EGF domain swap converts a drosophila EGF receptor activator into an inhibitor
In Drosophila the function of the epidermal growth factor (EGF) receptor is modulated zygotically by three EGF-like proteins: Spitz (Spi), which is a potent activator; Vein (Vn), which is a moderate activator; and Argos (Aos), which is an inhibitor. Chimeric molecules were constructed in which the E...
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| Veröffentlicht in: | Genes & development 1998-04, Vol.12 (7), p.908-913 |
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| container_title | Genes & development |
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| creator | Schnepp, B Donaldson, T Grumbling, G Ostrowski, S Schweitzer, R Shilo, B Z Simcox, A |
| description | In Drosophila the function of the epidermal growth factor (EGF) receptor is modulated zygotically by three EGF-like proteins: Spitz (Spi), which is a potent activator; Vein (Vn), which is a moderate activator; and Argos (Aos), which is an inhibitor. Chimeric molecules were constructed in which the EGF domain of Vn was swapped with the EGF domain from each factor. The modified Vn proteins behaved both in vitro and in vivo with properties characteristic of the factor from which the EGF domain was derived. These results demonstrate that the EGF domain is the key determinant that gives DER inhibitors and activators their distinct properties. |
| doi_str_mv | 10.1101/gad.12.7.908 |
| format | Article |
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Chimeric molecules were constructed in which the EGF domain of Vn was swapped with the EGF domain from each factor. The modified Vn proteins behaved both in vitro and in vivo with properties characteristic of the factor from which the EGF domain was derived. These results demonstrate that the EGF domain is the key determinant that gives DER inhibitors and activators their distinct properties.</description><identifier>ISSN: 0890-9369</identifier><identifier>DOI: 10.1101/gad.12.7.908</identifier><identifier>PMID: 9531530</identifier><language>eng</language><publisher>United States: Cold Spring Harbor Laboratory Press</publisher><subject>Amino Acid Sequence ; Animals ; Drosophila - genetics ; Drosophila Proteins ; Epidermal Growth Factor - chemistry ; Epidermal Growth Factor - genetics ; Epidermal Growth Factor - physiology ; ErbB Receptors - agonists ; ErbB Receptors - antagonists & inhibitors ; ErbB Receptors - drug effects ; Eye - anatomy & histology ; Eye - drug effects ; Eye Proteins - chemistry ; Eye Proteins - genetics ; Genetic Engineering ; Insect Proteins - chemistry ; Insect Proteins - genetics ; Insect Proteins - pharmacology ; Insect Proteins - physiology ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Molecular Sequence Data ; Nerve Tissue Proteins - chemistry ; Nerve Tissue Proteins - genetics ; Neuregulins ; Phenotype ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - pharmacology ; Research Communication ; Sequence Alignment ; Sequence Homology, Amino Acid ; Wings, Animal - anatomy & histology ; Wings, Animal - drug effects</subject><ispartof>Genes & development, 1998-04, Vol.12 (7), p.908-913</ispartof><rights>Copyright © 1998, Cold Spring Harbor Laboratory Press 1998</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-13e583b6ed05f8de475e99b00db18479e292113071478bdece764b77dcd8f0953</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC316677/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC316677/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9531530$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schnepp, B</creatorcontrib><creatorcontrib>Donaldson, T</creatorcontrib><creatorcontrib>Grumbling, G</creatorcontrib><creatorcontrib>Ostrowski, S</creatorcontrib><creatorcontrib>Schweitzer, R</creatorcontrib><creatorcontrib>Shilo, B Z</creatorcontrib><creatorcontrib>Simcox, A</creatorcontrib><title>EGF domain swap converts a drosophila EGF receptor activator into an inhibitor</title><title>Genes & development</title><addtitle>Genes Dev</addtitle><description>In Drosophila the function of the epidermal growth factor (EGF) receptor is modulated zygotically by three EGF-like proteins: Spitz (Spi), which is a potent activator; Vein (Vn), which is a moderate activator; and Argos (Aos), which is an inhibitor. 