Trafficking of the IKs‐Complex in MDCK Cells: Site of Subunit Assembly and Determinants of Polarized Localization
The voltage‐gated potassium channel KV7.1 is regulated by non‐pore forming regulatory KCNE β‐subunits. Together with KCNE1, it forms the slowly activating delayed rectifier potassium current IKs. However, where the subunits assemble and which of the subunits determines localization of the IKs‐comple...
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| Veröffentlicht in: | Traffic (Copenhagen, Denmark) Denmark), 2013-04, Vol.14 (4), p.399-411 |
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| creator | David, Jens‐Peter Andersen, Martin N. Olesen, Søren‐Peter Rasmussen, Hanne B. Schmitt, Nicole |
| description | The voltage‐gated potassium channel KV7.1 is regulated by non‐pore forming regulatory KCNE β‐subunits. Together with KCNE1, it forms the slowly activating delayed rectifier potassium current IKs. However, where the subunits assemble and which of the subunits determines localization of the IKs‐complex has not been unequivocally resolved yet. We employed trafficking‐deficient KV7.1 and KCNE1 mutants to investigate IKs trafficking using the polarized Madin‐Darby Canine Kidney cell line. We find that the assembly happens early in the secretory pathway but provide three lines of evidence that it takes place in a post‐endoplasmic reticulum compartment. We demonstrate that KV7.1 targets the IKs‐complex to the basolateral membrane, but that KCNE1 can redirect the complex to the apical membrane upon mutation of critical KV7.1 basolateral targeting signals. Our data provide a possible explanation to the fact that KV7.1 can be localized apically or basolaterally in different epithelial tissues and offer a solution to divergent literature results regarding the effect of KCNE subunits on the subcellular localization of KV7.1/KCNE complexes. |
| doi_str_mv | 10.1111/tra.12042 |
| format | Article |
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Together with KCNE1, it forms the slowly activating delayed rectifier potassium current IKs. However, where the subunits assemble and which of the subunits determines localization of the IKs‐complex has not been unequivocally resolved yet. We employed trafficking‐deficient KV7.1 and KCNE1 mutants to investigate IKs trafficking using the polarized Madin‐Darby Canine Kidney cell line. We find that the assembly happens early in the secretory pathway but provide three lines of evidence that it takes place in a post‐endoplasmic reticulum compartment. We demonstrate that KV7.1 targets the IKs‐complex to the basolateral membrane, but that KCNE1 can redirect the complex to the apical membrane upon mutation of critical KV7.1 basolateral targeting signals. Our data provide a possible explanation to the fact that KV7.1 can be localized apically or basolaterally in different epithelial tissues and offer a solution to divergent literature results regarding the effect of KCNE subunits on the subcellular localization of KV7.1/KCNE complexes.</description><identifier>ISSN: 1398-9219</identifier><identifier>EISSN: 1600-0854</identifier><identifier>DOI: 10.1111/tra.12042</identifier><identifier>PMID: 23324056</identifier><language>eng</language><publisher>Former Munksgaard: John Wiley & Sons A/S</publisher><subject>Animals ; Cell Membrane - metabolism ; Cells ; Dogs ; Endoplasmic Reticulum - metabolism ; Golgi Apparatus - metabolism ; KCNE1 ; KCNQ1 ; KCNQ1 Potassium Channel - chemistry ; KCNQ1 Potassium Channel - genetics ; KCNQ1 Potassium Channel - metabolism ; LQT ; Madin Darby Canine Kidney Cells ; MDCK ; Mutation, Missense ; Potassium Channels, Voltage-Gated - chemistry ; Potassium Channels, Voltage-Gated - genetics ; Potassium Channels, Voltage-Gated - metabolism ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Protein Sorting Signals - genetics ; Protein Subunits - genetics ; Protein Subunits - metabolism ; Protein Transport ; Proteins ; Rab1 ; Secretory Pathway ; trafficking</subject><ispartof>Traffic (Copenhagen, Denmark), 2013-04, Vol.14 (4), p.399-411</ispartof><rights>2013 John Wiley & Sons A/S</rights><rights>2013 John Wiley & Sons A/S.