Compartmentalization of the exocyst complex in lipid rafts controls Glut4 vesicle tethering
Lipid raft microdomains act as organizing centers for signal transduction. We report here that the exocyst complex, consisting of Exo70, Sec6, and Sec8, regulates the compartmentalization of Glut4-containing vesicles at lipid raft domains in adipocytes. Exo70 is recruited by the G protein TC10 after...
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| Veröffentlicht in: | Molecular biology of the cell 2006-05, Vol.17 (5), p.2303-2311 |
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| creator | Inoue, Mayumi Chiang, Shian-Huey Chang, Louise Chen, Xiao-Wei Saltiel, Alan R |
| description | Lipid raft microdomains act as organizing centers for signal transduction. We report here that the exocyst complex, consisting of Exo70, Sec6, and Sec8, regulates the compartmentalization of Glut4-containing vesicles at lipid raft domains in adipocytes. Exo70 is recruited by the G protein TC10 after activation by insulin and brings with it Sec6 and Sec8. Knockdowns of these proteins block insulin-stimulated glucose uptake. Moreover, their targeting to lipid rafts is required for glucose uptake and Glut4 docking at the plasma membrane. The assembly of this complex also requires the PDZ domain protein SAP97, a member of the MAGUKs family, which binds to Sec8 upon its translocation to the lipid raft. Exocyst assembly at lipid rafts sets up targeting sites for Glut4 vesicles, which transiently associate with these microdomains upon stimulation of cells with insulin. These results suggest that the TC10/exocyst complex/SAP97 axis plays an important role in the tethering of Glut4 vesicles to the plasma membrane in adipocytes. |
| doi_str_mv | 10.1091/mbc.E06-01-0030 |
| format | Article |
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We report here that the exocyst complex, consisting of Exo70, Sec6, and Sec8, regulates the compartmentalization of Glut4-containing vesicles at lipid raft domains in adipocytes. Exo70 is recruited by the G protein TC10 after activation by insulin and brings with it Sec6 and Sec8. Knockdowns of these proteins block insulin-stimulated glucose uptake. Moreover, their targeting to lipid rafts is required for glucose uptake and Glut4 docking at the plasma membrane. The assembly of this complex also requires the PDZ domain protein SAP97, a member of the MAGUKs family, which binds to Sec8 upon its translocation to the lipid raft. Exocyst assembly at lipid rafts sets up targeting sites for Glut4 vesicles, which transiently associate with these microdomains upon stimulation of cells with insulin. These results suggest that the TC10/exocyst complex/SAP97 axis plays an important role in the tethering of Glut4 vesicles to the plasma membrane in adipocytes.</description><identifier>ISSN: 1059-1524</identifier><identifier>EISSN: 1939-4586</identifier><identifier>DOI: 10.1091/mbc.E06-01-0030</identifier><identifier>PMID: 16525015</identifier><language>eng</language><publisher>United States: The American Society for Cell Biology</publisher><subject>3T3-L1 Cells ; Adaptor Proteins, Signal Transducing - metabolism ; Adipocytes - drug effects ; Adipocytes - metabolism ; Animals ; Apoptosis ; Carrier Proteins - analysis ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Membrane - metabolism ; Discs Large Homolog 1 Protein ; Glucose - metabolism ; Glucose Transporter Type 4 - metabolism ; Guanylate Kinases ; Insulin - pharmacology ; Membrane Fusion ; Membrane Microdomains - chemistry ; Membrane Microdomains - metabolism ; Membrane Proteins - analysis ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Mice ; Protein Structure, Tertiary ; Protein Transport ; rho GTP-Binding Proteins ; RNA Interference ; Transport Vesicles - metabolism ; Vesicular Transport Proteins</subject><ispartof>Molecular biology of the cell, 2006-05, Vol.17 (5), p.2303-2311</ispartof><rights>Copyright © 2006, The American Society for Cell Biology 