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The flightless I protein localizes to actin‐based structures during embryonic development
Author(s) -
Davy Deborah A,
Ball Eldon E,
Matthaei Klaus I,
Campbell Hugh D,
Crouch Michael F
Publication year - 2000
Publication title -
immunology and cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.999
H-Index - 104
eISSN - 1440-1711
pISSN - 0818-9641
DOI - 10.1046/j.1440-1711.2000.00926.x
Subject(s) - drosophila melanogaster , biology , microbiology and biotechnology , cytoskeleton , actin , actin cytoskeleton , gelsolin , actin remodeling , homology (biology) , drosophilidae , genetics , gene , cell
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 .