Further analysis revealed that this signal was not transmitted to the downstream effector of Akt signalling, NF-kB. Cells were transfected with NF-kB reporter vector. Treatment of cells with Figure 1 . ACE2 binds an integrin. A) Evolutionary alignment of a part of the ACE2 amino acid sequence. ACE2 protein sequence conservation surrounding and including the proposed integrin binding site. Amino acids are shown as their one letter codes. The predicted integrin binding site is highlighted in red, whilst the homologous region in ACE is coloured blue. This alignment of the ACE2 protein sequence was taken from the Uniprot database. B) Immunoprecipitation of ITGB1 with ACE2 in HEK-ACE2. HEK cell lysates incubated with ITGB1 antibody and eluted using protein G. Immunoblotting for ACE2 was performed with anti-ACE2 antibody. C) Immunoprecipitation of ITGB1 and ITGA5 with ACE2 in Huh7 cell monolayers. Cell monolayers were cross-linked using DTBP before lysis and immunoprecipitation as before. D) Immunocytochemical detection of ACE2 and ITGB1 location in HEK-ACE2 cells. Cell imaging shows ACE2 (green) and ITGB1 (red) are located together (yellow) on the cell membrane of HEK-ACE2 cells. doi:10.1371/journal.pone.0034747.g001 sACE2 or ACE for between 2 and 24 h resulted in no significant change in luminescence compared to control (Figure 7 ). Furthermore, neither Ang II nor Ang-(1-7) had any significant effect (data not shown).