Figure 1: 4E-BPs bind to a lateral surface of eIF4E.
From: 4E-BPs require non-canonical 4E-binding motifs and a lateral surface of eIF4E to repress translation
(a) Schematic representation of eIF4G and the 4E-BPs that were analyzed in this study. All the proteins contain a canonical (C) and a non-canonical (NC) 4E-BM. CUP and 4E-T contain a region with similarity to human 4E-transporter (4E-T) region. eIF4G contains a PABP-interacting region and MIF4G and MA3 domains. The amino-acid positions at the domain/motif boundaries are indicated below the protein outlines. (b) Cartoon representation of the overall structure of the eIF4E–CUP complex. eIF4E is shown in cyan and CUP in orange (PDB code 4AXG)27. Selected secondary structure elements are labeled in black for eIF4E and in orange for CUP. (c,d) Close-up views of the dorsal (c) and lateral (d) interfaces between eIF4E and CUP. Selected interface residues are shown as cyan and orange sticks for eIF4E and CUP, respectively. The eIF4E and CUP residues are labeled in black and orange, respectively, and underlined if they are mutated. (e–g) WB showing the interaction of HA–eIF4E (either WT or mutated) with GFP-tagged full-length 4E-BPs (CUP, Thor and 4E-T) and endogenous eIF4G. The size markers (kDa) are shown to the right of each panel. The original WB shown in this figure can be found in Supplementary Fig. 8.
