The BAR domain of amphiphysin is required for cleavage furrow tip–tubule formation during cellularization inDrosophilaembryos
The BAR domain of amphiphysin is required for cleavage furrow tip–tubule formation during cellularization inDrosophilaembryos
De novo formation of cells in the Drosophila embryo is achieved when each nucleus is surrounded by a furrow of plasma membrane. Remodeling of the plasma membrane during cleavage furrow ingression involves the exocytic and endocytic pathways, including endocytic tubules that form at cleavage furrow tips (CFT-tubules). The tubules are marked by amphiphysin but are otherwise poorly understood. Here we identify the septin family of GTPases as new tubule markers. Septins do not decorate CFT-tubules homogeneously: instead, novel septin complexes decorate different CFT-tubules or different domains of the same CFT-tubule. Using these new tubule markers, we determine that all CFT-tubule formation requires the BAR domain of amphiphysin. In contrast, dynamin activity is preferentially required for the formation of the subset of CFT-tubules containing the septin Peanut. The absence of tubules in amphiphysin-null embryos correlates with faster cleavage furrow ingression rates. In contrast, upon inhibition of dynamin, longer tubules formed, which correlated with slower cleavage furrow ingression rates. These data suggest that regulating the recycling of membrane within the embryo is important in supporting timely furrow ingression.
- Hospital for Sick Children Canada
- University of Toronto Canada
Dynamins, Embryo, Nonmammalian, Microfilament Proteins, Nerve Tissue Proteins, Articles, Endocytosis, Actin Cytoskeleton, Kinetics, Protein Transport, Drosophila melanogaster, Animals, Drosophila Proteins, Female, Protein Interaction Domains and Motifs, Biomarkers, Septins
Dynamins, Embryo, Nonmammalian, Microfilament Proteins, Nerve Tissue Proteins, Articles, Endocytosis, Actin Cytoskeleton, Kinetics, Protein Transport, Drosophila melanogaster, Animals, Drosophila Proteins, Female, Protein Interaction Domains and Motifs, Biomarkers, Septins
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