Insulin-responsive amino peptidase follows the Glut4 pathway but is dispensable for the formation and translocation of insulin-responsive vesicles
In fat and skeletal muscle cells, insulin-responsive amino peptidase (IRAP) along with glucose transporter 4 (Glut4) and sortilin, represents a major component protein of the insulin-responsive vesicles (IRVs). Here, we show that IRAP, similar to Glut4 and sortilin, is retrieved from endosomes to th...
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| Veröffentlicht in: | Molecular biology of the cell 2019-06, Vol.30 (12), p.1536-1543 |
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| container_title | Molecular biology of the cell |
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| creator | Pan, Xiang Meriin, Anatoli Huang, Guanrong Kandror, Konstantin V |
| description | In fat and skeletal muscle cells, insulin-responsive amino peptidase (IRAP) along with glucose transporter 4 (Glut4) and sortilin, represents a major component protein of the insulin-responsive vesicles (IRVs). Here, we show that IRAP, similar to Glut4 and sortilin, is retrieved from endosomes to the
-Golgi network by retromer. Unlike Glut4, retrograde transport of IRAP does not require sortilin, as retromer can directly bind to the cytoplasmic tail of IRAP. Ablation of IRAP in 3T3-L1 adipocytes shifts the endosomal pool of Glut4 to more acidic endosomes, but does not affect IRV targeting, stability, and insulin responsiveness of Glut4. |
| doi_str_mv | 10.1091/mbc.e18-12-0792 |
| format | Article |
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-Golgi network by retromer. Unlike Glut4, retrograde transport of IRAP does not require sortilin, as retromer can directly bind to the cytoplasmic tail of IRAP. Ablation of IRAP in 3T3-L1 adipocytes shifts the endosomal pool of Glut4 to more acidic endosomes, but does not affect IRV targeting, stability, and insulin responsiveness of Glut4.</description><identifier>ISSN: 1059-1524</identifier><identifier>EISSN: 1939-4586</identifier><identifier>DOI: 10.1091/mbc.e18-12-0792</identifier><identifier>PMID: 30943117</identifier><language>eng</language><publisher>United States: The American Society for Cell Biology</publisher><subject>3T3-L1 Cells ; Adipocytes - drug effects ; Adipocytes - metabolism ; Animals ; Cell Differentiation ; Cystinyl Aminopeptidase - metabolism ; Glucose - metabolism ; Glucose Transporter Type 4 - metabolism ; Insulin - pharmacology ; Mice ; Transport Vesicles - drug effects ; Transport Vesicles - metabolism ; Vesicular Transport Proteins - metabolism</subject><ispartof>Molecular biology of the cell, 2019-06, Vol.30 (12), p.1536-1543</ispartof><rights>2019 Pan “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. 2019</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c505t-8e8fe074cf282c340aca196b9c4672c5451a3d72aa861106e9343114486227703</citedby><cites>FETCH-LOGICAL-c505t-8e8fe074cf282c340aca196b9c4672c5451a3d72aa861106e9343114486227703</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/PMC6724691/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6724691/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,729,782,786,887,27931,27932,53798,53800</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30943117$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Martin, Thomas F. J.</contributor><creatorcontrib>Pan, Xiang</creatorcontrib><creatorcontrib>Meriin, Anatoli</creatorcontrib><creatorcontrib>Huang, Guanrong</creatorcontrib><creatorcontrib>Kandror, Konstantin V</creatorcontrib><title>Insulin-responsive amino peptidase follows the Glut4 pathway but is dispensable for the formation and translocation of insulin-responsive vesicles</title><title>Molecular biology of the cell</title><addtitle>Mol Biol Cell</addtitle><description>In fat and skeletal muscle cells, insulin-responsive amino peptidase (IRAP) along with glucose transporter 4 (Glut4) and sortilin, represents a major component protein of the insulin-responsive vesicles (IRVs). Here, we show that IRAP, similar to Glut4 and sortilin, is retrieved from endosomes to the
