Specific domains drive VM32E protein distribution and integration in Drosophila eggshell layers

A study was made of the localization and assembly of the VM32E protein, a p utative vitelline membrane component of the Drosophila eggshell. The result s highlight some unique features of this protein compared with the other pr oteins of the same gene family. At the time of its synthesis (stage 10), th e VM32E protein is not detectable in polar follicle cells. However, it is a ble to move in the extracellular space around the oocyte and, by stage 11 i s uniformly distributed in the vitelline membrane. During the terminal stag es of oogenesis the VM32E protein is partially released from the vitelline membrane and becomes localized in the endochorion layer also. By analyzing transgenic flies carrying variously truncated VM32E proteins, we could iden tify the protein domains required for the proper assembly of the VM32E prot ein in the eggshell. The highly conserved vitelline membrane domain is impl icated in the early interactions with other components and is required for cross-linking VM32E protein in the vitelline membrane. The terminal carboxy lic domain is necessary for localization to the endochorion layer. Protein with the C-end domain deleted is localized solely to the vitelline membrane and cross-linked only in laid eggs, as occurs for the other vitelline memb rane proteins.