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In  Drosophila melanogaster  M. (Diptera: Drosophilidae), a phospholipase-C to proteininase-C signal cascade leads to the endocytic uptake of yolk precursor molecules. The data suggest that  D. melanogaster  has a phospholipase-C/proteinkinase-C signaling pathway similar to that previously shown to be required for vitellogenesis in the milkweed bug,  Oncopeltus fasciatus  Dallas (Hemiptera: Lygaeidae). Calmodulin, derived from epithelial cells and transported to the oocytes via gap junctions, may trigger this pathway. To investigate this, a series of known antagonists to various elements of the pathway were used. W-7 (which prevents calmodulin binding to phospholipase-C), U-73122 (which prevents activation of phospholipase-C), verapamil (which blocks Ca 2+  release by IP3), HAG (which blocks diacylglycerol), and staurosporine (which inactivates proteinkinase-C) were each shown to inhibit endocytosis, thereby blocking formation of nascent yolk spheres.

journal of insect science

Vitellogenesis in the Fruit Fly,<i>Drosophila melanogaster:</i>Antagonists Demonstrate that the PLC, IP<sub>3</sub>/DAG, PK-C Pathway is Triggered by Calmodulin

Vitellogenesis in the Fruit Fly,Drosophila melanogaster:Antagonists Demonstrate that the PLC, IP3/DAG, PK-C Pathway is Triggered by Calmodulin

Vitellogenesis in the Fruit Fly,Drosophila melanogaster:Antagonists Demonstrate that the PLC, IP₃/DAG, PK-C Pathway is Triggered by Calmodulin