Phosphorylation of Rab11-FIP2 regulates polarity in MDCK cells
The Rab11 effector Rab11-family interacting protein 2 (Rab11-FIP2) regulates transcytosis through its interactions with Rab11a and myosin Vb. Previous studies implicated Rab11-FIP2 in the establishment of polarity in Madin-Darby canine kidney (MDCK) cells through phosphorylation of Ser-227 by MARK2....
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| Veröffentlicht in: | Molecular biology of the cell 2012-06, Vol.23 (12), p.2302-2318 |
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| container_title | Molecular biology of the cell |
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| creator | Lapierre, Lynne A Avant, Kenya M Caldwell, Cathy M Oztan, Asli Apodaca, Gerard Knowles, Byron C Roland, Joseph T Ducharme, Nicole A Goldenring, James R |
| description | The Rab11 effector Rab11-family interacting protein 2 (Rab11-FIP2) regulates transcytosis through its interactions with Rab11a and myosin Vb. Previous studies implicated Rab11-FIP2 in the establishment of polarity in Madin-Darby canine kidney (MDCK) cells through phosphorylation of Ser-227 by MARK2. Here we examine the dynamic role of Rab11-FIP2 phosphorylation on MDCK cell polarity. Endogenous Rab11-FIP2 phosphorylated on Ser-227 coalesces on vesicular plaques during the reestablishment of polarity after either monolayer wounding or calcium switch. Whereas expression of the nonphosphorylatable Rab11-FIP2(S227A) elicits a loss in lumen formation in MDCK cell cysts grown in Matrigel, the putative pseudophosphorylated Rab11-FIP2(S227E) mutant induces the formation of cysts with multiple lumens. On permeable filters, Rab11-FIP2(S227E)-expressing cells exhibit alterations in the composition of both the adherens and tight junctions. At the adherens junction, p120 catenin and K-cadherin are retained, whereas the majority of the E-cadherin is lost. Although ZO-1 is retained at the tight junction, occludin is lost and the claudin composition is altered. Of interest, the effects of Rab11-FIP2 on cellular polarity did not involve myosin Vb or Rab11a. These results indicate that Ser-227 phosphorylation of Rab11-FIP2 regulates the composition of both adherens and tight junctions and is intimately involved in the regulation of polarity in epithelial cells. |
| doi_str_mv | 10.1091/mbc.E11-08-0681 |
| format | Article |
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Previous studies implicated Rab11-FIP2 in the establishment of polarity in Madin-Darby canine kidney (MDCK) cells through phosphorylation of Ser-227 by MARK2. Here we examine the dynamic role of Rab11-FIP2 phosphorylation on MDCK cell polarity. Endogenous Rab11-FIP2 phosphorylated on Ser-227 coalesces on vesicular plaques during the reestablishment of polarity after either monolayer wounding or calcium switch. Whereas expression of the nonphosphorylatable Rab11-FIP2(S227A) elicits a loss in lumen formation in MDCK cell cysts grown in Matrigel, the putative pseudophosphorylated Rab11-FIP2(S227E) mutant induces the formation of cysts with multiple lumens. On permeable filters, Rab11-FIP2(S227E)-expressing cells exhibit alterations in the composition of both the adherens and tight junctions. At the adherens junction, p120 catenin and K-cadherin are retained, whereas the majority of the E-cadherin is lost. Although ZO-1 is retained at the tight junction, occludin is lost and the claudin composition is altered. Of interest, the effects of Rab11-FIP2 on cellular polarity did not involve myosin Vb or Rab11a. These results indicate that Ser-227 phosphorylation of Rab11-FIP2 regulates the composition of both adherens and tight junctions and is intimately involved in the regulation of polarity in epithelial cells.</description><identifier>ISSN: 1059-1524</identifier><identifier>EISSN: 1939-4586</identifier><identifier>DOI: 10.1091/mbc.E11-08-0681</identifier><identifier>PMID: 22553350</identifier><language>eng</language><publisher>United States: The American Society for Cell Biology</publisher><subject>Adherens Junctions - metabolism ; Animals ; Blotting, Western ; Cadherins - genetics ; Cadherins - metabolism ; Catenins - genetics ; Catenins - metabolism ; Cell Line ; Cell Polarity ; Claudins - genetics ; Claudins - metabolism ; Dogs ; Epithelial Cells - metabolism ; Green Fluorescent Proteins - genetics ; Green Fluorescent Proteins - metabolism ; HEK293 Cells ; Humans ; Kidney - cytology ; Kidney - metabolism ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Microscopy, Confocal ; Mutation ; Occludin ; Phosphorylation ; Reverse Transcriptase Polymerase Chain Reaction ; Serine - genetics ; Serine - metabolism ; Tight Junctions - metabolism ; Vesicular Transport Proteins - genetics ; Vesicular Transport Proteins - metabolism</subject><ispartof>Molecular biology of the cell, 2012-06, Vol.23 (12), p.2302-2318</ispartof><rights>2012 Lapierre This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License ( ). 