Rap1 Co-Localization with E-Cadherin and Beta-Intregrin During Drosophila Eye Development

The focus of this research is to understand how cell adhesion is regulated. Cell adhesion plays crucial roles in tissue compartmentalization, tissue rearrangement, and cell migration but the mechanisms that regulate these properties are not fully understood. Two of the proteins that give cells their adhesive properties are cadherins and integrins, which are both transmembrane proteins. Cadherins link cells within tissues and integrins mediate adhesion between cells and the extracellular matrix. The myospheroid gene encodes the Drosophila beta-integrin. Rap1 is a signaling protein that acts like a molecular switch. Previous studies have shown that Rap1, E-Cadherin and Myospheroid play crucial roles during Drosophila eye development, making this system suitable to study Rap1 regulation of both molecules in the same developmental context. Our recent studies suggest that Rap1 interacts genetically with both E-cadherin and myospheroid in the Drosophila eye. We hypothesize that Rap1 controls localization of both E-cadherin and Myospheroid to their respective subcellular domains, allowing the cells to switch between binding other cells and binding to the extracellular matrix.  To test this, we aim to determine the subcellular localization of Rap1 with respect to E-cadherin and Myospheroid. We extracted Drosophila larval eye discs from a fly strain carrying a Rap1-GFP fusion protein.  We stained the eye discs for E-cadherin and Myospheroid using immunofluorescence. Using confocal microscopy we were able to show that Rap1, Myospheroid, and E-cadherin co-localize within the cells, suggesting that Rap1 is in the right place to control localization of E-cadherin and Myospheroid.