High impact information on Vm32E

• A study was made of the localization and assembly of the VM32E protein, a putative vitelline membrane component of the Drosophila eggshell [1].
• During the terminal stages of oogenesis the VM32E protein is partially released from the vitelline membrane and becomes localized in the endochorion layer also [1].
• By analyzing transgenic flies carrying variously truncated VM32E proteins, we could identify the protein domains required for the proper assembly of the VM32E protein in the eggshell [1].
• Here, we show that this spatial restriction of VM32E gene expression is conserved in the D. pseudoobscura orthologous gene, suggestive of a conserved function of VM32E protein [2].
• The VM32E gene is not expressed in the centripetal migrating follicle cells, where the Decapentaplegic (Dpp) pathway is active in patterning the anterior eggshell structures [2].

Biological context of Vm32E

• In this paper we analyze the expression in follicular cells and regulation of the vitelline membrane protein gene we identified in region 32E of the second chromosome of D. melanogaster (VMP32E) [3].
• We report germ line transformation results obtained with different kinds of gene fusion leading to the identification of a follicular cell subpopulation involved in the expression of the VMP32E [3].
• Regulatory elements in the promoter of the vitelline membrane gene VM32E of Drosophila melanogaster direct gene expression in distinct domains of the follicular epithelium [4].
• Results from germ line transformation experiments using different fragments of the -465/-39 VM32E region fused to the hsp/lacZ reporter gene revealed that the region -348/-39 is sufficient to confer the wild-type expression pattern [4].
• Our previous work on the VM32E gene defined the promoter regions required for the control of gene expression in the ventral and dorsal follicle domains [5].

Anatomical context of Vm32E

• At least one vitelline membrane protein (Vm32E), specifically localized on the outer eggshell, is also evolving faster than other vitelline membrane proteins suggesting that all proteins localized on the outer eggshell may be evolving rapidly [6].
• We suggest that the expression of the VM32E gene throughout the follicular epithelium is controlled by specific cis-regulatory elements acting in distinct spatial domains and following a precise developmental program [4].

References