Rab14 Regulates Apical Targeting in Polarized Epithelial Cells
Epithelial cells display distinct apical and basolateral membrane domains, and maintenance of this asymmetry is essential to the function of epithelial tissues. Polarized delivery of apical and basolateral membrane proteins from the trans Golgi network (TGN) and/or endosomes to the correct domain re...
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| Veröffentlicht in: | Traffic (Copenhagen, Denmark) Denmark), 2008-07, Vol.9 (7), p.1218-1231 |
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| creator | Kitt, Khameeka N Hernández-Deviez, Delia Ballantyne, Sarah D Spiliotis, Elias T Casanova, James E Wilson, Jean M |
| description | Epithelial cells display distinct apical and basolateral membrane domains, and maintenance of this asymmetry is essential to the function of epithelial tissues. Polarized delivery of apical and basolateral membrane proteins from the trans Golgi network (TGN) and/or endosomes to the correct domain requires specific cytoplasmic machinery to control the sorting, budding and fission of vesicles. However, the molecular machinery that regulates polarized delivery of apical proteins remains poorly understood. In this study, we show that the small guanosine triphosphatase Rab14 is involved in the apical targeting pathway. Using yeast two-hybrid analysis and glutathione S-transferase pull down, we show that Rab14 interacts with apical membrane proteins and localizes to the TGN and apical endosomes. Overexpression of the GDP mutant form of Rab14 (S25N) induces an enlargement of the TGN and vesicle accumulation around Golgi membranes. Moreover, expression of Rab14-S25N results in mislocalization of the apical raft-associated protein vasoactive intestinal peptide/MAL to the basolateral domain but does not disrupt basolateral targeting or recycling. These data suggest that Rab14 specifically regulates delivery of cargo from the TGN to the apical domain. |
| doi_str_mv | 10.1111/j.1600-0854.2008.00752.x |
| format | Article |
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Polarized delivery of apical and basolateral membrane proteins from the trans Golgi network (TGN) and/or endosomes to the correct domain requires specific cytoplasmic machinery to control the sorting, budding and fission of vesicles. However, the molecular machinery that regulates polarized delivery of apical proteins remains poorly understood. In this study, we show that the small guanosine triphosphatase Rab14 is involved in the apical targeting pathway. Using yeast two-hybrid analysis and glutathione S-transferase pull down, we show that Rab14 interacts with apical membrane proteins and localizes to the TGN and apical endosomes. Overexpression of the GDP mutant form of Rab14 (S25N) induces an enlargement of the TGN and vesicle accumulation around Golgi membranes. Moreover, expression of Rab14-S25N results in mislocalization of the apical raft-associated protein vasoactive intestinal peptide/MAL to the basolateral domain but does not disrupt basolateral targeting or recycling. These data suggest that Rab14 specifically regulates delivery of cargo from the TGN to the apical domain.</description><identifier>ISSN: 1398-9219</identifier><identifier>EISSN: 1600-0854</identifier><identifier>DOI: 10.1111/j.1600-0854.2008.00752.x</identifier><identifier>PMID: 18429929</identifier><language>eng</language><publisher>Oxford, UK: Oxford, UK : Blackwell Publishing Ltd</publisher><subject>Animals ; apical targeting ; Cell Line ; Cytoplasm - metabolism ; Dogs ; Endosomes - metabolism ; epithelial cells ; Epithelial Cells - cytology ; Glutathione Transferase - metabolism ; Golgi Apparatus - metabolism ; GTP Phosphohydrolases - metabolism ; Mutation ; polarity ; Protein Transport ; rab GTP-Binding Proteins - metabolism ; rab GTP-Binding Proteins - physiology ; Rab14 ; Rats ; Two-Hybrid System Techniques</subject><ispartof>Traffic (Copenhagen, Denmark), 2008-07, Vol.9 (7), p.1218-1231</ispartof><rights>2008 The Authors Journal compilation © 2008 Blackwell Publishing Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5612-d015e3f5529dcd479353714399fbaa101d2e408b749938a79f71d6b4c17377893</citedby><cites>FETCH-LOGICAL-c5612-d015e3f5529dcd479353714399fbaa101d2e408b749938a79f71d6b4c17377893</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1600-0854.2008.00752.