The Dual Role of Zonula Occludens (ZO) Proteins

ZO (zonula occludens) proteins are scaffolding proteins providing the structural basis for the assembly of multiprotein complexes at the cytoplasmic surface of intercellular junctions. In addition, they provide a link between the integral membrane proteins and the filamentous cytoskeleton. ZO protei...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:BioMed research international 2010-01, Vol.2010 (2010), p.1-11
Hauptverfasser: Lametschwandtner, A., Zweimueller-Mayer, J., Steinbacher, P., Bauer, H. C., Bauer, H.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 11
container_issue 2010
container_start_page 1
container_title BioMed research international
container_volume 2010
creator Lametschwandtner, A.
Zweimueller-Mayer, J.
Steinbacher, P.
Bauer, H. C.
Bauer, H.
description ZO (zonula occludens) proteins are scaffolding proteins providing the structural basis for the assembly of multiprotein complexes at the cytoplasmic surface of intercellular junctions. In addition, they provide a link between the integral membrane proteins and the filamentous cytoskeleton. ZO proteins belong to the large family of membrane-associated guanylate kinase (MAGUK)-like proteins comprising a number of subfamilies based on domain content and sequence similarity. Besides their structural function at cell-cell contacts, ZO proteins appear to participate in the regulation of cell growth and proliferation. Detailed molecular studies have shown that ZO proteins exhibit conserved functional nuclear localization and nuclear export motifs within their amino acid sequence. Further, ZO proteins interact with dual residency proteins localizing to the plasma membrane and the nucleus. Although the nuclear targeting of ZO proteins has well been described, many questions concerning the biological significance of this process have remained open. This review focuses on the dual role of ZO proteins, being indispensable structural components at the junctional site and functioning in signal transduction pathways related to gene expression and cell behavior.
doi_str_mv 10.1155/2010/402593
format Article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2836178</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2287888881</sourcerecordid><originalsourceid>FETCH-LOGICAL-c594t-ce624e65077c9a40ff31d3f01756d8695d0cde930802e8420297f061915974d83</originalsourceid><addsrcrecordid>eNqN0c-LEzEUB_Agiu1WT56Vwcu6yti8_JxchKWuq1CoSL30EmLmjZ1lOulOZpT97zdlalEvekogH768ly8hz4C-BZByzijQuaBMGv6ATAGA5ppJeHi6Cz4hZzHeUAq6UOYxmTDKmFBST8l8vcXs_eCa7EtoMAtVtgnt0Lhs5X0zlNjG7NVmdZF97kKPdRufkEeVayI-PZ4z8vXD1XrxMV-urj8tLpe5l0b0uUfFBCpJtfbGCVpVHEpepQGkKtMMsqS-RMNpQRkWIs1jdEUVGJBGi7LgM_JuzN0P33ZYemz7zjV239U7193Z4Gr750tbb-338MOygqu0Zgo4PwZ04XbA2NtdHT02jWsxDNFqIVQB9H8k51yA0CrJl3_JmzB0bfoHW0gFShsBCb0Zke9CjB1Wp6GB2kNh9lCYHQtL-sXve57sr4YSeD2Cbd2W7mf9j7TnI8ZEsHInLJRhIPk97LuitA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>856167941</pqid></control><display><type>article</type><title>The Dual Role of Zonula Occludens (ZO) Proteins</title><source>MEDLINE</source><source>Wiley Online Library Open Access</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>PubMed Central Open Access</source><creator>Lametschwandtner, A. ; Zweimueller-Mayer, J. ; Steinbacher, P. ; Bauer, H. C. ; Bauer, H.</creator><contributor>McCann, Amanda</contributor><creatorcontrib>Lametschwandtner, A. ; Zweimueller-Mayer, J. ; Steinbacher, P. ; Bauer, H. C. ; Bauer, H. ; McCann, Amanda</creatorcontrib><description>ZO (zonula occludens) proteins are scaffolding proteins providing the structural basis for the assembly of multiprotein complexes at the cytoplasmic surface of intercellular junctions. In addition, they provide a link between the integral membrane proteins and the filamentous cytoskeleton. ZO proteins belong to the large family of membrane-associated guanylate kinase (MAGUK)-like proteins comprising a number of subfamilies based on domain content and sequence similarity. Besides their structural function at cell-cell contacts, ZO proteins appear to participate in the regulation of cell growth and proliferation. Detailed molecular studies have shown that ZO proteins exhibit conserved functional nuclear localization and nuclear export motifs within their amino acid sequence. Further, ZO proteins interact with dual residency proteins localizing to the plasma membrane and the nucleus. Although the nuclear targeting of ZO proteins has well been described, many questions concerning the biological significance of this process have remained open. This review focuses on the dual role of ZO proteins, being indispensable structural components at the junctional site and functioning in signal transduction pathways related to gene expression and cell behavior.