Genetic and molecular characterization of a Notch mutation in its Delta- and Serrate-binding domain in Drosophila

The Drosophila Notch gene product is a transmembrane protein that functions as a receptor of intercellular signals in several Drosophila developmental processes. Two other transmembrane proteins, encoded by the genes Delta and Serrate, genetically and molecularly behave as Notch ligands. All these p...

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Detalles Bibliográficos
Autores: Celis, José F. de, Barrio, Rosa, Arco, Araceli del, García-Bellido, Antonio
Tipo de recurso: artículo
Fecha de publicación:1993
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/47841
Acceso en línea:http://hdl.handle.net/10261/47841
Access Level:acceso embargado
Palabra clave:Drosophila
Melanogaster
Notch
Gene
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repository_id_str
spelling Genetic and molecular characterization of a Notch mutation in its Delta- and Serrate-binding domain in DrosophilaCelis, José F. deBarrio, RosaArco, Araceli delGarcía-Bellido, AntonioDrosophilaMelanogasterNotchGeneThe Drosophila Notch gene product is a transmembrane protein that functions as a receptor of intercellular signals in several Drosophila developmental processes. Two other transmembrane proteins, encoded by the genes Delta and Serrate, genetically and molecularly behave as Notch ligands. All these proteins share the presence of epidermal growth factor (EGF)-like repeats in their extracellular domain. The Notch protein has 36 EGF-like repeats, 2 of which, numbers 11 and 12, are required for the interaction with the Delta and Serrate ligands. We have isolated and molecularly characterized a Notch mutation in its Delta- and Serrate-binding domain that behaves genetically as both a Notch antimorphic and a loss-of-function mutation. This mutation, NM1, carries a Glu-->Val substitution in the Notch EGF repeat 12. The NM1 allele interacts with other Notch alleles such as Abruptex and split and with mutations in the Notch-ligand genes Delta and Serrate. The basis for the genetic antimorphism of NM1 seems to reside in the titration of Notch wild-type products into NM1/N+ nonfunctional dimers and/or the titration of Delta products into nonfunctional ligand-receptor complexes.Peer reviewedNational Academy of Sciences (U.S.)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]201220121993info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501http://hdl.handle.net/10261/47841reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1073/pnas.90.9.4037Síinfo:eu-repo/semantics/embargoedAccessoai:digital.csic.es:10261/478412026-05-22T06:33:51Z
dc.title.none.fl_str_mv Genetic and molecular characterization of a Notch mutation in its Delta- and Serrate-binding domain in Drosophila
title Genetic and molecular characterization of a Notch mutation in its Delta- and Serrate-binding domain in Drosophila
spellingShingle Genetic and molecular characterization of a Notch mutation in its Delta- and Serrate-binding domain in Drosophila
Celis, José F. de
Drosophila
Melanogaster
Notch
Gene
title_short Genetic and molecular characterization of a Notch mutation in its Delta- and Serrate-binding domain in Drosophila
title_full Genetic and molecular characterization of a Notch mutation in its Delta- and Serrate-binding domain in Drosophila
title_fullStr Genetic and molecular characterization of a Notch mutation in its Delta- and Serrate-binding domain in Drosophila
title_full_unstemmed Genetic and molecular characterization of a Notch mutation in its Delta- and Serrate-binding domain in Drosophila
title_sort Genetic and molecular characterization of a Notch mutation in its Delta- and Serrate-binding domain in Drosophila
dc.creator.none.fl_str_mv Celis, José F. de
Barrio, Rosa
Arco, Araceli del
García-Bellido, Antonio
author Celis, José F. de
author_facet Celis, José F. de
Barrio, Rosa
Arco, Araceli del
García-Bellido, Antonio
author_role author
author2 Barrio, Rosa
Arco, Araceli del
García-Bellido, Antonio
author2_role author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Drosophila
Melanogaster
Notch
Gene
topic Drosophila
Melanogaster
Notch
Gene
description The Drosophila Notch gene product is a transmembrane protein that functions as a receptor of intercellular signals in several Drosophila developmental processes. Two other transmembrane proteins, encoded by the genes Delta and Serrate, genetically and molecularly behave as Notch ligands. All these proteins share the presence of epidermal growth factor (EGF)-like repeats in their extracellular domain. The Notch protein has 36 EGF-like repeats, 2 of which, numbers 11 and 12, are required for the interaction with the Delta and Serrate ligands. We have isolated and molecularly characterized a Notch mutation in its Delta- and Serrate-binding domain that behaves genetically as both a Notch antimorphic and a loss-of-function mutation. This mutation, NM1, carries a Glu-->Val substitution in the Notch EGF repeat 12. The NM1 allele interacts with other Notch alleles such as Abruptex and split and with mutations in the Notch-ligand genes Delta and Serrate. The basis for the genetic antimorphism of NM1 seems to reside in the titration of Notch wild-type products into NM1/N+ nonfunctional dimers and/or the titration of Delta products into nonfunctional ligand-receptor complexes.
publishDate 1993
dc.date.none.fl_str_mv 1993
2012
2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/47841
url http://hdl.handle.net/10261/47841
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1073/pnas.90.9.4037
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/embargoedAccess
eu_rights_str_mv embargoedAccess
dc.publisher.none.fl_str_mv National Academy of Sciences (U.S.)
publisher.none.fl_str_mv National Academy of Sciences (U.S.)
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,198674

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