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Ftra.12042$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Ftra.12042$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,778,782,1414,1430,27913,27914,45563,45564,46398,46822</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23324056$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>David, Jens‐Peter</creatorcontrib><creatorcontrib>Andersen, Martin N.</creatorcontrib><creatorcontrib>Olesen, Søren‐Peter</creatorcontrib><creatorcontrib>Rasmussen, Hanne B.</creatorcontrib><creatorcontrib>Schmitt, Nicole</creatorcontrib><title>Trafficking of the IKs‐Complex in MDCK Cells: Site of Subunit Assembly and Determinants of Polarized Localization</title><title>Traffic (Copenhagen, Denmark)</title><addtitle>Traffic</addtitle><description>The voltage‐gated potassium channel KV7.1 is regulated by non‐pore forming regulatory KCNE β‐subunits. Together with KCNE1, it forms the slowly activating delayed rectifier potassium current IKs. However, where the subunits assemble and which of the subunits determines localization of the IKs‐complex has not been unequivocally resolved yet. We employed trafficking‐deficient KV7.1 and KCNE1 mutants to investigate IKs trafficking using the polarized Madin‐Darby Canine Kidney cell line. We find that the assembly happens early in the secretory pathway but provide three lines of evidence that it takes place in a post‐endoplasmic reticulum compartment. We demonstrate that KV7.1 targets the IKs‐complex to the basolateral membrane, but that KCNE1 can redirect the complex to the apical membrane upon mutation of critical KV7.1 basolateral targeting signals. Our data provide a possible explanation to the fact that KV7.1 can be localized apically or basolaterally in different epithelial tissues and offer a solution to divergent literature results regarding the effect of KCNE subunits on the subcellular localization of KV7.1/KCNE complexes.</description><subject>Animals</subject><subject>Cell Membrane - metabolism</subject><subject>Cells</subject><subject>Dogs</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Golgi Apparatus - metabolism</subject><subject>KCNE1</subject><subject>KCNQ1</subject><subject>KCNQ1 Potassium Channel - chemistry</subject><subject>KCNQ1 Potassium Channel - genetics</subject><subject>KCNQ1 Potassium Channel - metabolism</subject><subject>LQT</subject><subject>Madin Darby Canine Kidney Cells</subject><subject>MDCK</subject><subject>Mutation, Missense</subject><subject>Potassium Channels, Voltage-Gated - chemistry</subject><subject>Potassium Channels, Voltage-Gated - genetics</subject><subject>Potassium Channels, Voltage-Gated - metabolism</subject><subject>Protein Interaction Domains and Motifs</subject><subject>Protein Multimerization</subject><subject>Protein Sorting Signals - genetics</subject><subject>Protein Subunits - genetics</subject><subject>Protein Subunits - metabolism</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>Rab1</subject><subject>Secretory Pathway</subject><subject>trafficking</subject><issn>1398-9219</issn><issn>1600-0854</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkUtOwzAQhi0EolBYcAFkiQ2btH7ESc2uSnlUFIGgrCPHscGQOCVOBO2KI3AEzsJROAmmFBbMYuaX5tNoZn4A9jDqYR_9phY9TFBI1sAWjhAK0ICF615TPgg4wbwDtp17QAgRFoaboEMoJSFi0RZop7XQ2shHY-9gpWFzr-D43H2-viVVOSvUCzQWXoySc5ioonBH8MY0yoMf7zdt1lrTwKFzqsyKORQ2hyPVqLo0VtjGLamrqhC1WagcTiopCrMQjansDtjQonBqd1W74PbkeJqcBZPL03EynAQzQjgJGFISCUqRFBHSeYx5nOVERlJwSTOkuNAxRRGVBGdCZ0zKjOhBTBjjlGmW0y44_Jk7q6unVrkmLY2T_hBhVdW6FFPMIkqpT11w8A99qNra-u2-qTjkEebEU_srqs1Klaez2pSinqe_D_VA_wd4NoWa__UxSr-dSr1T6dKpdHo9XAr6BQ4ah5o</recordid><startdate>201304</startdate><enddate>201304</enddate><creator>David, Jens‐Peter</creator><creator>Andersen, Martin N.</creator><creator>Olesen, Søren‐Peter</creator><creator>Rasmussen, Hanne B.