</description><identifier>ISSN: 1110-7243</identifier><identifier>ISSN: 2314-6133</identifier><identifier>EISSN: 1110-7251</identifier><identifier>EISSN: 2314-6141</identifier><identifier>DOI: 10.1155/2010/402593</identifier><identifier>PMID: 20224657</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Puplishing Corporation</publisher><subject>Adapter proteins ; Adenoviruses ; Animals ; Biomedical research ; Cell adhesion &amp; migration ; Cell cycle ; Cell Enlargement ; Cell growth ; Cell Nucleus - physiology ; Cell Proliferation ; Epithelial Cells - physiology ; Humans ; Insects ; Kinases ; Membrane Proteins - metabolism ; Review ; Signal transduction ; Tight Junctions - physiology</subject><ispartof>BioMed research international, 2010-01, Vol.2010 (2010), p.1-11</ispartof><rights>Copyright © 2010</rights><rights>Copyright © 2010 H. Bauer et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.</rights><rights>Copyright © 2010 H. Bauer et al. 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c594t-ce624e65077c9a40ff31d3f01756d8695d0cde930802e8420297f061915974d83</citedby><cites>FETCH-LOGICAL-c594t-ce624e65077c9a40ff31d3f01756d8695d0cde930802e8420297f061915974d83</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/PMC2836178/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2836178/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20224657$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>McCann, Amanda</contributor><creatorcontrib>Lametschwandtner, A.</creatorcontrib><creatorcontrib>Zweimueller-Mayer, J.</creatorcontrib><creatorcontrib>Steinbacher, P.</creatorcontrib><creatorcontrib>Bauer, H. C.</creatorcontrib><creatorcontrib>Bauer, H.</creatorcontrib><title>The Dual Role of Zonula Occludens (ZO) Proteins</title><title>BioMed research international</title><addtitle>J Biomed Biotechnol</addtitle><description>ZO (zonula occludens) proteins are scaffolding proteins providing the structural basis for the assembly of multiprotein complexes at the cytoplasmic surface of intercellular junctions. In addition, they provide a link between the integral membrane proteins and the filamentous cytoskeleton. ZO proteins belong to the large family of membrane-associated guanylate kinase (MAGUK)-like proteins comprising a number of subfamilies based on domain content and sequence similarity. Besides their structural function at cell-cell contacts, ZO proteins appear to participate in the regulation of cell growth and proliferation. Detailed molecular studies have shown that ZO proteins exhibit conserved functional nuclear localization and nuclear export motifs within their amino acid sequence. Further, ZO proteins interact with dual residency proteins localizing to the plasma membrane and the nucleus. Although the nuclear targeting of ZO proteins has well been described, many questions concerning the biological significance of this process have remained open. This review focuses on the dual role of ZO proteins, being indispensable structural components at the junctional site and functioning in signal transduction pathways related to gene expression and cell behavior.</description><subject>Adapter proteins</subject><subject>Adenoviruses</subject><subject>Animals</subject><subject>Biomedical research</subject><subject>Cell adhesion &amp; migration</subject><subject>Cell cycle</subject><subject>Cell Enlargement</subject><subject>Cell growth</subject><subject>Cell Nucleus - physiology</subject><subject>Cell Proliferation</subject><subject>Epithelial Cells - physiology</subject><subject>Humans</subject><subject>Insects</subject><subject>Kinases</subject><subject>Membrane Proteins - metabolism</subject><subject>Review</subject><subject>Signal transduction</subject><subject>Tight Junctions - physiology</subject><issn>1110-7243</issn><issn>2314-6133</issn><issn>1110-7251</issn><issn>2314-6141</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqN0c-LEzEUB_Agiu1WT56Vwcu6yti8_JxchKWuq1CoSL30EmLmjZ1lOulOZpT97zdlalEvekogH768ly8hz4C-BZByzijQuaBMGv6ATAGA5ppJeHi6Cz4hZzHeUAq6UOYxmTDKmFBST8l8vcXs_eCa7EtoMAtVtgnt0Lhs5X0zlNjG7NVmdZF97kKPdRufkEeVayI-PZ4z8vXD1XrxMV-urj8tLpe5l0b0uUfFBCpJtfbGCVpVHEpepQGkKtMMsqS-RMNpQRkWIs1jdEUVGJBGi7LgM_JuzN0P33ZYemz7zjV239U7193Z4Gr750tbb-338MOygqu0Zgo4PwZ04XbA2NtdHT02jWsxDNFqIVQB9H8k51yA0CrJl3_JmzB0bfoHW0gFShsBCb0Zke9CjB1Wp6GB2kNh9lCYHQtL-sXve57sr4YSeD2Cbd2W7mf9j7TnI8ZEsHInLJRhIPk97LuitA</recordid><startdate>20100101</startdate><enddate>20100101</enddate><creator>Lametschwandtner, A.</creator><creator>Zweimueller-Mayer, J.</creator><creator>Steinbacher, P.</creator><creator>Bauer, H. C.</creator><creator>Bauer, H.</creator><general>Hindawi Puplishing Corporation</general><general>Hindawi Publishing Corporation</general><general>Hindawi Limited</general><scope>ADJCN</scope><scope>AHFXO</scope><scope>RHU</scope><scope>RHW</scope><scope>RHX</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>7QO</scope><scope>7T7</scope><scope>7TK</scope><scope>7U7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>CWDGH</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20100101</creationdate><title>The Dual Role of Zonula Occludens (ZO) Proteins</title><author>Lametschwandtner, A. ; Zweimueller-Mayer, J. ; Steinbacher, P. ; Bauer, H. C. ; Bauer, H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c594t-ce624e65077c9a40ff31d3f01756d8695d0cde930802e8420297f061915974d83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Adapter proteins</topic><topic>Adenoviruses</topic><topic>Animals</topic><topic>Biomedical research</topic><topic>Cell adhesion &amp; migration</topic><topic>Cell cycle</topic><topic>Cell Enlargement</topic><topic>Cell growth</topic><topic>Cell Nucleus - physiology</topic><topic>Cell Proliferation</topic><topic>Epithelial Cells - physiology</topic><topic>Humans</topic><topic>Insects</topic><topic>Kinases</topic><topic>Membrane Proteins - metabolism</topic><topic>Review</topic><topic>Signal transduction</topic><topic>Tight Junctions - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lametschwandtner, A.