduced calmodulin binding. Recombinant CaMKII phosphorylated Myo1c in vitro and siRNA knockdown of CaMKIIδ abolished insulin-dependent Myo1c phosphorylation in vivo. CaMKII activity was increased upon insulin treatment and the CaMKII inhibitors CN21 and KN-62 or the Ca
2+ chelator BAPTA-AM blocked insulin-dependent Myo1c phosphorylation and insulin-stimulated glucose transport in adipocytes. Myo1c ATPase activity was increased after CaMKII phosphorylation in vitro and after insulin stimulation of CHO/IR/IRS-1 cells. Expression of wild-type Myo1c, but not S701A or ATPase dead mutant K111A, rescued the inhibition of GLUT4 translocation by siRNA-mediated Myo1c knockdown. These data suggest that insulin regulates Myo1c function via CaMKII-dependent phosphorylation, and these events play a role in insulin-regulated GLUT4 trafficking in adipocytes likely involving Myo1c motor activity.</description><identifier>ISSN: 1550-4131</identifier><identifier>EISSN: 1932-7420</identifier><identifier>DOI: 10.1016/j.cmet.2008.09.011</identifier><identifier>PMID: 19046570</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine - analogs & derivatives ; 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine - pharmacology ; 14-3-3 Proteins - metabolism ; Adipocytes - metabolism ; Animals ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 - antagonists & inhibitors ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 - physiology ; Cell Line ; Cricetinae ; Glucose Transporter Type 4 - metabolism ; HUMDISEASE ; Insulin - physiology ; Mice ; Myosin Type I ; Myosins - metabolism ; Phosphorylation ; Protein Transport ; SIGNALING ; SYSBIO</subject><ispartof>Cell metabolism, 2008-11, Vol.8 (5), p.384-398</ispartof><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3791-5fb87dc4a262254061603cacaf388e24a4607daca07335e283ef8e63b44f1ad23</citedby><cites>FETCH-LOGICAL-c3791-5fb87dc4a262254061603cacaf388e24a4607daca07335e283ef8e63b44f1ad23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.cmet.2008.09.011$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19046570$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yip, Ming Fai</creatorcontrib><creatorcontrib>Ramm, Georg</creatorcontrib><creatorcontrib>Larance, Mark</creatorcontrib><creatorcontrib>Hoehn, Kyle L.</creatorcontrib><creatorcontrib>Wagner, Mark C.</creatorcontrib><creatorcontrib>Guilhaus, Michael</creatorcontrib><creatorcontrib>James, David E.</creatorcontrib><title>CaMKII-Mediated Phosphorylation of the Myosin Motor Myo1c Is Required for Insulin-Stimulated GLUT4 Translocation in Adipocytes</title><title>Cell metabolism</title><addtitle>Cell Metab</addtitle><description>The unconventional myosin Myo1c has been implicated in insulin-regulated GLUT4 translocation to the plasma membrane in adipocytes. We show that Myo1c undergoes insulin-dependent phosphorylation at S701. Phosphorylation was accompanied by enhanced 14-3-3 binding and reduced calmodulin binding. Recombinant CaMKII phosphorylated Myo1c in vitro and siRNA knockdown of CaMKIIδ abolished insulin-dependent Myo1c phosphorylation in vivo. CaMKII activity was increased upon insulin treatment and the CaMKII inhibitors CN21 and KN-62 or the Ca