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These results demonstrate that the EGF domain is the key determinant that gives DER inhibitors and activators their distinct properties.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Drosophila - genetics</subject><subject>Drosophila Proteins</subject><subject>Epidermal Growth Factor - chemistry</subject><subject>Epidermal Growth Factor - genetics</subject><subject>Epidermal Growth Factor - physiology</subject><subject>ErbB Receptors - agonists</subject><subject>ErbB Receptors - antagonists & inhibitors</subject><subject>ErbB Receptors - drug effects</subject><subject>Eye - anatomy & histology</subject><subject>Eye - drug effects</subject><subject>Eye Proteins - chemistry</subject><subject>Eye Proteins - genetics</subject><subject>Genetic Engineering</subject><subject>Insect Proteins - chemistry</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - pharmacology</subject><subject>Insect Proteins - physiology</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - genetics</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Neuregulins</subject><subject>Phenotype</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - pharmacology</subject><subject>Research Communication</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Wings, Animal - anatomy & histology</subject><subject>Wings, Animal - drug effects</subject><issn>0890-9369</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkb1PwzAQxT2ASilsrEiZmGg4x4k_BgZUtQUJwQKz5cROa5TEwU6L-O9x1aqCieks3-_53vkhdIUhxRjw3UrpFGcpSwXwEzQGLmAqCBVn6DyEDwCgQOkIjURBcEFgjF7my0WiXatsl4Qv1SeV67bGDyFRifYuuH5tG5XsKG8q0w_OJ6oa7FbtTrYbXKK6WNe2tPHmAp3Wqgnm8lAn6H0xf5s9Tp9fl0-zh-dplYMYppiYgpOSGg1FzbXJWWGEKAF0iXnOhMlEhjEBhnPGSx0HM5qXjOlK8xqi-Qm637_bb8rW6Mp0g1eN7L1tlf-WTln5t9PZtVy5rSSYUsai_uag9-5zY8IgWxsq0zSqM24TJBOMcRI9_gdimmdFxneObvdgFX8teFMfzWCQu2xkzEbiTDIZs4n49e8FjvAhGPIDmJuNLg</recordid><startdate>19980401</startdate><enddate>19980401</enddate><creator>Schnepp, B</creator><creator>Donaldson, T</creator><creator>Grumbling, G</creator><creator>Ostrowski, S</creator><creator>Schweitzer, R</creator><creator>Shilo, B Z</creator><creator>Simcox, A</creator><general>Cold Spring Harbor Laboratory 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>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19980401</creationdate><title>EGF domain swap converts a drosophila EGF receptor activator into an inhibitor</title><author>Schnepp, B ; 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Vein (Vn), which is a moderate activator; and Argos (Aos), which is an inhibitor. Chimeric molecules were constructed in which the EGF domain of Vn was swapped with the EGF domain from each factor. The modified Vn proteins behaved both in vitro and in vivo with properties characteristic of the factor from which the EGF domain was derived. These results demonstrate that the EGF domain is the key determinant that gives DER inhibitors and activators their distinct properties.</abstract><cop>United States</cop><pub>Cold Spring Harbor Laboratory Press</pub><pmid>9531530</pmid><doi>10.1101/gad.12.7.908</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0890-9369 |
| ispartof | Genes & development, 1998-04, Vol.12 (7), p.908-913 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Amino Acid Sequence Animals Drosophila - genetics Drosophila Proteins Epidermal Growth Factor - chemistry Epidermal Growth Factor - genetics Epidermal Growth Factor - physiology ErbB Receptors - agonists ErbB Receptors - antagonists & inhibitors ErbB Receptors - drug effects Eye - anatomy & histology Eye - drug effects Eye Proteins - chemistry Eye Proteins - genetics Genetic Engineering Insect Proteins - chemistry Insect Proteins - genetics Insect Proteins - pharmacology Insect Proteins - physiology Membrane Proteins - chemistry Membrane Proteins - genetics Molecular Sequence Data Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - genetics Neuregulins Phenotype Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - pharmacology Research Communication Sequence Alignment Sequence Homology, Amino Acid Wings, Animal - anatomy & histology Wings, Animal - drug effects |
| title | EGF domain swap converts a drosophila EGF receptor activator into an inhibitor |
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