We stated a transgene encoding Vpu in various Drosophila tissues using the Gal4/UAS binary system. Ubiquitous expression of Vpu resulted in lethality in the first BAY 11-7082 BAY 11-7821 instar larval stage, thus showing that Vpu inhibits important developmental paths. In order to address more correctly which cellular functions were affected, we restricted Vpu expression to particular areas in the developing larval wing primordium applying engrailed Gal4 and decapentaplegic Gal4 transgenes which show Gal4 in the rear compartment and in a stripe of anterior compartment cells abutting the anteroposterior compartment border of the wing disc, respectively. In both cases, Vpu expression induced defects in the adult wing showing muscle damage and adjustment of patterning throughout development. The expressivity of Vpu induced phenotypes improved with the temperature, showing they be determined by Gal4 activity, which also increases with the temperature. Expression of Vpu with Papillary thyroid cancer the en Gal4 driver generated a reduced amount of the whole wing along with vein defects and additional tissue loss in the rear compartment. Under the same conditions, the size of the posterior compartment of the larval wing imaginal disc was reduced when compared to the wild-type. Phrase of Vpu with dpp Gal4 also led to loss of wing tissue, mostly in the anterior area, between longitudinal vein 2 and L3, including section of L3, as well as loss of the proximal cross vein between veins L3 and L4 connected with tissue loss between L3 L4. Consistent Tipifarnib molecular weight with this specific adult wing phenotype, a slight reduction of the anterior area of the wing pouch was also seen in the corresponding wing imaginal discs. Nevertheless, in these same discs, the stripe of dpp expression appeared widened, specifically in two regions of the wing pouch. Developmental disorders were also apparent in the adult eye utilizing the GMR Gal4 driver. The appearance of the viral protein Vpu throughout Drosophila development thus caused phenotypic defects in different cell types. In eye and wing, Vpu expression results in a reduction in the size of the body by which it was expressed, suggesting that it possibly induced cell death or reduced growth and cell proliferation. bThe above effects suggested that Vpu interacts with one or more Drosophila meats thereby interfering with their normal function. We tested whether Vpu interacts with the fly b TrCP homolog, SLIMB, since many known functions of Vpu are due to its connection with the human b TrCP. In human cells, the Vpu/b TrCP discussion requires phosphorylation of Ser56 and Vpu Ser52 and the primary Wd-40 repeat of w TrCP. Using equally a yeast two hybrid and a co immunoprecipitation assay, we showed that Vpu interacts with the primary WD area of SLIMB, and that this interaction is abolished when using a low phosphorylatable mutant type of Vpu, Vpu2 6, which is incapable of binding w TrCP.