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Immunol Cell Biol. 2000 Aug;78(4):423-9.

The flightless I protein localizes to actin-based structures during embryonic development.

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1
Molecular Signalling Group, Division of Neuroscience, Division of Biochemistry and Molecular Biology, John Curtin School of Medical Research, Ausralian National University, Canberra. Deb.Davy@anu.edu.au

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.

[Indexed for MEDLINE]

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