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1600-0854.2008.00752.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18429929$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kitt, Khameeka N</creatorcontrib><creatorcontrib>Hernández-Deviez, Delia</creatorcontrib><creatorcontrib>Ballantyne, Sarah D</creatorcontrib><creatorcontrib>Spiliotis, Elias T</creatorcontrib><creatorcontrib>Casanova, James E</creatorcontrib><creatorcontrib>Wilson, Jean M</creatorcontrib><title>Rab14 Regulates Apical Targeting in Polarized Epithelial Cells</title><title>Traffic (Copenhagen, Denmark)</title><addtitle>Traffic</addtitle><description>Epithelial cells display distinct apical and basolateral membrane domains, and maintenance of this asymmetry is essential to the function of epithelial tissues. Polarized delivery of apical and basolateral membrane proteins from the trans Golgi network (TGN) and/or endosomes to the correct domain requires specific cytoplasmic machinery to control the sorting, budding and fission of vesicles. However, the molecular machinery that regulates polarized delivery of apical proteins remains poorly understood. In this study, we show that the small guanosine triphosphatase Rab14 is involved in the apical targeting pathway. Using yeast two-hybrid analysis and glutathione S-transferase pull down, we show that Rab14 interacts with apical membrane proteins and localizes to the TGN and apical endosomes. Overexpression of the GDP mutant form of Rab14 (S25N) induces an enlargement of the TGN and vesicle accumulation around Golgi membranes. Moreover, expression of Rab14-S25N results in mislocalization of the apical raft-associated protein vasoactive intestinal peptide/MAL to the basolateral domain but does not disrupt basolateral targeting or recycling. These data suggest that Rab14 specifically regulates delivery of cargo from the TGN to the apical domain.</description><subject>Animals</subject><subject>apical targeting</subject><subject>Cell Line</subject><subject>Cytoplasm - metabolism</subject><subject>Dogs</subject><subject>Endosomes - metabolism</subject><subject>epithelial cells</subject><subject>Epithelial Cells - cytology</subject><subject>Glutathione Transferase - metabolism</subject><subject>Golgi Apparatus - metabolism</subject><subject>GTP Phosphohydrolases - metabolism</subject><subject>Mutation</subject><subject>polarity</subject><subject>Protein Transport</subject><subject>rab GTP-Binding Proteins - metabolism</subject><subject>rab GTP-Binding Proteins - physiology</subject><subject>Rab14</subject><subject>Rats</subject><subject>Two-Hybrid System Techniques</subject><issn>1398-9219</issn><issn>1600-0854</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkFtv1DAQhS1URC_wF2ie-pYwvsWxVFVarUpBqgRats8jJ3FSr7zJ1s6Wll-Pl10V-sa8zEhzzvH4IySjUNBUn1YFLQFyqKQoGEBVACjJiqc35ORlcZRmrqtcM6qPyWmMKwBgUoh35JhWgmnN9Am5Wpiaimxh-603k43ZbOMa47OlCb2d3NBnbsi-j94E98u22fXGTffWu6SYW-_je_K2Mz7aD4d-Ru4-Xy_nX_Lbbzdf57PbvJElZXkLVFreScl027RCaS65ooJr3dXGUKAtswKqWgmteWWU7hRty1o0VHGlKs3PyNU-d7Ot17Zt7DAF43ET3NqEZxyNw9ebwd1jPz4iU4qXpUoBF4eAMD5sbZxw7WKTvmAGO24jlponjkokYbUXNmGMMdju5REKuIOPK9wxxh1j3MHHP_DxKVk__nvkX-OBdhJc7gU_nbfP_x2My8UsDcl-vrd3ZkTTBxfx7gcDmi7XoLgU_DcFO5q-</recordid><startdate>200807</startdate><enddate>200807</enddate><creator>Kitt, Khameeka N</creator><creator>Hernández-Deviez, Delia</creator><creator>Ballantyne, Sarah D</creator><creator>Spiliotis, Elias T</creator><creator>Casanova, James E</creator><creator>Wilson, Jean