The lethal myospheroid gene of Drosophila encodes a membrane protein homologous to vertebrate integrin beta subunits
A mutant of Drosophila melanogaster carrying the lethal(1) myospheroid mutation [l(1)mys] has a defective musculature and a phenotype that suggests a defect of basement membranes. The genomic region that is interrupted by an insertion in a mutant carrying l(1)mys was used to isolate cDNA clones, and...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1988-04, Vol.85 (8), p.2633-2637 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | MacKrell, A.J Blumberg, B Haynes, S.R Fessler, J.H |
| description | A mutant of Drosophila melanogaster carrying the lethal(1) myospheroid mutation [l(1)mys] has a defective musculature and a phenotype that suggests a defect of basement membranes. The genomic region that is interrupted by an insertion in a mutant carrying l(1)mys was used to isolate cDNA clones, and their sequences are presented here. The cDNA sequence predicts a cysteine-rich integral membrane protein that displays 45% sequence identity to chicken integrin and the human fibronectin receptor β subunit and much greater similarity over localized segments. These similarities extend to other vertebrate integrin β subunits, and we conclude that the myospheroid protein is an integrin β subunit of Drosophila. This implies evolutionary conservation of a group of transmembrane proteins that are receptors for extracellular matrix and, coupled with the myospheroid phenotype, indicates an important role for the interaction of cells with extracellular matrix during development. |
| doi_str_mv | 10.1073/pnas.85.8.2633 |
| format | Article |
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The genomic region that is interrupted by an insertion in a mutant carrying l(1)mys was used to isolate cDNA clones, and their sequences are presented here. The cDNA sequence predicts a cysteine-rich integral membrane protein that displays 45% sequence identity to chicken integrin and the human fibronectin receptor β subunit and much greater similarity over localized segments. These similarities extend to other vertebrate integrin β subunits, and we conclude that the myospheroid protein is an integrin β subunit of Drosophila. 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The genomic region that is interrupted by an insertion in a mutant carrying l(1)mys was used to isolate cDNA clones, and their sequences are presented here. The cDNA sequence predicts a cysteine-rich integral membrane protein that displays 45% sequence identity to chicken integrin and the human fibronectin receptor β subunit and much greater similarity over localized segments. These similarities extend to other vertebrate integrin β subunits, and we conclude that the myospheroid protein is an integrin β subunit of Drosophila. This implies evolutionary conservation of a group of transmembrane proteins that are receptors for extracellular matrix and, coupled with the myospheroid phenotype, indicates an important role for the interaction of cells with extracellular matrix during development.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cell Adhesion</subject><subject>Chickens</subject><subject>CLONE</subject><subject>CLONES</subject><subject>Cloning, Molecular</subject><subject>CODE GENETIQUE</subject><subject>CODIGO GENETICO</subject><subject>Complementary DNA</subject><subject>DESARROLLO EMBRIONARIO</subject><subject>DEVELOPPEMENT EMBRYONNAIRE</subject><subject>DNA - genetics</subject><subject>DROSOPHILA</subject><subject>DROSOPHILA MELANOGASTER</subject><subject>Drosophila melanogaster - genetics</subject><subject>EMBRYONIC DEVELOPMENT</subject><subject>Extracellular matrix</subject><subject>Extracellular Matrix - physiology</subject><subject>GENE LETAL</subject><subject>Genes</subject><subject>GENES LETALES</subject><subject>GENETIC CODE</subject><subject>Integrins</subject><subject>LETHAL GENES</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane proteins</subject><subject>Membrane Proteins - genetics</subject><subject>Molecular Sequence Data</subject><subject>Muscles - embryology</subject><subject>Muscles - physiology</subject><subject>MUTANT</subject><subject>MUTANTES</subject><subject>MUTANTS</subject><subject>NUCLEOTIDE</subject><subject>NUCLEOTIDES</subject><subject>NUCLEOTIDOS</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>Receptors</subject><subject>Vertebrates</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkE1v1DAYhC0EKkvLlQMSkk_cEvwRx84RlY8iVeqh7dmys683qZw42A6i_75e7VL20JMP88y840HoAyU1JZJ_WWaTaiVqVbOW81doQ0lHq7bpyGu0IYTJSjWseYvepfRACOmEImfojFOmZMc2KN8NgD3kwXg8PYa0DBDDuMU7mAEHh7_FkMIyjN5gmPuwhYQNnmCy0RRgiSHDOOMhTMGHXVgTzgH_gZihABnwOGfYxUJYyAan1a7zmNMFeuOMT_D--J6j-x_f7y6vquubn78uv15XfaNkrhRXQrKe9C30znAheMeI4K2zTGxl33JmWds2ijZgKBDHHLWKAZHWNNYSy8_R50Nu6fl7hZT1NKYevC_dS1ctFZWMCV7A-gD25bspgtNLHCcTHzUlej-z3s-sldBK72cuhk_H5NVOsH3Gj7ueXN77_qnPfu1W7zP8zSdBL4JF_3jQH1IO8eROo7r_ojNBm7Jz0ve3qsxGVcufAP7Bo6s</recordid><startdate>19880401</startdate><enddate>19880401</enddate><creator>MacKrell, A.J</creator><creator>Blumberg, B</creator><creator>Haynes, S.R</creator><creator>Fessler, J.H</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>FBQ</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>7X8</scope></search><sort><creationdate>19880401</creationdate><title>The