Your browser doesn't support javascript.
loading
Drosophila coracle, a member of the protein 4.1 superfamily, has essential structural functions in the septate junctions and developmental functions in embryonic and adult epithelial cells.
Lamb, R S; Ward, R E; Schweizer, L; Fehon, R G.
Afiliación
  • Lamb RS; Developmental, Cellular, and Molecular Biology Group, Duke University, Durham, North Carolina 27708-1000, USA.
Mol Biol Cell ; 9(12): 3505-19, 1998 Dec.
Article en En | MEDLINE | ID: mdl-9843584
ABSTRACT
Although extensively studied biochemically, members of the Protein 4. 1 superfamily have not been as well characterized genetically. Studies of coracle, a Drosophila Protein 4.1 homologue, provide an opportunity to examine the genetic functions of this gene family. coracle was originally identified as a dominant suppressor of EgfrElp, a hypermorphic form of the Drosophila Epidermal growth factor receptor gene. In this article, we present a phenotypic analysis of coracle, one of the first for a member of the Protein 4. 1 superfamily. Screens for new coracle alleles confirm the null coracle phenotype of embryonic lethality and failure in dorsal closure, and they identify additional defects in the embryonic epidermis and salivary glands. Hypomorphic coracle alleles reveal functions in many imaginal tissues. Analysis of coracle mutant cells indicates that Coracle is a necessary structural component of the septate junction required for the maintenance of the transepithelial barrier but is not necessary for apical-basal polarity, epithelial integrity, or cytoskeletal integrity. In addition, coracle phenotypes suggest a specific role in cell signaling events. Finally, complementation analysis provides information regarding the functional organization of Coracle and possibly other Protein 4.1 superfamily members. These studies provide insights into a range of in vivo functions for coracle in developing embryos and adults.
Asunto(s)

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Neuropéptidos / Proteínas de Insectos / Proteínas del Citoesqueleto / Drosophila / Proteínas de la Membrana Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Mol Biol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 1998 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Neuropéptidos / Proteínas de Insectos / Proteínas del Citoesqueleto / Drosophila / Proteínas de la Membrana Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Mol Biol Cell Asunto de la revista: BIOLOGIA MOLECULAR Año: 1998 Tipo del documento: Article País de afiliación: Estados Unidos