-Golgi network by retromer. Unlike Glut4, retrograde transport of IRAP does not require sortilin, as retromer can directly bind to the cytoplasmic tail of IRAP. Ablation of IRAP in 3T3-L1 adipocytes shifts the endosomal pool of Glut4 to more acidic endosomes, but does not affect IRV targeting, stability, and insulin responsiveness of Glut4.</description><subject>3T3-L1 Cells</subject><subject>Adipocytes - drug effects</subject><subject>Adipocytes - metabolism</subject><subject>Animals</subject><subject>Cell Differentiation</subject><subject>Cystinyl Aminopeptidase - metabolism</subject><subject>Glucose - metabolism</subject><subject>Glucose Transporter Type 4 - metabolism</subject><subject>Insulin - pharmacology</subject><subject>Mice</subject><subject>Transport Vesicles - drug effects</subject><subject>Transport Vesicles - metabolism</subject><subject>Vesicular Transport Proteins - metabolism</subject><issn>1059-1524</issn><issn>1939-4586</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNplkc1uFTEMhSMEoqWwZoeyZDNtnGR-skFCVSmVKrGBdZTJeLhBmWQYz9yqr9EnJpdbKhArW_bnY1uHsbcgzkEYuJh6f47QVSAr0Rr5jJ2CUabSddc8L7moTQW11CfsFdEPIUDrpn3JTpQwWgG0p-zhJtEWQ6oWpDknCnvkbgop8xnnNQyOkI85xnxHfN0hv47bqvns1t2du-f9tvJAfAg0YyLXxwO8_AZLnNwacuIuDXxdXKKY_bGSRx7-X7tHCj4ivWYvRhcJ3zzGM_bt09XXy8_V7Zfrm8uPt5WvRb1WHXYjilb7UXbSKy2cd2Ca3vjyo_S1rsGpoZXOdQ2AaNCow89ad42UbSvUGftw1J23fsLBYypXRjsvYXLLvc0u2H87Kezs97y3RV43BorA-0eBJf_ckFY7BfIYo0uYN7JSCgUKmtYU9OKI-iUTLTg-rQFhD07a4qS9gs6CtAcny8S7v6974v9Yp34BSvSebA</recordid><startdate>20190601</startdate><enddate>20190601</enddate><creator>Pan, Xiang</creator><creator>Meriin, Anatoli</creator><creator>Huang, Guanrong</creator><creator>Kandror, Konstantin V</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>20190601</creationdate><title>Insulin-responsive amino peptidase follows the Glut4 pathway but is dispensable for the formation and translocation of insulin-responsive vesicles</title><author>Pan, Xiang ; Meriin, Anatoli ; Huang, Guanrong ; Kandror, Konstantin V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-8e8fe074cf282c340aca196b9c4672c5451a3d72aa861106e9343114486227703</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>3T3-L1 Cells</topic><topic>Adipocytes - drug effects</topic><topic>Adipocytes - metabolism</topic><topic>Animals</topic><topic>Cell Differentiation</topic><topic>Cystinyl Aminopeptidase - metabolism</topic><topic>Glucose - metabolism</topic><topic>Glucose Transporter Type 4 - metabolism</topic><topic>Insulin - pharmacology</topic><topic>Mice</topic><topic>Transport Vesicles - drug effects</topic><topic>Transport Vesicles - metabolism</topic><topic>Vesicular Transport Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pan, Xiang</creatorcontrib><creatorcontrib>Meriin, Anatoli</creatorcontrib><creatorcontrib>Huang, Guanrong</creatorcontrib><creatorcontrib>Kandror, Konstantin V</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>Pan, Xiang</au><au>Meriin, Anatoli</au><au>Huang, Guanrong</au><au>Kandror, Konstantin V</au><au>Martin, Thomas F. J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Insulin-responsive amino peptidase follows the Glut4 pathway but is dispensable for the formation and translocation of insulin-responsive vesicles</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2019-06-01</date><risdate>2019</risdate><volume>30</volume><issue>12</issue><spage>1536</spage><epage>1543</epage><pages>1536-1543</pages><issn>1059-1524</issn><eissn>1939-4586</eissn><abstract>In fat and skeletal muscle cells, insulin-responsive amino peptidase (IRAP) along with glucose transporter 4 (Glut4) and sortilin, represents a major component protein of the insulin-responsive vesicles (IRVs). Here, we show that IRAP, similar to Glut4 and sortilin, is retrieved from endosomes to the
-Golgi network by retromer. Unlike Glut4, retrograde transport of IRAP does not require sortilin, as retromer can directly bind to the cytoplasmic tail of IRAP. Ablation of IRAP in 3T3-L1 adipocytes shifts the endosomal pool of Glut4 to more acidic endosomes, but does not affect IRV targeting, stability, and insulin responsiveness of Glut4.</abstract><cop>United States</cop><pub>The American Society for Cell Biology</pub><pmid>30943117</pmid><doi>10.1091/mbc.e18-12-0792</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular biology of the cell, 2019-06, Vol.30 (12), p.1536-1543 |
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| source | MEDLINE; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | 3T3-L1 Cells Adipocytes - drug effects Adipocytes - metabolism Animals Cell Differentiation Cystinyl Aminopeptidase - metabolism Glucose - metabolism Glucose Transporter Type 4 - metabolism Insulin - pharmacology Mice Transport Vesicles - drug effects Transport Vesicles - metabolism Vesicular Transport Proteins - metabolism |
| title | Insulin-responsive amino peptidase follows the Glut4 pathway but is dispensable for the formation and translocation of insulin-responsive vesicles |
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