</creatorcontrib><creatorcontrib>Zweimueller-Mayer, J.</creatorcontrib><creatorcontrib>Steinbacher, P.</creatorcontrib><creatorcontrib>Bauer, H. C.</creatorcontrib><creatorcontrib>Bauer, H.</creatorcontrib><collection>الدوريات العلمية والإحصائية - e-Marefa Academic and Statistical Periodicals</collection><collection>معرفة - المحتوى العربي الأكاديمي المتكامل - e-Marefa Academic Complete</collection><collection>Hindawi Publishing Complete</collection><collection>Hindawi Publishing Subscription Journals</collection><collection>Hindawi Publishing Open Access</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>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies &amp; Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>Middle East &amp; Africa Database</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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Advanced Technologies &amp; Aerospace Database</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Publicly Available Content Database</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 China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>BioMed research international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lametschwandtner, A.</au><au>Zweimueller-Mayer, J.</au><au>Steinbacher, P.</au><au>Bauer, H. C.</au><au>Bauer, H.</au><au>McCann, Amanda</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Dual Role of Zonula Occludens (ZO) Proteins</atitle><jtitle>BioMed research international</jtitle><addtitle>J Biomed Biotechnol</addtitle><date>2010-01-01</date><risdate>2010</risdate><volume>2010</volume><issue>2010</issue><spage>1</spage><epage>11</epage><pages>1-11</pages><issn>1110-7243</issn><issn>2314-6133</issn><eissn>1110-7251</eissn><eissn>2314-6141</eissn><abstract>ZO (zonula occludens) proteins are scaffolding proteins providing the structural basis for the assembly of multiprotein complexes at the cytoplasmic surface of intercellular junctions. In addition, they provide a link between the integral membrane proteins and the filamentous cytoskeleton. ZO proteins belong to the large family of membrane-associated guanylate kinase (MAGUK)-like proteins comprising a number of subfamilies based on domain content and sequence similarity. Besides their structural function at cell-cell contacts, ZO proteins appear to participate in the regulation of cell growth and proliferation. Detailed molecular studies have shown that ZO proteins exhibit conserved functional nuclear localization and nuclear export motifs within their amino acid sequence. Further, ZO proteins interact with dual residency proteins localizing to the plasma membrane and the nucleus. Although the nuclear targeting of ZO proteins has well been described, many questions concerning the biological significance of this process have remained open. This review focuses on the dual role of ZO proteins, being indispensable structural components at the junctional site and functioning in signal transduction pathways related to gene expression and cell behavior.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Puplishing Corporation</pub><pmid>20224657</pmid><doi>10.1155/2010/402593</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1110-7243
ispartof BioMed research international, 2010-01, Vol.2010 (2010), p.1-11
issn 1110-7243
2314-6133
1110-7251
2314-6141
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2836178
source MEDLINE; Wiley Online Library Open Access; PubMed Central; Alma/SFX Local Collection; PubMed Central Open Access
subjects Adapter proteins
Adenoviruses
Animals
Biomedical research
Cell adhesion & migration
Cell cycle
Cell Enlargement
Cell growth
Cell Nucleus - physiology
Cell Proliferation
Epithelial Cells - physiology
Humans
Insects
Kinases
Membrane Proteins - metabolism
Review
Signal transduction
Tight Junctions - physiology
title The Dual Role of Zonula Occludens (ZO) Proteins
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-10T01%3A24%3A44IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Dual%20Role%20of%20Zonula%20Occludens%20(ZO)%20Proteins&rft.jtitle=BioMed%20research%20international&rft.au=Lametschwandtner,%20A.&rft.date=2010-01-01&rft.volume=2010&rft.issue=2010&rft.spage=1&rft.epage=11&rft.pages=1-11&rft.issn=1110-7243&rft.eissn=1110-7251&rft_id=info:doi/10.1155/2010/402593&rft_dat=%3Cproquest_pubme%3E2287888881%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=856167941&rft_id=info:pmid/20224657&rfr_iscdi=true