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. 2016 Jun 24;44(13):6318–6334. doi: 10.1093/nar/gkw565

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© The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — 4E-T interacts with UNR, which in turn binds unrip. (A) Cartoon of UNR and unrip proteins, indicating their domains and the C-terminal unrip-binding site in UNR. (B) Anti-FLAG immunoprecipitations were carried out using FLAG-tagged GFP, -UNR, -UNRΔC, -unrip and -DDX6. UNRΔC is a C-terminally truncated version of UNR predicted not to interact with unrip. UT, untransfected cells. (C and D) HEK293T were co-transfected with siRNA against β-globin (control), DDX6, UNR or unrip as indicated, and with FLAG-4E-T, or not transfected (UT). Input and bound samples were analysed by western blot with indicated antibodies. (E) Schematic cartoon of interaction sites of 4E-T-binding proteins. Region A is 694–716, conserved in 4E-T proteins, part of the P- body localization sequences (26). Interactions shown in this study: solid line—interactions displayed by deletion and truncated fragments of 4E-T, as well as by FLAG-tagged UNR, -unrip and -DDX6. Brackets indicate regions of interactions with indicated proteins displayed by truncated fragments of 4E-T. Dotted grey line, interactions shown by FLAG-tagged UNR, -unrip and -DDX6. Arrows indicate bait identity. Interactions solved structurally in other studies: the canonical and non-canonical 4E-T-eIF4E binding sites (8) and 4E-T-DDX6-CNOT1 (36).