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The supramolecular architecture of junctional microdomains in native lens membranes
Gap junctions formed by connexons and thin junctions formed by lens‐specific aquaporin 0 (AQP0) mediate the tight packing of fibre cells necessary for lens transparency. Gap junctions conduct water, ions and metabolites between cells, whereas junctional AQP0 seems to be involved in cell adhesion. Hi...
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Published in: | EMBO reports 2007-01, Vol.8 (1), p.51-55 |
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description | Gap junctions formed by connexons and thin junctions formed by lens‐specific aquaporin 0 (AQP0) mediate the tight packing of fibre cells necessary for lens transparency. Gap junctions conduct water, ions and metabolites between cells, whereas junctional AQP0 seems to be involved in cell adhesion. High‐resolution atomic force microscopy (AFM) showed the supramolecular organization of these proteins in native lens core membranes, in which AQP0 forms two‐dimensional arrays that are surrounded by densely packed gap junction channels. These junctional microdomains simultaneously provide adhesion and communication between fibre cells. The AFM topographs also showed that the extracellular loops of AQP0 in junctional microdomains adopt a conformation that closely resembles the structure of junctional AQP0, in which the water pore is thought to be closed. Finally, time‐lapse AFM imaging provided insights into AQP0 array formation. This first high‐resolution view of a multicomponent eukaryotic membrane shows how membrane proteins self‐assemble into functional microdomains. |
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Gap junctions conduct water, ions and metabolites between cells, whereas junctional AQP0 seems to be involved in cell adhesion. High‐resolution atomic force microscopy (AFM) showed the supramolecular organization of these proteins in native lens core membranes, in which AQP0 forms two‐dimensional arrays that are surrounded by densely packed gap junction channels. These junctional microdomains simultaneously provide adhesion and communication between fibre cells. The AFM topographs also showed that the extracellular loops of AQP0 in junctional microdomains adopt a conformation that closely resembles the structure of junctional AQP0, in which the water pore is thought to be closed. Finally, time‐lapse AFM imaging provided insights into AQP0 array formation. 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Gap junctions conduct water, ions and metabolites between cells, whereas junctional AQP0 seems to be involved in cell adhesion. High‐resolution atomic force microscopy (AFM) showed the supramolecular organization of these proteins in native lens core membranes, in which AQP0 forms two‐dimensional arrays that are surrounded by densely packed gap junction channels. These junctional microdomains simultaneously provide adhesion and communication between fibre cells. The AFM topographs also showed that the extracellular loops of AQP0 in junctional microdomains adopt a conformation that closely resembles the structure of junctional AQP0, in which the water pore is thought to be closed. Finally, time‐lapse AFM imaging provided insights into AQP0 array formation. This first high‐resolution view of a multicomponent eukaryotic membrane shows how membrane proteins self‐assemble into functional microdomains.</description><subject>Adhesion</subject><subject>Animals</subject><subject>aquaporin</subject><subject>Aquaporins - ultrastructure</subject><subject>Arrays</subject><subject>atomic force microscopy</subject><subject>Cell adhesion & migration</subject><subject>Cell Membrane - ultrastructure</subject><subject>connexin</subject><subject>Eukaryotes</subject><subject>Eye Proteins - ultrastructure</subject><subject>Eyes & eyesight</subject><subject>gap junction</subject><subject>Gap Junctions - ultrastructure</subject><subject>Ions</subject><subject>Lens, Crystalline - ultrastructure</subject><subject>Membrane Glycoproteins - ultrastructure</subject><subject>membrane protein</subject><subject>Membranes</subject><subject>Metabolites</subject><subject>Microscopy, Atomic Force</subject><subject>Molecular biology</subject><subject>Proteins</subject><subject>Scientific