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. 2015 Apr 18;6(15):13019–13035. doi: 10.18632/oncotarget.3864

Figure 4. Mutation of hIRE1 Y628 enhances autophosphorylation.

Figure 4

A. Autophosphorylation of hIRE1 wild-type (wt) and Y628 mutants measured by DELFIA assay. Results are color-coded by protein variant, protein concentration and presence or absence of ATP at 100 μM ATP. Black lines - absence of ATP. Green - wt IRE1 at 700 nM. Dark and light red – IRE1 Tyr628Phe at 1400 nM and 700 nM, respectively. Dark blue and light blue – Tyr628Leu at 1400 nM and 700 nM, respectively. B. View of the conformational changes between the ADP-hIRE1 structure (pink carbon atoms) and the apo-hIRE1 structure in the vicinity of Tyr628. Note that Asp620 in the αC-β4 linker moves by ~8 Å upon back-to-back dimer formation, and forms salt-bridge interactions with Arg594 and Arg627 from a second molecule of hIRE1 in the back-to-back dimer interface.