The flightless I protein localizes to actin-based structures during embryonic development
Date
2000
Authors
Davy, Deborah
Ball, Eldon
Matthaei, Klaus
Campbell, Hugh
Crouch, Michael F
Journal Title
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Volume Title
Publisher
Blackwell Publishing Ltd
Abstract
The product of the flightless I gene is predicted to provide a link between molecules of an as yet unidentified signal transduction pathway and the actin cytoskeleton. Previous work has shown that weak and severe mutations of the flightless I locus in Drosophila melanogaster cause disruption in the indirect flight muscles and in embryonic cellularization events, respectively, indicative of a regulatory role for the flightless I protein in cytoskeletal rearrangements. A C-terminal domain within flightless I with significant homology to the gelsolin-like family of actin-binding proteins has been identified, but evidence of a direct interaction between endogenous flightless I and actin remains to be shown. In the present study, chick, mouse and Drosophila melanogaster embryos have been examined and the localization of flightless I investigated in relation to the actin cytoskeleton. It is shown that flightless I localization is coincident with actin-rich regions in parasympathetic neurons harvested from chicks, in mouse blastocysts and in structures associated with cellularization in Drosophila melanogaster.
Description
Keywords
Keywords: actin; gene product; actin filament; animal cell; article; controlled study; cytoskeleton; Drosophila melanogaster; embryo; embryo development; nonhuman; protein binding; protein localization; signal transduction; 3T3 Cells; Actins; Animals; Blotting, Wes Actin; Cytoskeleton; Development; Drosophila melanogaster; Flightless I; Neuron
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Source
Immunology and Cell Biology
Type
Journal article
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DOI
10.1046/j.1440-1711.2000.00926.x
Restricted until
2037-12-31