Cell‐specific diversity in the expression and organization of cytoplasmic plaque proteins of apical junctions
Tight and adherens junctions play critical roles in the barrier, adhesion, and signaling functions of epithelial and endothelial cells. How the molecular organization of these junctions is tuned to the widely diverse physiological requirements of each tissue type is not well understood. Here, we add...
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| Veröffentlicht in: | Annals of the New York Academy of Sciences 2017-10, Vol.1405 (1), p.160-176 |
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| creator | Vasileva, Ekaterina Sluysmans, Sophie Bochaton‐Piallat, Marie‐Luce Citi, Sandra |
| description | Tight and adherens junctions play critical roles in the barrier, adhesion, and signaling functions of epithelial and endothelial cells. How the molecular organization of these junctions is tuned to the widely diverse physiological requirements of each tissue type is not well understood. Here, we address this question by examining the expression, localization, and interactions of major cytoplasmic plaque proteins of tight and adherens junctions in different cultured epithelial and endothelial cell lines. Immunoblotting and immunofluorescence analyses show that the expression profiles of cingulin, paracingulin, ZO‐1, ZO‐2, ZO‐3, PLEKHA7, afadin, PDZD11, p120‐catenin, and α‐catenin, as well as the transmembrane junctional proteins occludin, E‐cadherin, and VE‐cadherin, are significantly diverse when comparing kidney cells (MDCK, mCCD), keratinocytes (HaCaT), lung carcinoma (A427, A549), and endothelium‐derived cells (bEnd.3, meEC, H5V). Proximity ligation and co‐immunoprecipitation assays show that PLEKHA7 and PDZD11 are significantly more associated with the tight junction proteins cingulin and ZO‐1 in aortic endothelium–derived (meEC) cells but not kidney collecting duct epithelial (mCCD) cells. These results provide evidence that the cytoplasmic plaques of tight and adherens junctions are diverse in their composition and molecular architecture and establish a conceptual framework by which we can rationally address the mechanisms of tissue‐dependent junction physiology and signaling by cytoplasmic junctional proteins. |
| doi_str_mv | 10.1111/nyas.13391 |
| format | Article |
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How the molecular organization of these junctions is tuned to the widely diverse physiological requirements of each tissue type is not well understood. Here, we address this question by examining the expression, localization, and interactions of major cytoplasmic plaque proteins of tight and adherens junctions in different cultured epithelial and endothelial cell lines. Immunoblotting and immunofluorescence analyses show that the expression profiles of cingulin, paracingulin, ZO‐1, ZO‐2, ZO‐3, PLEKHA7, afadin, PDZD11, p120‐catenin, and α‐catenin, as well as the transmembrane junctional proteins occludin, E‐cadherin, and VE‐cadherin, are significantly diverse when comparing kidney cells (MDCK, mCCD), keratinocytes (HaCaT), lung carcinoma (A427, A549), and endothelium‐derived cells (bEnd.3, meEC, H5V). Proximity ligation and co‐immunoprecipitation assays show that PLEKHA7 and PDZD11 are significantly more associated with the tight junction proteins cingulin and ZO‐1 in aortic endothelium–derived (meEC) cells but not kidney collecting duct epithelial (mCCD) cells. These results provide evidence that the cytoplasmic plaques of tight and adherens junctions are diverse in their composition and molecular architecture and establish a conceptual framework by which we can rationally address the mechanisms of tissue‐dependent junction physiology and signaling by cytoplasmic junctional proteins.</description><identifier>ISSN: 0077-8923</identifier><identifier>EISSN: 1749-6632</identifier><identifier>DOI: 10.1111/nyas.13391</identifier><identifier>PMID: 28617990</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>adherens junction ; Adherens junctions ; Adherens Junctions - metabolism ; Animals ; Aorta ; Cadherins - metabolism ; Catenin ; Cell Line ; Collecting duct ; Cytoplasm - metabolism ; E-cadherin ; endothelia ; Endothelial cells ; Endothelium ; epithelia ; Epithelial Cells - metabolism ; Humans ; Immunoblotting ; Immunofluorescence ; Immunoprecipitation ; Keratinocytes ; Localization ; Lung carcinoma ; Membrane Proteins - metabolism ; Mice ; Plaques ; protein ; Proteins ; tight junction ; Tight Junction Proteins - metabolism ; Tight Junctions - metabolism ; Zonula occludens-1 protein</subject><ispartof>Annals of the New York Academy of Sciences, 2017-10, Vol.1405 (1), p.160-176</ispartof><rights>2017 New York Academy of Sciences.