Fig. 3: PTENα/β-NTE interacts with the WDR5 WIN site solely through the SSSRRSS WIN motif.
From: The NTE domain of PTENα/β promotes cancer progression by interacting with WDR5 via its SSSRRSS motif
A–D ITC binding curves for the titration of wild-type PTENα-NTE to different mutants of WDR5 (A, B) or different mutants of PTENα-NTE to wild-type WDR5 (C, D) by iTC-200 microcalorimeter (MicroCal, Inc.). E–G Mutation of the interacting residues affected the interaction between PTENα-NTE1–173 or full-length PTENα1–576 and WDR522–334. In vitro GST pulldown of wild-type WDR5 with wild-type or mutant of PTENα-NTE (E) or full-length PTENα (F), and wild-type or F133A/263A (WDR5-2A) mutant WDR5 with wild-type PTENα-NTE and full-length PTENα (G). Bacterially expressed proteins PTENα-NTE (E, G) or full length PTENα (F, G) and their mutants, as indicated, were incubated with GST or GST-tagged WDR5, followed by GST pulldown and CBB staining, with the specific binding indicated by an arrow. Kd: dissociation constants (μM); NB: no detectable binding; WB: weak binding; 2A: PTENα-NTE_R118A/R119A; 5A: PTENα-NTE_115–119-5A; 7A: PTENα-NTE_115–119-5A_R135A/R144A; CBB Coomassie brilliant blue.
