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. 2014 May 1;10(5):e1004102. doi: 10.1371/journal.ppat.1004102

Figure 7. Two adjacent residues located at the E4-ORF1 carboxyl-terminus determine binding to both PI3K and Dlg1.

Figure 7

(A) E4-ORF1 mutant KI is defective in binding to both PI3K and Dlg1. Co-IP assays were conducted with the indicated MCF10A lines as described in the legend to Figure 5. Vertical lines denote removal of extraneous sample lanes. (B) The location of the KI residues at the extreme carboxyl-terminus of E4-ORF1, along with their close proximity to the PBM and overlap with the TRI element, is shown. Also illustrated is that the KI residues determine PI3K binding; both the KI residues and the PBM element, defined by residues TLV, determine Dlg1 binding; and the TRI element, defined by residues VKI, determines E4-ORF1 homo-trimerization.