Report</subject><subject>Sheep</subject><issn>1469-221X</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNqFUUlv1DAYjRCIlsKdCyjiwC2Dl8SOL0idqguigFSKqLhYHvtLx8GJBzsp9N_jkmgGOMDJy1u-5WXZU4wWGNH6VWwX0K18WPASobqq72X7uGSioJjX9-c7IfhqL3sUY4sQqgSvH2Z7mGNSVhjvZx8v15DHcRNU5x3o0amQq6DXdgA9jAFy3-Tt2OvB-l65vLM6eOM7ZfuY2z7v1WBvIHeQnl1qJage4uPsQaNchCfzeZB9Ojm-PDorzj-cvjk6PC80o6IuKGkEJTWiypjGcK6hpIYLU5fpTwtTIbaqtGANGI5ZpRhCqlpVQA0gRSijB9nryXczrjowGvohKCc3wXYq3EqvrPwT6e1aXvsbiblgvMTJ4OVsEPy3EeIgOxs1OJem8GOUrKaCI3RX6cVfxNaPIS0kSpL2ThKJJhKaSGlFMQZotp1gJO_ikrGVv-KSc1xJ8vz3CXaCOZ9EEBPhu3Vw-19DefxuebEzx5M2Jll_DWHX9D8aejZpUrAp_W3BHV5MuI0D_NjCKnyVjFNeyc_vT-XyC7m4Wr49kyf0J2160D8</recordid><startdate>200701</startdate><enddate>200701</enddate><creator>Buzhynskyy, Nikolay</creator><creator>Hite, Richard K</creator><creator>Walz, Thomas</creator><creator>Scheuring, Simon</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><scope>BSCLL</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>3V.</scope><scope>7QL</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200701</creationdate><title>The supramolecular architecture of junctional microdomains in native lens membranes</title><author>Buzhynskyy, Nikolay ; Hite, Richard K ; Walz, Thomas ; Scheuring, Simon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6398-32f932803addfd77ce43d79d84803c9d506b5c96fed7165a600a5b5e3de0a2363</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adhesion</topic><topic>Animals</topic><topic>aquaporin</topic><topic>Aquaporins - ultrastructure</topic><topic>Arrays</topic><topic>atomic force microscopy</topic><topic>Cell adhesion & migration</topic><topic>Cell Membrane - ultrastructure</topic><topic>connexin</topic><topic>Eukaryotes</topic><topic>Eye Proteins - ultrastructure</topic><topic>Eyes & eyesight</topic><topic>gap junction</topic><topic>Gap Junctions - ultrastructure</topic><topic>Ions</topic><topic>Lens, Crystalline - ultrastructure</topic><topic>Membrane Glycoproteins - ultrastructure</topic><topic>membrane protein</topic><topic>Membranes</topic><topic>Metabolites</topic><topic>Microscopy, Atomic Force</topic><topic>Molecular biology</topic><topic>Proteins</topic><topic>Scientific Report</topic><topic>Sheep</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Buzhynskyy, Nikolay</creatorcontrib><creatorcontrib>Hite, Richard K</creatorcontrib><creatorcontrib>Walz, Thomas</creatorcontrib><creatorcontrib>Scheuring, Simon</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection (Proquest)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Buzhynskyy, Nikolay</au><au>Hite, Richard K</au><au>Walz, Thomas</au><au>Scheuring, Simon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The supramolecular architecture of junctional microdomains in native lens membranes</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2007-01</date><risdate>2007</risdate><volume>8</volume><issue>1</issue><spage>51</spage><epage>55</epage><pages>51-55</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><coden>ERMEAX</coden><abstract>Gap junctions formed by connexons and thin junctions formed by lens‐specific aquaporin 0 (AQP0) mediate the tight packing of fibre cells necessary for lens transparency. Gap junctions conduct water, ions and metabolites between cells, whereas junctional AQP0 seems to be involved in cell adhesion. High‐resolution atomic force microscopy (AFM) showed the supramolecular organization of these proteins in native lens core membranes, in which AQP0 forms two‐dimensional arrays that are surrounded by densely packed gap junction channels. These junctional microdomains simultaneously provide adhesion and communication between fibre cells. The AFM topographs also showed that the extracellular loops of AQP0 in junctional microdomains adopt a conformation that closely resembles the structure of junctional AQP0, in which the water pore is thought to be closed. Finally, time‐lapse AFM imaging provided insights into AQP0 array formation. This first high‐resolution view of a multicomponent eukaryotic membrane shows how membrane proteins self‐assemble into functional microdomains.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>17124511</pmid><doi>10.1038/sj.embor.7400858</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adhesion Animals aquaporin Aquaporins - ultrastructure Arrays atomic force microscopy Cell adhesion & migration Cell Membrane - ultrastructure connexin Eukaryotes Eye Proteins - ultrastructure Eyes & eyesight gap junction Gap Junctions - ultrastructure Ions Lens, Crystalline - ultrastructure Membrane Glycoproteins - ultrastructure membrane protein Membranes Metabolites Microscopy, Atomic Force Molecular biology Proteins Scientific Report Sheep |
title | The supramolecular architecture of junctional microdomains in native lens membranes |
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