Influenza A virus infection begins with the binding of viral hemagglutinin to sialyated host plasma membrane glycoprotein. Following endocytosis, viral particles are trafficked through early endosomes to late endosomes/lysosomes. In these compartments the conformation of HA is changed resulting in fusion of host-viral membranes and entry of viral ribonucleoproteins into the cytosol. We detected major changes in subcellular localization of Rasrelated small GTPases and vacuolar ATPases, which are involved in the regulation of endosomal recycling pathway and have recently been shown to be essential for influenza A virus replication [28] . Furthermore, it was shown that small molecule inhibitor of vacuolar ATPase can antagonize influenza A virus replication probably by inhibiting the entry of viral ribonucleoproteins to the cytosol. Interestingly, our secretome analysis showed that several Ras-related proteins, Rab-10, Rab-11A, Rab-1A, and Rap-2b as well as components of vacuolar ATPases, Vtype proton ATPases, are rapidly secreted in response to influenza A virus infection. The results suggest that these proteins are involved in protein secretion during influenza A virus infection.