</creator><creator>Schmitt, Nicole</creator><general>John Wiley & Sons A/S</general><general>Wiley Subscription Services, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QP</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>201304</creationdate><title>Trafficking of the IKs‐Complex in MDCK Cells: Site of Subunit Assembly and Determinants of Polarized Localization</title><author>David, Jens‐Peter ; Andersen, Martin N. ; Olesen, Søren‐Peter ; Rasmussen, Hanne B. ; Schmitt, Nicole</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p2292-50ec0a330ca60fd7197bd2c6ca9c3b0e9af73063c21bafb5ccb2f87255935f5d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Animals</topic><topic>Cell Membrane - metabolism</topic><topic>Cells</topic><topic>Dogs</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Golgi Apparatus - metabolism</topic><topic>KCNE1</topic><topic>KCNQ1</topic><topic>KCNQ1 Potassium Channel - chemistry</topic><topic>KCNQ1 Potassium Channel - genetics</topic><topic>KCNQ1 Potassium Channel - metabolism</topic><topic>LQT</topic><topic>Madin Darby Canine Kidney Cells</topic><topic>MDCK</topic><topic>Mutation, Missense</topic><topic>Potassium Channels, Voltage-Gated - chemistry</topic><topic>Potassium Channels, Voltage-Gated - genetics</topic><topic>Potassium Channels, Voltage-Gated - metabolism</topic><topic>Protein Interaction Domains and Motifs</topic><topic>Protein Multimerization</topic><topic>Protein Sorting Signals - genetics</topic><topic>Protein Subunits - genetics</topic><topic>Protein Subunits - metabolism</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>Rab1</topic><topic>Secretory Pathway</topic><topic>trafficking</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>David, Jens‐Peter</creatorcontrib><creatorcontrib>Andersen, Martin N.</creatorcontrib><creatorcontrib>Olesen, Søren‐Peter</creatorcontrib><creatorcontrib>Rasmussen, Hanne B.</creatorcontrib><creatorcontrib>Schmitt, Nicole</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Traffic (Copenhagen, Denmark)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>David, Jens‐Peter</au><au>Andersen, Martin N.</au><au>Olesen, Søren‐Peter</au><au>Rasmussen, Hanne B.</au><au>Schmitt, Nicole</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Trafficking of the IKs‐Complex in MDCK Cells: Site of Subunit Assembly and Determinants of Polarized Localization</atitle><jtitle>Traffic (Copenhagen, Denmark)</jtitle><addtitle>Traffic</addtitle><date>2013-04</date><risdate>2013</risdate><volume>14</volume><issue>4</issue><spage>399</spage><epage>411</epage><pages>399-411</pages><issn>1398-9219</issn><eissn>1600-0854</eissn><abstract>The voltage‐gated potassium channel KV7.1 is regulated by non‐pore forming regulatory KCNE β‐subunits. Together with KCNE1, it forms the slowly activating delayed rectifier potassium current IKs. However, where the subunits assemble and which of the subunits determines localization of the IKs‐complex has not been unequivocally resolved yet. We employed trafficking‐deficient KV7.1 and KCNE1 mutants to investigate IKs trafficking using the polarized Madin‐Darby Canine Kidney cell line. We find that the assembly happens early in the secretory pathway but provide three lines of evidence that it takes place in a post‐endoplasmic reticulum compartment. We demonstrate that KV7.1 targets the IKs‐complex to the basolateral membrane, but that KCNE1 can redirect the complex to the apical membrane upon mutation of critical KV7.1 basolateral targeting signals. Our data provide a possible explanation to the fact that KV7.1 can be localized apically or basolaterally in different epithelial tissues and offer a solution to divergent literature results regarding the effect of KCNE subunits on the subcellular localization of KV7.1/KCNE complexes.</abstract><cop>Former Munksgaard</cop><pub>John Wiley & Sons A/S</pub><pmid>23324056</pmid><doi>10.1111/tra.12042</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Cell Membrane - metabolism Cells Dogs Endoplasmic Reticulum - metabolism Golgi Apparatus - metabolism KCNE1 KCNQ1 KCNQ1 Potassium Channel - chemistry KCNQ1 Potassium Channel - genetics KCNQ1 Potassium Channel - metabolism LQT Madin Darby Canine Kidney Cells MDCK Mutation, Missense Potassium Channels, Voltage-Gated - chemistry Potassium Channels, Voltage-Gated - genetics Potassium Channels, Voltage-Gated - metabolism Protein Interaction Domains and Motifs Protein Multimerization Protein Sorting Signals - genetics Protein Subunits - genetics Protein Subunits - metabolism Protein Transport Proteins Rab1 Secretory Pathway trafficking |
| title | Trafficking of the IKs‐Complex in MDCK Cells: Site of Subunit Assembly and Determinants of Polarized Localization |
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