Arf6 regulates AP-1B-dependent sorting in polarized epithelial cells
The epithelial cell-specific clathrin adaptor complex AP-1B facilitates the sorting of various transmembrane proteins from recycling endosomes (REs) to the basolateral plasma membrane. Despite AP-1B's clear importance in polarized epithelial cells, we still do not fully understand how AP-1B orc...
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| Veröffentlicht in: | The Journal of cell biology 2011-09, Vol.194 (6), p.873-887 |
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| creator | Shteyn, Elina Pigati, Lucy Fölsch, Heike |
| description | The epithelial cell-specific clathrin adaptor complex AP-1B facilitates the sorting of various transmembrane proteins from recycling endosomes (REs) to the basolateral plasma membrane. Despite AP-1B's clear importance in polarized epithelial cells, we still do not fully understand how AP-1B orchestrates basolateral targeting. Here we identify the ADP-ribosylation factor 6 (Arf6) as an important regulator of AP-1B. We show that activated Arf6 pulled down AP-1B in vitro. Furthermore, interfering with Arf6 function through overexpression of dominant-active Arf6Q67L or dominant-negative Arf6D125N, as well as depletion of Arf6 with short hairpin RNA (shRNA), led to apical missorting of AP-1B-dependent cargos. In agreement with these data, we found that Arf6 colocalized with AP-1B and transferrin receptor (TfnR) in REs. In addition, we observed specific recruitment of AP-1B into Arf6-induced membrane ruffles in nonpolarized cells. We conclude that activated Arf6 directs membrane recruitment of AP-1B, thus regulating AP-1B's functions in polarized epithelial cells. |
| doi_str_mv | 10.1083/jcb.201106010 |
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Despite AP-1B's clear importance in polarized epithelial cells, we still do not fully understand how AP-1B orchestrates basolateral targeting. Here we identify the ADP-ribosylation factor 6 (Arf6) as an important regulator of AP-1B. We show that activated Arf6 pulled down AP-1B in vitro. Furthermore, interfering with Arf6 function through overexpression of dominant-active Arf6Q67L or dominant-negative Arf6D125N, as well as depletion of Arf6 with short hairpin RNA (shRNA), led to apical missorting of AP-1B-dependent cargos. In agreement with these data, we found that Arf6 colocalized with AP-1B and transferrin receptor (TfnR) in REs. In addition, we observed specific recruitment of AP-1B into Arf6-induced membrane ruffles in nonpolarized cells. We conclude that activated Arf6 directs membrane recruitment of AP-1B, thus regulating AP-1B's functions in polarized epithelial cells.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.201106010</identifier><identifier>PMID: 21911479</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Adaptor Protein Complex 1 - genetics ; Adaptor Protein Complex 1 - metabolism ; ADP-Ribosylation Factor 6 ; ADP-Ribosylation Factors - genetics ; ADP-Ribosylation Factors - metabolism ; Animals ; Cell Polarity - physiology ; Cells ; Cells, Cultured ; Dogs ; Epithelial Cells - cytology ; Epithelial Cells - metabolism ; Fluorescent Antibody Technique ; HEK293 Cells ; Humans ; Membranes ; Mice ; Plasma ; Proteins ; Rats ; Receptors, Transferrin - genetics ; Receptors, Transferrin - metabolism ; Ribonucleic acid ; RNA ; RNA, Small Interfering - genetics ; RNA, Small Interfering - metabolism ; Swine</subject><ispartof>The Journal of cell biology, 2011-09, Vol.194 (6), p.873-887</ispartof><rights>Copyright Rockefeller University Press Sep 19, 2011</rights><rights>2011 Shteyn et al. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c479t-201e7132c73505e8f078ca1a315408b5f79806bafc6bfe90f7abf44773ee05593</citedby><cites>FETCH-LOGICAL-c479t-201e7132c73505e8f078ca1a315408b5f79806bafc6bfe90f7abf44773ee05593</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21911479$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shteyn, Elina</creatorcontrib><creatorcontrib>Pigati, Lucy</creatorcontrib><creatorcontrib>Fölsch, Heike</creatorcontrib><title>Arf6 regulates AP-1B-dependent sorting in polarized epithelial cells</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>The epithelial cell-specific clathrin adaptor complex AP-1B facilitates the sorting of various transmembrane proteins from recycling endosomes (REs) to the basolateral plasma membrane. Despite AP-1B's clear importance in polarized epithelial cells, we still do not fully understand how AP-1B orchestrates basolateral targeting. Here we identify the ADP-ribosylation factor 6 (Arf6) as an important regulator of AP-1B. We show that activated Arf6 pulled down AP-1B in vitro. Furthermore, interfering with Arf6 function through overexpression of dominant-active Arf6Q67L or dominant-negative Arf6D125N, as well as depletion of Arf6 with short hairpin RNA (shRNA), led to apical missorting of AP-1B-dependent cargos. In agreement with these data, we found that Arf6 colocalized with AP-1B and transferrin receptor (TfnR) in REs. In addition, we observed specific recruitment of AP-1B into Arf6-induced membrane ruffles in nonpolarized cells. We conclude that activated Arf6 directs membrane recruitment of AP-1B, thus regulating AP-1B's functions in polarized epithelial cells.