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-4da6a7b4d30061a3622bd85c3f645dc70d3edb9f715e42b0718166bb4a04a43b3</citedby><cites>FETCH-LOGICAL-c393t-4da6a7b4d30061a3622bd85c3f645dc70d3edb9f715e42b0718166bb4a04a43b3</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/PMC3374749/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3374749/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22553350$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Brennwald, Patrick</contributor><creatorcontrib>Lapierre, Lynne A</creatorcontrib><creatorcontrib>Avant, Kenya M</creatorcontrib><creatorcontrib>Caldwell, Cathy M</creatorcontrib><creatorcontrib>Oztan, Asli</creatorcontrib><creatorcontrib>Apodaca, Gerard</creatorcontrib><creatorcontrib>Knowles, Byron C</creatorcontrib><creatorcontrib>Roland, Joseph T</creatorcontrib><creatorcontrib>Ducharme, Nicole A</creatorcontrib><creatorcontrib>Goldenring, James R</creatorcontrib><title>Phosphorylation of Rab11-FIP2 regulates polarity in MDCK cells</title><title>Molecular biology of the cell</title><addtitle>Mol Biol Cell</addtitle><description>The Rab11 effector Rab11-family interacting protein 2 (Rab11-FIP2) regulates transcytosis through its interactions with Rab11a and myosin Vb. Previous studies implicated Rab11-FIP2 in the establishment of polarity in Madin-Darby canine kidney (MDCK) cells through phosphorylation of Ser-227 by MARK2. Here we examine the dynamic role of Rab11-FIP2 phosphorylation on MDCK cell polarity. Endogenous Rab11-FIP2 phosphorylated on Ser-227 coalesces on vesicular plaques during the reestablishment of polarity after either monolayer wounding or calcium switch. Whereas expression of the nonphosphorylatable Rab11-FIP2(S227A) elicits a loss in lumen formation in MDCK cell cysts grown in Matrigel, the putative pseudophosphorylated Rab11-FIP2(S227E) mutant induces the formation of cysts with multiple lumens. On permeable filters, Rab11-FIP2(S227E)-expressing cells exhibit alterations in the composition of both the adherens and tight junctions. At the adherens junction, p120 catenin and K-cadherin are retained, whereas the majority of the E-cadherin is lost. Although ZO-1 is retained at the tight junction, occludin is lost and the claudin composition is altered. Of interest, the effects of Rab11-FIP2 on cellular polarity did not involve myosin Vb or Rab11a. These results indicate that Ser-227 phosphorylation of Rab11-FIP2 regulates the composition of both adherens and tight junctions and is intimately involved in the regulation of polarity in epithelial cells.</description><subject>Adherens Junctions - metabolism</subject><subject>Animals</subject><subject>Blotting, Western</subject><subject>Cadherins - genetics</subject><subject>Cadherins - metabolism</subject><subject>Catenins - genetics</subject><subject>Catenins - metabolism</subject><subject>Cell Line</subject><subject>Cell Polarity</subject><subject>Claudins - genetics</subject><subject>Claudins - metabolism</subject><subject>Dogs</subject><subject>Epithelial Cells - metabolism</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Kidney - cytology</subject><subject>Kidney - metabolism</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Microscopy, Confocal</subject><subject>Mutation</subject><subject>Occludin</subject><subject>Phosphorylation</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Serine - genetics</subject><subject>Serine - metabolism</subject><subject>Tight Junctions - metabolism</subject><subject>Vesicular Transport Proteins - genetics</subject><subject>Vesicular Transport Proteins - metabolism</subject><issn>1059-1524</issn><issn>1939-4586</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkM1Lw0AQxRdRbP04e5McvaTd2a8kl4LUVosVi-h52U02bSTJxt1E6H9vSmvR0wy8N7-ZeQjdAB4BTmBc6XQ0AwhxHGIRwwkaQkKTkPFYnPY95kkInLABuvD-E2NgTETnaEAI55RyPEST1cb6ZmPdtlRtYevA5sGb0j1yvliRwJl11wvGB40tlSvabVDUwcvD9DlITVn6K3SWq9Kb60O9RB_z2fv0KVy-Pi6m98swpQltQ5YpoSLNMoqxAEUFITqLeUpzwXiWRjijJtNJHgE3jGgcQQxCaM0UZopRTS_RZM9tOl2ZLDV161QpG1dUym2lVYX8r9TFRq7tt6Q0YhFLesDdAeDsV2d8K6vC715QtbGdl4ApBc4SRnrreG9NnfXemfy4BrDcpS771KUBkDiWu9T7idu_1x39vzHTH8rffXk</recordid><startdate>20120615</startdate><enddate>20120615</enddate><creator>Lapierre, Lynne A</creator><creator>Avant, Kenya M</creator><creator>Caldwell, Cathy M</creator><creator>Oztan, Asli</creator><creator>Apodaca, Gerard</creator><creator>Knowles, Byron C</creator><creator>Roland, Joseph T</creator><creator>Ducharme, Nicole A</creator><creator>Goldenring, James 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>20120615</creationdate><title>Phosphorylation of Rab11-FIP2 regulates polarity in MDCK cells</title><author>Lapierre, Lynne A ; Avant, Kenya M ; Caldwell, Cathy M ; Oztan, Asli ; Apodaca, Gerard ; Knowles, Byron C ; Roland, Joseph T ; Ducharme, Nicole A ; Goldenring, James R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-4da6a7b4d30061a3622bd85c3f645dc70d3edb9f715e42b0718166bb4a04a43b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Adherens Junctions - metabolism</topic><topic>Animals</topic><topic>Blotting, Western</topic><topic>Cadherins - genetics</topic><topic>Cadherins - metabolism</topic><topic>Catenins - genetics</topic><topic>Catenins - metabolism</topic><topic>Cell Line</topic><topic>Cell Polarity</topic><topic>Claudins - genetics</topic><topic>Claudins - metabolism</topic><topic>Dogs</topic><topic>Epithelial Cells - metabolism</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Green Fluorescent Proteins - metabolism</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Kidney - cytology</topic><topic>Kidney - metabolism</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Microscopy, Confocal</topic><topic>Mutation</topic><topic>Occludin</topic><topic>Phosphorylation</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Serine - genetics</topic><topic>Serine - metabolism</topic><topic>Tight Junctions - metabolism</topic><topic>Vesicular Transport Proteins - genetics</topic><topic>Vesicular Transport Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lapierre, Lynne A</creatorcontrib><creatorcontrib>Avant, Kenya M</creatorcontrib><creatorcontrib>Caldwell, Cathy M</creatorcontrib><creatorcontrib>Oztan, Asli</creatorcontrib><creatorcontrib>Apodaca, Gerard</creatorcontrib><creatorcontrib>Knowles, Byron C</creatorcontrib><creatorcontrib>Roland, Joseph T</creatorcontrib><creatorcontrib>Ducharme, Nicole A</creatorcontrib><creatorcontrib>Goldenring, James 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>Lapierre, Lynne A</au><au>Avant, Kenya M</au><au>Caldwell, Cathy M</au><au>Oztan, Asli</au><au>Apodaca, Gerard</au><au>Knowles, Byron C</au><au>Roland, Joseph T</au><au>Ducharme, Nicole A</au><au>Goldenring, James R</au><au>Brennwald, Patrick</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of Rab11-FIP2 regulates polarity in MDCK cells</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2012-06-15</date><risdate>2012</risdate><volume>23</volume><issue>12</issue><spage>2302</spage><epage>2318</epage><pages>2302-2318</pages><issn>1059-1524</issn><eissn>1939-4586</eissn><abstract>The Rab11 effector Rab11-family interacting protein 2 (Rab11-FIP2) regulates transcytosis through its interactions with Rab11a and myosin Vb. Previous studies implicated Rab11-FIP2 in the establishment of polarity in Madin-Darby canine kidney (MDCK) cells through phosphorylation of Ser-227 by MARK2. Here we examine the dynamic role of Rab11-FIP2 phosphorylation on MDCK cell polarity. Endogenous Rab11-FIP2 phosphorylated on Ser-227 coalesces on vesicular plaques during the reestablishment of polarity after either monolayer wounding or calcium switch. Whereas expression of the nonphosphorylatable Rab11-FIP2(S227A) elicits a loss in lumen formation in MDCK cell cysts grown in Matrigel, the putative pseudophosphorylated Rab11-FIP2(S227E) mutant induces the formation of cysts with multiple lumens. On permeable filters, Rab11-FIP2(S227E)-expressing cells exhibit alterations in the composition of both the adherens and tight junctions. At the adherens junction, p120 catenin and K-cadherin are retained, whereas the majority of the E-cadherin is lost. Although ZO-1 is retained at the tight junction, occludin is lost and the claudin composition is altered. Of interest, the effects of Rab11-FIP2 on cellular polarity did not involve myosin Vb or Rab11a. These results indicate that Ser-227 phosphorylation of Rab11-FIP2 regulates the composition of both adherens and tight junctions and is intimately involved in the regulation of polarity in epithelial cells.</abstract><cop>United States</cop><pub>The American Society for Cell Biology</pub><pmid>22553350</pmid><doi>10.1091/mbc.E11-08-0681</doi><tpages>17</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adherens Junctions - metabolism Animals Blotting, Western Cadherins - genetics Cadherins - metabolism Catenins - genetics Catenins - metabolism Cell Line Cell Polarity Claudins - genetics Claudins - metabolism Dogs Epithelial Cells - metabolism Green Fluorescent Proteins - genetics Green Fluorescent Proteins - metabolism HEK293 Cells Humans Kidney - cytology Kidney - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Microscopy, Confocal Mutation Occludin Phosphorylation Reverse Transcriptase Polymerase Chain Reaction Serine - genetics Serine - metabolism Tight Junctions - metabolism Vesicular Transport Proteins - genetics Vesicular Transport Proteins - metabolism |
| title | Phosphorylation of Rab11-FIP2 regulates polarity in MDCK cells |
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