E-Cadherin and APC Compete for the Interaction with β-Catenin and the Cytoskeleton
β-Catenin is involved in the formation of adherens junctions of mammalian epithelia. It interacts with the cell adhesion molecule E-cadherin and also with the tumor suppressor gene product APC, and the Drosophila homologue of β-catenin, armadillo, mediates morphogenetic signals. We demonstrate here...
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| Veröffentlicht in: | The Journal of cell biology 1994-12, Vol.127 (6), p.2061-2069 |
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| container_title | The Journal of cell biology |
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| creator | Hülsken, Jörg Birchmeier, Walter Behrens, Jürgen |
| description | β-Catenin is involved in the formation of adherens junctions of mammalian epithelia. It interacts with the cell adhesion molecule E-cadherin and also with the tumor suppressor gene product APC, and the Drosophila homologue of β-catenin, armadillo, mediates morphogenetic signals. We demonstrate here that E-cadherin and APC directly compete for binding to the internal, armadillo-like repeats of β-catenin; the NH2-terminal domain of β-catenin mediates the interaction of the alternative E-cadherin and APC complexes to the cytoskeleton by binding to α-catenin. Plakoglobin (γ-catenin), which is structurally related to β-catenin, mediates identical interactions. We thus show that the APC tumor suppressor gene product forms strikingly similar associations as found in cell junctions and suggest that β-catenin and plakoglobin are central regulators of cell adhesion, cytoskeletal interaction, and tumor suppression. |
| doi_str_mv | 10.1083/jcb.127.6.2061 |
| format | Article |
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It interacts with the cell adhesion molecule E-cadherin and also with the tumor suppressor gene product APC, and the Drosophila homologue of β-catenin, armadillo, mediates morphogenetic signals. We demonstrate here that E-cadherin and APC directly compete for binding to the internal, armadillo-like repeats of β-catenin; the NH2-terminal domain of β-catenin mediates the interaction of the alternative E-cadherin and APC complexes to the cytoskeleton by binding to α-catenin. Plakoglobin (γ-catenin), which is structurally related to β-catenin, mediates identical interactions. 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It interacts with the cell adhesion molecule E-cadherin and also with the tumor suppressor gene product APC, and the Drosophila homologue of β-catenin, armadillo, mediates morphogenetic signals. We demonstrate here that E-cadherin and APC directly compete for binding to the internal, armadillo-like repeats of β-catenin; the NH2-terminal domain of β-catenin mediates the interaction of the alternative E-cadherin and APC complexes to the cytoskeleton by binding to α-catenin. Plakoglobin (γ-catenin), which is structurally related to β-catenin, mediates identical interactions. We thus show that the APC tumor suppressor gene product forms strikingly similar associations as found in cell junctions and suggest that β-catenin and plakoglobin are central regulators of cell adhesion, cytoskeletal interaction, and tumor suppression.</description><subject>Adenomatous Polyposis Coli Protein</subject><subject>alpha Catenin</subject><subject>Amino Acid Sequence</subject><subject>Antibodies</subject><subject>Base Sequence</subject><subject>beta Catenin</subject><subject>Cadherins</subject><subject>Cadherins - genetics</subject><subject>Cadherins - isolation & purification</subject><subject>Cadherins - metabolism</subject><subject>Catenins</subject><subject>Cell adhesion</subject><subject>Cell lines</subject><subject>Cells</subject><subject>Cells, Cultured</subject><subject>Cellular biology</subject><subject>Complementary DNA</subject><subject>Cytoskeletal Proteins - genetics</subject><subject>Cytoskeletal Proteins - isolation & purification</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>Cytoskeleton - metabolism</subject><subject>Desmoplakins</subject><subject>Embryonic cells</subject><subject>Epithelial cells</subject><subject>Fluorescent Antibody Technique</subject><subject>gamma Catenin</subject><subject>Genes</subject><subject>Intercellular Junctions</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Neurons</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>Recombinant Proteins - metabolism</subject><subject>Trans-Activators</subject><subject>Tumors</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkc1u1DAUha0KVKaFbVcgRSy6S-p_OxukKiptpUogFdaW49wwGTL2YHtAfS0ehGfCoxm1hbu5i_Odo3t1EDojuCFYs4uV6xtCVSMbiiU5QgsiOK414fgFWmBMSd0KKl6hk5RWGGOuODtGx0pjKTRdoPururPDEuLkK-uH6vJzV3VhvYEM1RhilZdQ3foM0bo8BV_9mvKy-vO7mDL4g2fHdA85pO8wQw7-NXo52jnBm8M-RV8_Xn3pbuq7T9e33eVd7bjkuXbAGW9pj4UTVDpQjrRD2zKpe6aF7CljI5Wa65ERWQbTcSQtwKCsBMuBnaIP-9zNtl_D4MDnaGezidPaxgcT7GT-Vfy0NN_CT0MJxbTFJeD8EBDDjy2kbNZTcjDP1kPYJkNkqySXuoDv_wNXYRt9ea5kKayFEqJAzR5yMaQUYXy8hGCz68qUrkzpykiz66oY3j2__xE_lFP0t3t9lXKIT2mSSEU4-wttzpjx</recordid><startdate>19941201</startdate><enddate>19941201</enddate><creator>Hülsken, Jörg</creator><creator>Birchmeier, Walter</creator><creator>Behrens, Jürgen</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>7T5</scope><scope>7TO</scope><scope>5PM</scope></search><sort><creationdate>19941201</creationdate><title>E-Cadherin and APC Compete for the Interaction with β-Catenin and the Cytoskeleton</title><author>Hülsken, Jörg ; Birchmeier, Walter ; Behrens, Jürgen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c464t-ce43492b05c526ce7c19d99368b3856b233f26848f31666602ff19eed7a6ea4e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Adenomatous Polyposis Coli Protein</topic><topic>alpha Catenin</topic><topic>Amino Acid Sequence</topic><topic>Antibodies</topic><topic>Base Sequence</topic><topic>beta Catenin</topic><topic>Cadherins</topic><topic>Cadherins - genetics</topic><topic>Cadherins - isolation & purification</topic><topic>Cadherins - metabolism</topic><topic>Catenins</topic><topic>Cell adhesion</topic><topic>Cell lines</topic><topic>Cells</topic><topic>Cells, Cultured</topic><topic>Cellular biology</topic><topic>Complementary DNA</topic><topic>Cytoskeletal Proteins - genetics</topic><topic>Cytoskeletal Proteins - isolation & purification</topic><topic>Cytoskeletal Proteins - metabolism</topic><topic>Cytoskeleton - metabolism</topic><topic>Desmoplakins</topic><topic>Embryonic cells</topic><topic>Epithelial cells</topic><topic>Fluorescent Antibody Technique</topic><topic>gamma Catenin</topic><topic>Genes</topic><topic>Intercellular Junctions</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Neurons</topic><topic>Precipitin Tests</topic><topic>Protein Binding</topic><topic>Recombinant Proteins - metabolism</topic><topic>Trans-Activators</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hülsken, Jörg</creatorcontrib><creatorcontrib>Birchmeier, Walter</creatorcontrib><creatorcontrib>Behrens, Jürgen</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>Immunology Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</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>Hülsken, Jörg</au><au>Birchmeier, Walter</au><au>Behrens, Jürgen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>E-Cadherin and APC Compete for the Interaction with β-Catenin and the Cytoskeleton</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1994-12-01</date><risdate>1994</risdate><volume>127</volume><issue>6</issue><spage>2061</spage><epage>2069</epage><pages>2061-2069</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>β-Catenin is involved in the formation of adherens junctions of mammalian epithelia. It interacts with the cell adhesion molecule E-cadherin and also with the tumor suppressor gene product APC, and the Drosophila homologue of β-catenin, armadillo, mediates morphogenetic signals. We demonstrate here that E-cadherin and APC directly compete for binding to the internal, armadillo-like repeats of β-catenin; the NH2-terminal domain of β-catenin mediates the interaction of the alternative E-cadherin and APC complexes to the cytoskeleton by binding to α-catenin. Plakoglobin (γ-catenin), which is structurally related to β-catenin, mediates identical interactions. 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| subjects | Adenomatous Polyposis Coli Protein alpha Catenin Amino Acid Sequence Antibodies Base Sequence beta Catenin Cadherins Cadherins - genetics Cadherins - isolation & purification Cadherins - metabolism Catenins Cell adhesion Cell lines Cells Cells, Cultured Cellular biology Complementary DNA Cytoskeletal Proteins - genetics Cytoskeletal Proteins - isolation & purification Cytoskeletal Proteins - metabolism Cytoskeleton - metabolism Desmoplakins Embryonic cells Epithelial cells Fluorescent Antibody Technique gamma Catenin Genes Intercellular Junctions Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Neurons Precipitin Tests Protein Binding Recombinant Proteins - metabolism Trans-Activators Tumors |
| title | E-Cadherin and APC Compete for the Interaction with β-Catenin and the Cytoskeleton |
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