2006</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c534t-5a4db667217986f47ec874722f2cfcc56fa000af863f86f3ef936e0ca86768593</citedby><cites>FETCH-LOGICAL-c534t-5a4db667217986f47ec874722f2cfcc56fa000af863f86f3ef936e0ca86768593</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1446102/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1446102/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16525015$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Inoue, Mayumi</creatorcontrib><creatorcontrib>Chiang, Shian-Huey</creatorcontrib><creatorcontrib>Chang, Louise</creatorcontrib><creatorcontrib>Chen, Xiao-Wei</creatorcontrib><creatorcontrib>Saltiel, Alan R</creatorcontrib><title>Compartmentalization of the exocyst complex in lipid rafts controls Glut4 vesicle tethering</title><title>Molecular biology of the cell</title><addtitle>Mol Biol Cell</addtitle><description>Lipid raft microdomains act as organizing centers for signal transduction. We report here that the exocyst complex, consisting of Exo70, Sec6, and Sec8, regulates the compartmentalization of Glut4-containing vesicles at lipid raft domains in adipocytes. Exo70 is recruited by the G protein TC10 after activation by insulin and brings with it Sec6 and Sec8. Knockdowns of these proteins block insulin-stimulated glucose uptake. Moreover, their targeting to lipid rafts is required for glucose uptake and Glut4 docking at the plasma membrane. The assembly of this complex also requires the PDZ domain protein SAP97, a member of the MAGUKs family, which binds to Sec8 upon its translocation to the lipid raft. Exocyst assembly at lipid rafts sets up targeting sites for Glut4 vesicles, which transiently associate with these microdomains upon stimulation of cells with insulin. These results suggest that the TC10/exocyst complex/SAP97 axis plays an important role in the tethering of Glut4 vesicles to the plasma membrane in adipocytes.</description><subject>3T3-L1 Cells</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Adipocytes - drug effects</subject><subject>Adipocytes - metabolism</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Carrier Proteins - analysis</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Membrane - metabolism</subject><subject>Discs Large Homolog 1 Protein</subject><subject>Glucose - metabolism</subject><subject>Glucose Transporter Type 4 - metabolism</subject><subject>Guanylate Kinases</subject><subject>Insulin - pharmacology</subject><subject>Membrane Fusion</subject><subject>Membrane Microdomains - chemistry</subject><subject>Membrane Microdomains - metabolism</subject><subject>Membrane Proteins - analysis</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Transport</subject><subject>rho GTP-Binding Proteins</subject><subject>RNA Interference</subject><subject>Transport Vesicles - metabolism</subject><subject>Vesicular Transport Proteins</subject><issn>1059-1524</issn><issn>1939-4586</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUU1PGzEQtVArEmjPvSGfelsY7_pj94KEIkqRInFpTz1YjjMGV951ajsR8OtxREThMJrRzJs3H4-QbwzOGQzsYlzZ82uQDbAGoIMjMmdDNzRc9PJTjUEMDRMtn5GTnP8CMM6lOiYzJkUrgIk5-bOI48akMuJUTPDPpvg40ehoeUCKj9E-5UJtxQR8pH6iwW_8mibjSq7pqaQYMr0J28LpDrO3AWnB2pv8dP-FfHYmZPx68Kfk94_rX4ufzfLu5nZxtWys6HhphOHrlZSqZWropeMKba-4alvXWmetkM4AgHG97Kq5Dt3QSQRreqlkL4bulFy-8m62qxHXtp6STNCb5EeTnnQ0Xn-sTP5B38ed3r-DQVsJvh8IUvy3xVz06LPFEMyEcZu1VAOA4vtJF69Am2LOCd3bEAZ6L4iugmgEqYHpvSC14-z9bv_xBwW6F5MRicQ</recordid><startdate>200605</startdate><enddate>200605</enddate><creator>Inoue, Mayumi</creator><creator>Chiang, Shian-Huey</creator><creator>Chang, Louise</creator><creator>Chen, Xiao-Wei</creator><creator>Saltiel, Alan R</creator><general>The American Society for Cell Biology</general><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><scope>5PM</scope></search><sort><creationdate>200605</creationdate><title>Compartmentalization of the exocyst complex in lipid rafts controls Glut4 vesicle tethering</title><author>Inoue, Mayumi ; Chiang, Shian-Huey ; Chang, Louise ; Chen, Xiao-Wei ; Saltiel, Alan