The LIN-2/LIN-7/LIN-10 Complex Mediates Basolateral Membrane Localization of the C. elegans EGF Receptor LET-23 in Vulval Epithelial Cells
In C. elegans, the LET-23 receptor tyrosine kinase is localized to the basolateral membranes of polarized vulval epithelial cells. lin-2, lin-7, and lin-10 are required for basolateral localization of LET-23, since LET-23 is mislocalized to the apical membrane in lin-2, lin-7, and lin-10 mutants. Ye...
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| Veröffentlicht in: | Cell 1998-09, Vol.94 (6), p.761-771 |
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| description | In C. elegans, the LET-23 receptor tyrosine kinase is localized to the basolateral membranes of polarized vulval epithelial cells. lin-2, lin-7, and lin-10 are required for basolateral localization of LET-23, since LET-23 is mislocalized to the apical membrane in lin-2, lin-7, and lin-10 mutants. Yeast two-hybrid, in vitro binding, and in vivo coimmunoprecipitation experiments show that LIN-2, LIN-7, and LIN-10 form a protein complex. Furthermore, compensatory mutations in lin-7 and let-23 exhibit allele-specific suppression of apical mislocalization and signaling-defective phenotypes. These results present a mechanism for basolateral localization of LET-23 receptor tyrosine kinase by direct binding to the LIN-2/LIN-7/LIN-10 complex. Each of the binding interactions within this complex is conserved, suggesting that this complex may also mediate basolateral localization in mammals. |
| doi_str_mv | 10.1016/S0092-8674(00)81735-3 |
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Yeast two-hybrid, in vitro binding, and in vivo coimmunoprecipitation experiments show that LIN-2, LIN-7, and LIN-10 form a protein complex. Furthermore, compensatory mutations in lin-7 and let-23 exhibit allele-specific suppression of apical mislocalization and signaling-defective phenotypes. These results present a mechanism for basolateral localization of LET-23 receptor tyrosine kinase by direct binding to the LIN-2/LIN-7/LIN-10 complex. Each of the binding interactions within this complex is conserved, suggesting that this complex may also mediate basolateral localization in mammals.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/S0092-8674(00)81735-3</identifier><identifier>PMID: 9753323</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Caenorhabditis elegans ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans Proteins ; Drosophila ; Epithelial Cells - chemistry ; Epithelial Cells - enzymology ; ErbB Receptors - chemistry ; ErbB Receptors - metabolism ; Female ; Gene Expression Regulation, Enzymologic ; Helminth Proteins - chemistry ; Helminth Proteins - isolation & purification ; Helminth Proteins - metabolism ; Mammals ; Membrane Proteins - chemistry ; Membrane Proteins - isolation & purification ; Membrane Proteins - metabolism ; Multienzyme Complexes - metabolism ; Mutation - physiology ; Precipitin Tests ; Protein Binding - physiology ; Protein Structure, Tertiary ; Proteins ; Signal Transduction - physiology ; Substrate Specificity ; Vulva - chemistry ; Vulva - cytology ; Vulva - enzymology ; Yeasts - enzymology</subject><ispartof>Cell, 1998-09, Vol.94 (6), p.761-771</ispartof><rights>2002 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c611t-d4695998d5d98728a4e7cad6ef4bffe81eb994d77ae724c4329b4c6c26fcc0153</citedby><cites>FETCH-LOGICAL-c611t-d4695998d5d98728a4e7cad6ef4bffe81eb994d77ae724c4329b4c6c26fcc0153</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0092867400817353$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9753323$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kaech, Susan M</creatorcontrib><creatorcontrib>Whitfield, Charles W</creatorcontrib><creatorcontrib>Kim, Stuart K</creatorcontrib><title>The LIN-2/LIN-7/LIN-10 Complex Mediates Basolateral Membrane Localization of the C. elegans EGF Receptor LET-23 in Vulval Epithelial Cells</title><title>Cell</title><addtitle>Cell</addtitle><description>In C. elegans, the LET-23 receptor tyrosine kinase is localized to the basolateral membranes of polarized vulval epithelial cells. lin-2, lin-7, and lin-10 are required for basolateral localization of LET-23, since LET-23 is mislocalized to the apical membrane in lin-2, lin-7, and lin-10 mutants. Yeast two-hybrid, in vitro binding, and in vivo coimmunoprecipitation experiments show that LIN-2, LIN-7, and LIN-10 form a protein complex. Furthermore, compensatory mutations in lin-7 and let-23 exhibit allele-specific suppression of apical mislocalization and signaling-defective phenotypes. These results present a mechanism for basolateral localization of LET-23 receptor tyrosine kinase by direct binding to the LIN-2/LIN-7/LIN-10 complex. Each of the binding interactions within this complex is conserved, suggesting that this complex may also mediate basolateral localization in mammals.