2+ chelator BAPTA-AM blocked insulin-dependent Myo1c phosphorylation and insulin-stimulated glucose transport in adipocytes. Myo1c ATPase activity was increased after CaMKII phosphorylation in vitro and after insulin stimulation of CHO/IR/IRS-1 cells. Expression of wild-type Myo1c, but not S701A or ATPase dead mutant K111A, rescued the inhibition of GLUT4 translocation by siRNA-mediated Myo1c knockdown. These data suggest that insulin regulates Myo1c function via CaMKII-dependent phosphorylation, and these events play a role in insulin-regulated GLUT4 trafficking in adipocytes likely involving Myo1c motor activity.</description><subject>1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine - analogs & derivatives</subject><subject>1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine - pharmacology</subject><subject>14-3-3 Proteins - metabolism</subject><subject>Adipocytes - metabolism</subject><subject>Animals</subject><subject>Calcium-Calmodulin-Dependent Protein Kinase Type 2 - antagonists & inhibitors</subject><subject>Calcium-Calmodulin-Dependent Protein Kinase Type 2 - physiology</subject><subject>Cell Line</subject><subject>Cricetinae</subject><subject>Glucose Transporter Type 4 - metabolism</subject><subject>HUMDISEASE</subject><subject>Insulin - physiology</subject><subject>Mice</subject><subject>Myosin Type I</subject><subject>Myosins - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Transport</subject><subject>SIGNALING</subject><subject>SYSBIO</subject><issn>1550-4131</issn><issn>1932-7420</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE1r3DAQhkVISdIkf6CH4lNudkcflm3IJSxtarpLS7s5C608ZrXY1kaSC3vpb6-2u5BbTzMj3vcBPYR8oFBQoPLTrjAjxoIB1AU0BVB6QW5ow1leCQaXaS9LyAXl9Jq8D2EHwCVv-BW5pg0IWVZwQ_4s9Opb2-Yr7KyO2GU_ti7st84fBh2tmzLXZ3GL2erggp2ylYvOHw9qsjZkP_F1tj61-vTaTmEe7JT_inach3-w5-XLWmRrr6cwOHMCJspTZ_fOHCKGO_Ku10PA-_O8JS9fPq8XX_Pl9-d28bTMDa8ampf9pq46IzSTjJUCJJXAjTa653WNTGghoerSDRXnJbKaY1-j5Bsheqo7xm_Jw4m79-51xhDVaIPBYdATujko2dQlY7JKQXYKGu9C8Nirvbej9gdFQR2tq506WldH6woalayn0sczfd6M2L1VzppT4PEUwPTH3xa9CsbiZJJ0jyaqztn_8f8CzRyT7A</recordid><startdate>200811</startdate><enddate>200811</enddate><creator>Yip, Ming Fai</creator><creator>Ramm, Georg</creator><creator>Larance, Mark</creator><creator>Hoehn, Kyle L.</creator><creator>Wagner, Mark C.</creator><creator>Guilhaus, Michael</creator><creator>James, David E.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope></search><sort><creationdate>200811</creationdate><title>CaMKII-Mediated Phosphorylation of the Myosin Motor Myo1c Is Required for Insulin-Stimulated GLUT4 Translocation in Adipocytes</title><author>Yip, Ming Fai ; Ramm, Georg ; Larance, Mark ; Hoehn, Kyle L. ; Wagner, Mark C. ; Guilhaus, Michael ; James, David E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3791-5fb87dc4a262254061603cacaf388e24a4607daca07335e283ef8e63b44f1ad23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine - analogs & derivatives</topic><topic>1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine - pharmacology</topic><topic>14-3-3 Proteins - metabolism</topic><topic>Adipocytes - metabolism</topic><topic>Animals</topic><topic>Calcium-Calmodulin-Dependent Protein Kinase Type 2 - antagonists & inhibitors</topic><topic>Calcium-Calmodulin-Dependent Protein Kinase Type 2 - physiology</topic><topic>Cell Line</topic><topic>Cricetinae</topic><topic>Glucose Transporter Type 4 - metabolism</topic><topic>HUMDISEASE</topic><topic>Insulin - physiology</topic><topic>Mice</topic><topic>Myosin Type I</topic><topic>Myosins - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Transport</topic><topic>SIGNALING</topic><topic>SYSBIO</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yip, Ming Fai</creatorcontrib><creatorcontrib>Ramm, Georg</creatorcontrib><creatorcontrib>Larance, Mark</creatorcontrib><creatorcontrib>Hoehn, Kyle L.</creatorcontrib><creatorcontrib>Wagner, Mark C.</creatorcontrib><creatorcontrib>Guilhaus, Michael</creatorcontrib><creatorcontrib>James, David E.