The flightless I protein localizes to actin-based structures during embryonic development.
DAVY, DEBORAH A 1; BALL, ELDON E 2; MATTHAEI, KLAUS I 3; CAMPBELL, HUGH D 2; CROUCH, MICHAEL F 1
[Article]
Immunology & Cell Biology.
78(4):423-429, August 2000.
(Format: HTML)
Summary: 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.
(C) 2000 University of Adelaide