</description><subject>Animals</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans Proteins</subject><subject>Drosophila</subject><subject>Epithelial Cells - chemistry</subject><subject>Epithelial Cells - enzymology</subject><subject>ErbB Receptors - chemistry</subject><subject>ErbB Receptors - metabolism</subject><subject>Female</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Helminth Proteins - chemistry</subject><subject>Helminth Proteins - isolation & purification</subject><subject>Helminth Proteins - metabolism</subject><subject>Mammals</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Membrane Proteins - metabolism</subject><subject>Multienzyme Complexes - metabolism</subject><subject>Mutation - physiology</subject><subject>Precipitin Tests</subject><subject>Protein Binding - physiology</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Signal Transduction - physiology</subject><subject>Substrate Specificity</subject><subject>Vulva - chemistry</subject><subject>Vulva - cytology</subject><subject>Vulva - enzymology</subject><subject>Yeasts - enzymology</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUctu1DAUjRCoTAufUMkrBIu0fsbxBgTRtFQaQIKBreU4N62RJ07tzIjyCXw1nodGsOrm-sr3nGOfe4rinOALgkl1-Q1jRcu6kvw1xm9qIpko2ZNiRrCSJSeSPi1mR8jz4jSlnxjjWghxUpwoKRijbFb8Wd4BWtx8LunltspdJRg1YTV6-IU-QefMBAl9MCn43EXj8-WqjWbIxGCNd7_N5MKAQo-mLNZcIPBwa4aE5tdX6CtYGKcQ0WK-LClDbkA_1n6TVeajy3jvctuA9-lF8aw3PsHLw3lWfL-aL5uP5eLL9U3zflHaipCp7HilhFJ1JzpVS1obDtKaroKet30PNYFWKd5JaUBSbjmjquW2srTqrcVEsLPi7V53XLcr6CwMUzalx-hWJj7oYJz-fzK4O30bNppRymWlssCrg0AM92tIk165ZLOFvJKwTloyRQUX9FEgkVhxwrdAsQfaGFKK0B9_Q7Depq13aettlBpjvUtbs8w7_9fKkXWIN8_f7eeQ97lxEHWyDgabQ41gJ90F98gLfwEKSrjK</recordid><startdate>19980918</startdate><enddate>19980918</enddate><creator>Kaech, Susan M</creator><creator>Whitfield, Charles W</creator><creator>Kim, Stuart K</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19980918</creationdate><title>The LIN-2/LIN-7/LIN-10 Complex Mediates Basolateral Membrane Localization of the C. elegans EGF Receptor LET-23 in Vulval Epithelial Cells</title><author>Kaech, Susan M ; Whitfield, Charles W ; Kim, Stuart K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c611t-d4695998d5d98728a4e7cad6ef4bffe81eb994d77ae724c4329b4c6c26fcc0153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Animals</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - genetics</topic><topic>Caenorhabditis elegans Proteins</topic><topic>Drosophila</topic><topic>Epithelial Cells - chemistry</topic><topic>Epithelial Cells - enzymology</topic><topic>ErbB Receptors - chemistry</topic><topic>ErbB Receptors - metabolism</topic><topic>Female</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Helminth Proteins - chemistry</topic><topic>Helminth Proteins - isolation & purification</topic><topic>Helminth Proteins - metabolism</topic><topic>Mammals</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Membrane Proteins - metabolism</topic><topic>Multienzyme Complexes - metabolism</topic><topic>Mutation - physiology</topic><topic>Precipitin Tests</topic><topic>Protein Binding - physiology</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Signal Transduction - physiology</topic><topic>Substrate Specificity</topic><topic>Vulva - chemistry</topic><topic>Vulva - cytology</topic><topic>Vulva - enzymology</topic><topic>Yeasts - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kaech, Susan M</creatorcontrib><creatorcontrib>Whitfield, Charles W</creatorcontrib><creatorcontrib>Kim, Stuart K</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect: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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kaech, Susan M</au><au>Whitfield, Charles W</au><au>Kim, Stuart K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The LIN-2/LIN-7/LIN-10 Complex Mediates Basolateral Membrane Localization of the C. elegans EGF Receptor LET-23 in Vulval Epithelial Cells</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1998-09-18</date><risdate>1998</risdate><volume>94</volume><issue>6</issue><spage>761</spage><epage>771</epage><pages>761-771</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>In C. elegans, the LET-23 receptor tyrosine kinase is localized to the basolateral membranes of polarized vulval epithelial cells. lin-2, lin-7, and lin-10 are required for basolateral localization of LET-23, since LET-23 is mislocalized to the apical membrane in lin-2, lin-7, and lin-10 mutants. Yeast two-hybrid, in vitro binding, and in vivo coimmunoprecipitation experiments show that LIN-2, LIN-7, and LIN-10 form a protein complex. Furthermore, compensatory mutations in lin-7 and let-23 exhibit allele-specific suppression of apical mislocalization and signaling-defective phenotypes. These results present a mechanism for basolateral localization of LET-23 receptor tyrosine kinase by direct binding to the LIN-2/LIN-7/LIN-10 complex. Each of the binding interactions within this complex is conserved, suggesting that this complex may also mediate basolateral localization in mammals.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9753323</pmid><doi>10.1016/S0092-8674(00)81735-3</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Caenorhabditis elegans Caenorhabditis elegans - genetics Caenorhabditis elegans Proteins Drosophila Epithelial Cells - chemistry Epithelial Cells - enzymology ErbB Receptors - chemistry ErbB Receptors - metabolism Female Gene Expression Regulation, Enzymologic Helminth Proteins - chemistry Helminth Proteins - isolation & purification Helminth Proteins - metabolism Mammals Membrane Proteins - chemistry Membrane Proteins - isolation & purification Membrane Proteins - metabolism Multienzyme Complexes - metabolism Mutation - physiology Precipitin Tests Protein Binding - physiology Protein Structure, Tertiary Proteins Signal Transduction - physiology Substrate Specificity Vulva - chemistry Vulva - cytology Vulva - enzymology Yeasts - enzymology |
| title | The LIN-2/LIN-7/LIN-10 Complex Mediates Basolateral Membrane Localization of the C. elegans EGF Receptor LET-23 in Vulval Epithelial Cells |
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