lethal myospheroid gene of Drosophila encodes a membrane protein homologous to vertebrate integrin beta subunits</title><author>MacKrell, A.J ; Blumberg, B ; Haynes, S.R ; Fessler, J.H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c487t-838572c0c6ecfa3553920536fb25d7c632b2664814ea1e0f2f1b82e07ba4bb0b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Cell Adhesion</topic><topic>Chickens</topic><topic>CLONE</topic><topic>CLONES</topic><topic>Cloning, Molecular</topic><topic>CODE GENETIQUE</topic><topic>CODIGO GENETICO</topic><topic>Complementary DNA</topic><topic>DESARROLLO EMBRIONARIO</topic><topic>DEVELOPPEMENT EMBRYONNAIRE</topic><topic>DNA - genetics</topic><topic>DROSOPHILA</topic><topic>DROSOPHILA MELANOGASTER</topic><topic>Drosophila melanogaster - genetics</topic><topic>EMBRYONIC DEVELOPMENT</topic><topic>Extracellular matrix</topic><topic>Extracellular Matrix - physiology</topic><topic>GENE LETAL</topic><topic>Genes</topic><topic>GENES LETALES</topic><topic>GENETIC CODE</topic><topic>Integrins</topic><topic>LETHAL GENES</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane proteins</topic><topic>Membrane Proteins - genetics</topic><topic>Molecular Sequence Data</topic><topic>Muscles - embryology</topic><topic>Muscles - physiology</topic><topic>MUTANT</topic><topic>MUTANTES</topic><topic>MUTANTS</topic><topic>NUCLEOTIDE</topic><topic>NUCLEOTIDES</topic><topic>NUCLEOTIDOS</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>Receptors</topic><topic>Vertebrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MacKrell, A.J</creatorcontrib><creatorcontrib>Blumberg, B</creatorcontrib><creatorcontrib>Haynes, S.R</creatorcontrib><creatorcontrib>Fessler, J.H</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MacKrell, A.J</au><au>Blumberg, B</au><au>Haynes, S.R</au><au>Fessler, J.H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The lethal myospheroid gene of Drosophila encodes a membrane protein homologous to vertebrate integrin beta subunits</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1988-04-01</date><risdate>1988</risdate><volume>85</volume><issue>8</issue><spage>2633</spage><epage>2637</epage><pages>2633-2637</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>A mutant of Drosophila melanogaster carrying the lethal(1) myospheroid mutation [l(1)mys] has a defective musculature and a phenotype that suggests a defect of basement membranes. The genomic region that is interrupted by an insertion in a mutant carrying l(1)mys was used to isolate cDNA clones, and their sequences are presented here. The cDNA sequence predicts a cysteine-rich integral membrane protein that displays 45% sequence identity to chicken integrin and the human fibronectin receptor β subunit and much greater similarity over localized segments. These similarities extend to other vertebrate integrin β subunits, and we conclude that the myospheroid protein is an integrin β subunit of Drosophila. This implies evolutionary conservation of a group of transmembrane proteins that are receptors for extracellular matrix and, coupled with the myospheroid phenotype, indicates an important role for the interaction of cells with extracellular matrix during development.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>3128792</pmid><doi>10.1073/pnas.85.8.2633</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1988-04, Vol.85 (8), p.2633-2637 |
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| source | MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; JSTOR |
| subjects | Amino Acid Sequence Amino acids Animals Base Sequence Cell Adhesion Chickens CLONE CLONES Cloning, Molecular CODE GENETIQUE CODIGO GENETICO Complementary DNA DESARROLLO EMBRIONARIO DEVELOPPEMENT EMBRYONNAIRE DNA - genetics DROSOPHILA DROSOPHILA MELANOGASTER Drosophila melanogaster - genetics EMBRYONIC DEVELOPMENT Extracellular matrix Extracellular Matrix - physiology GENE LETAL Genes GENES LETALES GENETIC CODE Integrins LETHAL GENES Membrane Glycoproteins - genetics Membrane proteins Membrane Proteins - genetics Molecular Sequence Data Muscles - embryology Muscles - physiology MUTANT MUTANTES MUTANTS NUCLEOTIDE NUCLEOTIDES NUCLEOTIDOS PROTEINAS PROTEINE PROTEINS Receptors Vertebrates |
| title | The lethal myospheroid gene of Drosophila encodes a membrane protein homologous to vertebrate integrin beta subunits |
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