</rights><rights>2017 The New York Academy of Sciences</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4231-dadb0ef2ee1b755d71dc453f718313059216b81a9855ce8198cea261199892883</citedby><cites>FETCH-LOGICAL-c4231-dadb0ef2ee1b755d71dc453f718313059216b81a9855ce8198cea261199892883</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%2Fnyas.13391$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fnyas.13391$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28617990$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vasileva, Ekaterina</creatorcontrib><creatorcontrib>Sluysmans, Sophie</creatorcontrib><creatorcontrib>Bochaton‐Piallat, Marie‐Luce</creatorcontrib><creatorcontrib>Citi, Sandra</creatorcontrib><title>Cell‐specific diversity in the expression and organization of cytoplasmic plaque proteins of apical junctions</title><title>Annals of the New York Academy of Sciences</title><addtitle>Ann N Y Acad Sci</addtitle><description>Tight and adherens junctions play critical roles in the barrier, adhesion, and signaling functions of epithelial and endothelial cells. How the molecular organization of these junctions is tuned to the widely diverse physiological requirements of each tissue type is not well understood. Here, we address this question by examining the expression, localization, and interactions of major cytoplasmic plaque proteins of tight and adherens junctions in different cultured epithelial and endothelial cell lines. Immunoblotting and immunofluorescence analyses show that the expression profiles of cingulin, paracingulin, ZO‐1, ZO‐2, ZO‐3, PLEKHA7, afadin, PDZD11, p120‐catenin, and α‐catenin, as well as the transmembrane junctional proteins occludin, E‐cadherin, and VE‐cadherin, are significantly diverse when comparing kidney cells (MDCK, mCCD), keratinocytes (HaCaT), lung carcinoma (A427, A549), and endothelium‐derived cells (bEnd.3, meEC, H5V). Proximity ligation and co‐immunoprecipitation assays show that PLEKHA7 and PDZD11 are significantly more associated with the tight junction proteins cingulin and ZO‐1 in aortic endothelium–derived (meEC) cells but not kidney collecting duct epithelial (mCCD) cells. These results provide evidence that the cytoplasmic plaques of tight and adherens junctions are diverse in their composition and molecular architecture and establish a conceptual framework by which we can rationally address the mechanisms of tissue‐dependent junction physiology and signaling by cytoplasmic junctional proteins.</description><subject>adherens junction</subject><subject>Adherens junctions</subject><subject>Adherens Junctions - metabolism</subject><subject>Animals</subject><subject>Aorta</subject><subject>Cadherins - metabolism</subject><subject>Catenin</subject><subject>Cell Line</subject><subject>Collecting duct</subject><subject>Cytoplasm - metabolism</subject><subject>E-cadherin</subject><subject>endothelia</subject><subject>Endothelial cells</subject><subject>Endothelium</subject><subject>epithelia</subject><subject>Epithelial Cells - metabolism</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Immunofluorescence</subject><subject>Immunoprecipitation</subject><subject>Keratinocytes</subject><subject>Localization</subject><subject>Lung carcinoma</subject><subject>Membrane Proteins - metabolism</subject><subject>Mice</subject><subject>Plaques</subject><subject>protein</subject><subject>Proteins</subject><subject>tight junction</subject><subject>Tight Junction Proteins - metabolism</subject><subject>Tight Junctions - metabolism</subject><subject>Zonula occludens-1 protein</subject><issn>0077-8923</issn><issn>1749-6632</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcFO3DAQhq0KVBbaSx-gstRLVSnUEyexfUQrWpAQHNoeeoq8zgS8ytrBTmjDiUfgGXkSHJZy6IG5jDT-5tc__gn5AOwQUn11k46HwLmCN2QBolBZVfF8hywYEyKTKud7ZD_GNWOQy0K8JXu5rEAoxRbEL7HrHu7uY4_GttbQxt5giHaYqHV0uEKKf_uAMVrvqHYN9eFSO3urh3ngW2qmwfedjpu0m_r1iLQPfkDr4vyse2t0R9ejM_NGfEd2W91FfP_cD8ivb8c_lyfZ2cX30-XRWWaKnEPW6GbFsM0RYSXKshHQmKLkrQDJgbNS5VCtJGgly9KgBCUN6rwCUCrdKyU_IJ-3uslM8hSHemOjSbdqh36MNShgQhWciYR--g9d-zG45C5RhSg5VIol6suWMsHHGLCt-2A3Okw1sHqOoZ5jqJ9iSPDHZ8lxtcHmBf337wmALfDHdji9IlWf_z76sRV9BPnRlG8</recordid><startdate>201710</startdate><enddate>201710</enddate><creator>Vasileva, Ekaterina</creator><creator>Sluysmans, Sophie</creator><creator>Bochaton‐Piallat, Marie‐Luce</creator><creator>Citi, Sandra</creator><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>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7ST</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U7</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope></search><sort><creationdate>201710</creationdate><title>Cell‐specific diversity in the expression and organization of cytoplasmic plaque proteins of apical junctions</title><author>Vasileva, Ekaterina ; Sluysmans, Sophie ; Bochaton‐Piallat, Marie‐Luce ; Citi, Sandra</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4231-dadb0ef2ee1b755d71dc453f718313059216b81a9855ce8198cea261199892883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>adherens junction</topic><topic>Adherens junctions</topic><topic>Adherens Junctions - metabolism</topic><topic>Animals</topic><topic>Aorta</topic><topic>Cadherins - metabolism</topic><topic>Catenin</topic><topic>Cell Line</topic><topic>Collecting duct</topic><topic>Cytoplasm - metabolism</topic><topic>E-cadherin</topic><topic>endothelia</topic><topic>Endothelial cells</topic><topic>Endothelium</topic><topic>epithelia</topic><topic>Epithelial Cells - metabolism</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Immunofluorescence</topic><topic>Immunoprecipitation</topic><topic>Keratinocytes</topic><topic>Localization</topic><topic>Lung carcinoma</topic><topic>Membrane Proteins - metabolism</topic><topic>Mice</topic><topic>Plaques</topic><topic>protein</topic><topic>Proteins</topic><topic>tight junction</topic><topic>Tight Junction Proteins - metabolism</topic><topic>Tight Junctions - metabolism</topic><topic>Zonula occludens-1 protein</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vasileva, Ekaterina</creatorcontrib><creatorcontrib>Sluysmans, Sophie</creatorcontrib><creatorcontrib>Bochaton‐Piallat, Marie‐Luce</creatorcontrib><creatorcontrib>Citi, Sandra</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Toxicology 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>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Annals of the New York Academy of Sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vasileva, Ekaterina</au><au>Sluysmans, Sophie</au><au>Bochaton‐Piallat, Marie‐Luce</au><au>Citi, Sandra</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cell‐specific diversity in the expression and organization of cytoplasmic plaque proteins of apical junctions</atitle><jtitle>Annals of the New York Academy of Sciences</jtitle><addtitle>Ann N Y Acad Sci</addtitle><date>2017-10</date><risdate>2017</risdate><volume>1405</volume><issue>1</issue><spage>160</spage><epage>176</epage><pages>160-176</pages><issn>0077-8923</issn><eissn>1749-6632</eissn><abstract>Tight and adherens junctions play critical roles in the barrier, adhesion, and signaling functions of epithelial and endothelial cells. How the molecular organization of these junctions is tuned to the widely diverse physiological requirements of each tissue type is not well understood. Here, we address this question by examining the expression, localization, and interactions of major cytoplasmic plaque proteins of tight and adherens junctions in different cultured epithelial and endothelial cell lines. Immunoblotting and immunofluorescence analyses show that the expression profiles of cingulin, paracingulin, ZO‐1, ZO‐2, ZO‐3, PLEKHA7, afadin, PDZD11, p120‐catenin, and α‐catenin, as well as the transmembrane junctional proteins occludin, E‐cadherin, and VE‐cadherin, are significantly diverse when comparing kidney cells (MDCK, mCCD), keratinocytes (HaCaT), lung carcinoma (A427, A549), and endothelium‐derived cells (bEnd.3, meEC, H5V). Proximity ligation and co‐immunoprecipitation assays show that PLEKHA7 and PDZD11 are significantly more associated with the tight junction proteins cingulin and ZO‐1 in aortic endothelium–derived (meEC) cells but not kidney collecting duct epithelial (mCCD) cells. These results provide evidence that the cytoplasmic plaques of tight and adherens junctions are diverse in their composition and molecular architecture and establish a conceptual framework by which we can rationally address the mechanisms of tissue‐dependent junction physiology and signaling by cytoplasmic junctional proteins.</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>28617990</pmid><doi>10.1111/nyas.13391</doi><tpages>17</tpages></addata></record> |
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| ispartof | Annals of the New York Academy of Sciences, 2017-10, Vol.1405 (1), p.160-176 |
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| subjects | adherens junction Adherens junctions Adherens Junctions - metabolism Animals Aorta Cadherins - metabolism Catenin Cell Line Collecting duct Cytoplasm - metabolism E-cadherin endothelia Endothelial cells Endothelium epithelia Epithelial Cells - metabolism Humans Immunoblotting Immunofluorescence Immunoprecipitation Keratinocytes Localization Lung carcinoma Membrane Proteins - metabolism Mice Plaques protein Proteins tight junction Tight Junction Proteins - metabolism Tight Junctions - metabolism Zonula occludens-1 protein |
| title | Cell‐specific diversity in the expression and organization of cytoplasmic plaque proteins of apical junctions |
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