As illustrated in Figure 8, the SLC39A14- mediated inhibitory effect may be due to the direct action of the transported Zn or to an indirect one via unidentified molecular chaperone that receives Zn through SLC39A14 and provides it to PDE. Since GPCRs are expressed in numerous Rapamycin tissues, the Slc39a14-KO mice may be useful for studying GPCRmediated biological events. Further studies on the mechanism by which SLC39A14 provides Zn to target molecules should help illuminate the regulation of GPCR-mediated signaling and Zn�C associated biological events. Rift Valley fever virus is an aerosol- and mosquitoborne virus endemic to sub-Saharan Africa. RVFV causes periodic, explosive epizootics, affecting livestock and humans. Sheep and cattle are particularly susceptible to the virus, with abortion rates approaching 100% and high mortality rates among young animals. Most humans infected with RVFV have a flulike illness. However, a small percentage of cases are more severe and include manifestations such as hemorrhagic disease and encephalitis. Despite the severity of the disease to the economy and human health, there are no USDA or FDAapproved therapeutic or prophylactic treatments. A better understanding of the RVFV replication cycle may lead to the identification of novel therapeutic targets. In this study, we have identified roles for each of the viral structural components in the assembly and release of RVFV and have identified a potential conserved target for therapeutic development. RVFV is a segmented, negative-sense RNA virus belonging to the family Bunyaviridae, genus Phlebovirus. The 12 kilobase genome is comprised of three segments termed L, M and S, which encode for the RNA-dependent RNA polymerase, envelope glycoproteins and nucleocapsid protein, respectively. The S and M segments also encode nonstructural proteins known as NSs and NSm, however these proteins are dispensable for RVFV replication in cell culture. Upon entry into host cells, the encapsidated genome and RdRp are released into the cytoplasm where transcription and replication of the viral genome occurs. RdRp acts as both transcriptase and replicase, but requires N for both activities. RdRp and N do not contain signal peptides, and are presumably translated on cytoplasmic ribosomes. The glycoproteins enter the secretory pathway as a precursor polyprotein, which is cleaved by signal peptidase to yield mature Gn and Gc. Gn and Gc form a complex and localize in steady-state to the Golgi apparatus, the site of virus assembly, due to a localization signal on Gn. It is not known how the encapsidated genome and RdRp are recruited to the Golgi apparatus for virus assembly or which viral components are involved in the Doxorubicin cellular release of virus.