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Cell metabolism</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yip, Ming Fai</au><au>Ramm, Georg</au><au>Larance, Mark</au><au>Hoehn, Kyle L.</au><au>Wagner, Mark C.</au><au>Guilhaus, Michael</au><au>James, David E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CaMKII-Mediated Phosphorylation of the Myosin Motor Myo1c Is Required for Insulin-Stimulated GLUT4 Translocation in Adipocytes</atitle><jtitle>Cell metabolism</jtitle><addtitle>Cell Metab</addtitle><date>2008-11</date><risdate>2008</risdate><volume>8</volume><issue>5</issue><spage>384</spage><epage>398</epage><pages>384-398</pages><issn>1550-4131</issn><eissn>1932-7420</eissn><abstract>The unconventional myosin Myo1c has been implicated in insulin-regulated GLUT4 translocation to the plasma membrane in adipocytes. We show that Myo1c undergoes insulin-dependent phosphorylation at S701. Phosphorylation was accompanied by enhanced 14-3-3 binding and reduced calmodulin binding. Recombinant CaMKII phosphorylated Myo1c in vitro and siRNA knockdown of CaMKIIδ abolished insulin-dependent Myo1c phosphorylation in vivo. CaMKII activity was increased upon insulin treatment and the CaMKII inhibitors CN21 and KN-62 or the Ca
2+ chelator BAPTA-AM blocked insulin-dependent Myo1c phosphorylation and insulin-stimulated glucose transport in adipocytes. Myo1c ATPase activity was increased after CaMKII phosphorylation in vitro and after insulin stimulation of CHO/IR/IRS-1 cells. Expression of wild-type Myo1c, but not S701A or ATPase dead mutant K111A, rescued the inhibition of GLUT4 translocation by siRNA-mediated Myo1c knockdown. These data suggest that insulin regulates Myo1c function via CaMKII-dependent phosphorylation, and these events play a role in insulin-regulated GLUT4 trafficking in adipocytes likely involving Myo1c motor activity.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>19046570</pmid><doi>10.1016/j.cmet.2008.09.011</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1550-4131 |
| ispartof | Cell metabolism, 2008-11, Vol.8 (5), p.384-398 |
| issn | 1550-4131 1932-7420 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69852267 |
| source | MEDLINE; Cell Press Free Archives; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals |
| subjects | 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine - analogs & derivatives 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine - pharmacology 14-3-3 Proteins - metabolism Adipocytes - metabolism Animals Calcium-Calmodulin-Dependent Protein Kinase Type 2 - antagonists & inhibitors Calcium-Calmodulin-Dependent Protein Kinase Type 2 - physiology Cell Line Cricetinae Glucose Transporter Type 4 - metabolism HUMDISEASE Insulin - physiology Mice Myosin Type I Myosins - metabolism Phosphorylation Protein Transport SIGNALING SYSBIO |
| title | CaMKII-Mediated Phosphorylation of the Myosin Motor Myo1c Is Required for Insulin-Stimulated GLUT4 Translocation in Adipocytes |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-06T22%3A47%3A12IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=CaMKII-Mediated%20Phosphorylation%20of%20the%20Myosin%20Motor%20Myo1c%20Is%20Required%20for%20Insulin-Stimulated%20GLUT4%20Translocation%20in%20Adipocytes&rft.jtitle=Cell%20metabolism&rft.au=Yip,%20Ming%20Fai&rft.date=2008-11&rft.volume=8&rft.issue=5&rft.spage=384&rft.epage=398&rft.pages=384-398&rft.issn=1550-4131&rft.eissn=1932-7420&rft_id=info:doi/10.1016/j.cmet.2008.09.011&rft_dat=%3Cproquest_cross%3E69852267%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=69852267&rft_id=info:pmid/19046570&rft_els_id=S1550413108002969&rfr_iscdi=true |