Merlin kauffman domainer
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Studies in Drosophila demonstrate that the receptor tyrosine kinases Sevenless and the EGF receptor homologue are localized to the apical junctional complex and enriched at the adherens junction ( Tomlinson et al., 1987 Zak and Shilo, 1992). The molecular characterization of numerous proteins that function within an array of signaling pathways has revealed that the junctional complex is a primary site for cellular interactions. The septate junction, characterized by ladder-like septa in electron micrographs, is an invertebrate specific junction which has been proposed, based upon similar molecular components, to be functionally analogous to the vertebrate tight junction ( Willott et al., 1993). In Drosophila and other invertebrate epithelia, the apicolateral junctional complex consists of an apical adherens junction and a more basal septate junction ( Poodry and Schneiderman, 1970 Tepass and Hartenstein, 1994). Epithelial tissues exhibit an apicobasal polarity with the apical domain separated from the basolateral domain by a junctional complex. Together these results indicate that Coracle provides essential membrane-organizing functions at the septate junction, and that these functions are carried out by an amino-terminal domain that is conserved in all protein 4.1 superfamily members.Ĭ ell–cell communication within an epithelium plays vital roles in the maintenance of epithelial character and in correct specification of cell fate. Consistent with this notion, immunoprecipitation and in vitro binding studies demonstrate that the amino-terminal 383 amino acids of Coracle and cytoplasmic domain of Neurexin interact directly. Furthermore, the localization of Coracle and the transmembrane protein Neurexin to the septate junction display an interdependent relationship, suggesting that Coracle and Neurexin interact with one another at the cytoplasmic face of the septate junction. Genetic mutations within this domain disrupt the subcellular localization of Coracle and severely affect its genetic function, indicating that correct subcellular localization is essential for Coracle function.
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Using in vitro mutagenesis, we demonstrate that the amino-terminal 383 amino acids of Coracle define a functional domain that is both necessary and sufficient for proper septate junction localization in transgenic embryos. Coracle, a Drosophila protein 4.1 homologue, is required during embryogenesis and is localized to the cytoplasmic face of the septate junction in epithelial cells. The protein 4.1 superfamily is comprised of a diverse group of cytoplasmic proteins, many of which have been shown to associate with the plasma membrane via binding to specific transmembrane proteins.