</description><subject>Adaptor Protein Complex 1 - genetics</subject><subject>Adaptor Protein Complex 1 - metabolism</subject><subject>ADP-Ribosylation Factor 6</subject><subject>ADP-Ribosylation Factors - genetics</subject><subject>ADP-Ribosylation Factors - metabolism</subject><subject>Animals</subject><subject>Cell Polarity - physiology</subject><subject>Cells</subject><subject>Cells, Cultured</subject><subject>Dogs</subject><subject>Epithelial Cells - cytology</subject><subject>Epithelial Cells - metabolism</subject><subject>Fluorescent Antibody Technique</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Membranes</subject><subject>Mice</subject><subject>Plasma</subject><subject>Proteins</subject><subject>Rats</subject><subject>Receptors, Transferrin - genetics</subject><subject>Receptors, Transferrin - metabolism</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA, Small Interfering - genetics</subject><subject>RNA, Small Interfering - metabolism</subject><subject>Swine</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkT1PwzAQhi0EouVjZEURC1PKOY5jZ0Eq5VOqBAPMlpOcW1dpEuwECX49iVoqYLrhHr33nF5CzihMKEh2tcqzSQSUQgIU9siY8hhCSWPYJ2OAiIYpj_iIHHm_AoBYxOyQjCKaUhqLdExup84kgcNFV-oWfTB9CelNWGCDVYFVG_jatbZaBLYKmrrUzn5hEWBj2yWWVpdBjmXpT8iB0aXH0-08Jm_3d6-zx3D-_PA0m87DvL_Vhr0mCsqiXDAOHKUBIXNNNRucZcaNSCUkmTZ5khlMwQidmTgWgiEC5yk7Jteb3KbL1ljkvaDTpWqcXWv3qWpt1d9NZZdqUX8oFoGIUtoHXG4DXP3eoW_V2vrhBV1h3XklUxZJliSyJy_-kau6c1X_3QCJmEs2-IQbKHe19w7NToWCGtpRfTtq107Pn__239E_dbBve5iKAQ</recordid><startdate>20110919</startdate><enddate>20110919</enddate><creator>Shteyn, Elina</creator><creator>Pigati, Lucy</creator><creator>Fölsch, Heike</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110919</creationdate><title>Arf6 regulates AP-1B-dependent sorting in polarized epithelial cells</title><author>Shteyn, Elina ; Pigati, Lucy ; Fölsch, Heike</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c479t-201e7132c73505e8f078ca1a315408b5f79806bafc6bfe90f7abf44773ee05593</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Adaptor Protein Complex 1 - genetics</topic><topic>Adaptor Protein Complex 1 - metabolism</topic><topic>ADP-Ribosylation Factor 6</topic><topic>ADP-Ribosylation Factors - genetics</topic><topic>ADP-Ribosylation Factors - metabolism</topic><topic>Animals</topic><topic>Cell Polarity - physiology</topic><topic>Cells</topic><topic>Cells, Cultured</topic><topic>Dogs</topic><topic>Epithelial Cells - cytology</topic><topic>Epithelial Cells - metabolism</topic><topic>Fluorescent Antibody Technique</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Membranes</topic><topic>Mice</topic><topic>Plasma</topic><topic>Proteins</topic><topic>Rats</topic><topic>Receptors, Transferrin - genetics</topic><topic>Receptors, Transferrin - metabolism</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>RNA, Small Interfering - genetics</topic><topic>RNA, Small Interfering - metabolism</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shteyn, Elina</creatorcontrib><creatorcontrib>Pigati, Lucy</creatorcontrib><creatorcontrib>Fölsch, Heike</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shteyn, Elina</au><au>Pigati, Lucy</au><au>Fölsch, Heike</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Arf6 regulates AP-1B-dependent sorting in polarized epithelial cells</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>2011-09-19</date><risdate>2011</risdate><volume>194</volume><issue>6</issue><spage>873</spage><epage>887</epage><pages>873-887</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>The epithelial cell-specific clathrin adaptor complex AP-1B facilitates the sorting of various transmembrane proteins from recycling endosomes (REs) to the basolateral plasma membrane. Despite AP-1B's clear importance in polarized epithelial cells, we still do not fully understand how AP-1B orchestrates basolateral targeting. Here we identify the ADP-ribosylation factor 6 (Arf6) as an important regulator of AP-1B. We show that activated Arf6 pulled down AP-1B in vitro. Furthermore, interfering with Arf6 function through overexpression of dominant-active Arf6Q67L or dominant-negative Arf6D125N, as well as depletion of Arf6 with short hairpin RNA (shRNA), led to apical missorting of AP-1B-dependent cargos. In agreement with these data, we found that Arf6 colocalized with AP-1B and transferrin receptor (TfnR) in REs. In addition, we observed specific recruitment of AP-1B into Arf6-induced membrane ruffles in nonpolarized cells. 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| subjects | Adaptor Protein Complex 1 - genetics Adaptor Protein Complex 1 - metabolism ADP-Ribosylation Factor 6 ADP-Ribosylation Factors - genetics ADP-Ribosylation Factors - metabolism Animals Cell Polarity - physiology Cells Cells, Cultured Dogs Epithelial Cells - cytology Epithelial Cells - metabolism Fluorescent Antibody Technique HEK293 Cells Humans Membranes Mice Plasma Proteins Rats Receptors, Transferrin - genetics Receptors, Transferrin - metabolism Ribonucleic acid RNA RNA, Small Interfering - genetics RNA, Small Interfering - metabolism Swine |
| title | Arf6 regulates AP-1B-dependent sorting in polarized epithelial cells |
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