M</creator><general>Oxford, UK : Blackwell Publishing Ltd</general><general>Blackwell Publishing Ltd</general><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>200807</creationdate><title>Rab14 Regulates Apical Targeting in Polarized Epithelial Cells</title><author>Kitt, Khameeka N ; Hernández-Deviez, Delia ; Ballantyne, Sarah D ; Spiliotis, Elias T ; Casanova, James E ; Wilson, Jean M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5612-d015e3f5529dcd479353714399fbaa101d2e408b749938a79f71d6b4c17377893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>apical targeting</topic><topic>Cell Line</topic><topic>Cytoplasm - metabolism</topic><topic>Dogs</topic><topic>Endosomes - metabolism</topic><topic>epithelial cells</topic><topic>Epithelial Cells - cytology</topic><topic>Glutathione Transferase - metabolism</topic><topic>Golgi Apparatus - metabolism</topic><topic>GTP Phosphohydrolases - metabolism</topic><topic>Mutation</topic><topic>polarity</topic><topic>Protein Transport</topic><topic>rab GTP-Binding Proteins - metabolism</topic><topic>rab GTP-Binding Proteins - physiology</topic><topic>Rab14</topic><topic>Rats</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kitt, Khameeka N</creatorcontrib><creatorcontrib>Hernández-Deviez, Delia</creatorcontrib><creatorcontrib>Ballantyne, Sarah D</creatorcontrib><creatorcontrib>Spiliotis, Elias T</creatorcontrib><creatorcontrib>Casanova, James E</creatorcontrib><creatorcontrib>Wilson, Jean M</creatorcontrib><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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Traffic (Copenhagen, Denmark)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kitt, Khameeka N</au><au>Hernández-Deviez, Delia</au><au>Ballantyne, Sarah D</au><au>Spiliotis, Elias T</au><au>Casanova, James E</au><au>Wilson, Jean M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Rab14 Regulates Apical Targeting in Polarized Epithelial Cells</atitle><jtitle>Traffic (Copenhagen, Denmark)</jtitle><addtitle>Traffic</addtitle><date>2008-07</date><risdate>2008</risdate><volume>9</volume><issue>7</issue><spage>1218</spage><epage>1231</epage><pages>1218-1231</pages><issn>1398-9219</issn><eissn>1600-0854</eissn><abstract>Epithelial cells display distinct apical and basolateral membrane domains, and maintenance of this asymmetry is essential to the function of epithelial tissues. Polarized delivery of apical and basolateral membrane proteins from the trans Golgi network (TGN) and/or endosomes to the correct domain requires specific cytoplasmic machinery to control the sorting, budding and fission of vesicles. However, the molecular machinery that regulates polarized delivery of apical proteins remains poorly understood. In this study, we show that the small guanosine triphosphatase Rab14 is involved in the apical targeting pathway. Using yeast two-hybrid analysis and glutathione S-transferase pull down, we show that Rab14 interacts with apical membrane proteins and localizes to the TGN and apical endosomes. Overexpression of the GDP mutant form of Rab14 (S25N) induces an enlargement of the TGN and vesicle accumulation around Golgi membranes. Moreover, expression of Rab14-S25N results in mislocalization of the apical raft-associated protein vasoactive intestinal peptide/MAL to the basolateral domain but does not disrupt basolateral targeting or recycling. 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| subjects | Animals apical targeting Cell Line Cytoplasm - metabolism Dogs Endosomes - metabolism epithelial cells Epithelial Cells - cytology Glutathione Transferase - metabolism Golgi Apparatus - metabolism GTP Phosphohydrolases - metabolism Mutation polarity Protein Transport rab GTP-Binding Proteins - metabolism rab GTP-Binding Proteins - physiology Rab14 Rats Two-Hybrid System Techniques |
| title | Rab14 Regulates Apical Targeting in Polarized Epithelial Cells |
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