R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c534t-5a4db667217986f47ec874722f2cfcc56fa000af863f86f3ef936e0ca86768593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>3T3-L1 Cells</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Adipocytes - drug effects</topic><topic>Adipocytes - metabolism</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Carrier Proteins - analysis</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Membrane - metabolism</topic><topic>Discs Large Homolog 1 Protein</topic><topic>Glucose - metabolism</topic><topic>Glucose Transporter Type 4 - metabolism</topic><topic>Guanylate Kinases</topic><topic>Insulin - pharmacology</topic><topic>Membrane Fusion</topic><topic>Membrane Microdomains - chemistry</topic><topic>Membrane Microdomains - metabolism</topic><topic>Membrane Proteins - analysis</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Transport</topic><topic>rho GTP-Binding Proteins</topic><topic>RNA Interference</topic><topic>Transport Vesicles - metabolism</topic><topic>Vesicular Transport Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Inoue, Mayumi</creatorcontrib><creatorcontrib>Chiang, Shian-Huey</creatorcontrib><creatorcontrib>Chang, Louise</creatorcontrib><creatorcontrib>Chen, Xiao-Wei</creatorcontrib><creatorcontrib>Saltiel, Alan R</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular biology of the cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Inoue, Mayumi</au><au>Chiang, Shian-Huey</au><au>Chang, Louise</au><au>Chen, Xiao-Wei</au><au>Saltiel, Alan R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Compartmentalization of the exocyst complex in lipid rafts controls Glut4 vesicle tethering</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2006-05</date><risdate>2006</risdate><volume>17</volume><issue>5</issue><spage>2303</spage><epage>2311</epage><pages>2303-2311</pages><issn>1059-1524</issn><eissn>1939-4586</eissn><abstract>Lipid raft microdomains act as organizing centers for signal transduction. We report here that the exocyst complex, consisting of Exo70, Sec6, and Sec8, regulates the compartmentalization of Glut4-containing vesicles at lipid raft domains in adipocytes. Exo70 is recruited by the G protein TC10 after activation by insulin and brings with it Sec6 and Sec8. Knockdowns of these proteins block insulin-stimulated glucose uptake. Moreover, their targeting to lipid rafts is required for glucose uptake and Glut4 docking at the plasma membrane. The assembly of this complex also requires the PDZ domain protein SAP97, a member of the MAGUKs family, which binds to Sec8 upon its translocation to the lipid raft. Exocyst assembly at lipid rafts sets up targeting sites for Glut4 vesicles, which transiently associate with these microdomains upon stimulation of cells with insulin. These results suggest that the TC10/exocyst complex/SAP97 axis plays an important role in the tethering of Glut4 vesicles to the plasma membrane in adipocytes.</abstract><cop>United States</cop><pub>The American Society for Cell Biology</pub><pmid>16525015</pmid><doi>10.1091/mbc.E06-01-0030</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 3T3-L1 Cells Adaptor Proteins, Signal Transducing - metabolism Adipocytes - drug effects Adipocytes - metabolism Animals Apoptosis Carrier Proteins - analysis Carrier Proteins - genetics Carrier Proteins - metabolism Cell Membrane - metabolism Discs Large Homolog 1 Protein Glucose - metabolism Glucose Transporter Type 4 - metabolism Guanylate Kinases Insulin - pharmacology Membrane Fusion Membrane Microdomains - chemistry Membrane Microdomains - metabolism Membrane Proteins - analysis Membrane Proteins - genetics Membrane Proteins - metabolism Mice Protein Structure, Tertiary Protein Transport rho GTP-Binding Proteins RNA Interference Transport Vesicles - metabolism Vesicular Transport Proteins |
| title | Compartmentalization of the exocyst complex in lipid rafts controls Glut4 vesicle tethering |
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