Fig. 1: ERK3 is a novel binding partner of FBXW7.
From: FBXW7-mediated ERK3 degradation regulates the proliferation of lung cancer cells
a Interaction screening of FBXW7 and kinases by mammalian two-hybrid assay. The interaction strengths between FBXW7 and each of the indicated kinases were assessed by measuring pG5-luciferase activity. The data are from a triplicate experiment and were normalized by Renilla luciferase activity. The values are shown ±SEMs. Significance; *p < 0.001 vs. pACT-mock control cells (Student’s t test). b Confirmation of the interaction between ERK3 and FBXW7. The interaction of FBXW7 and ERK3 was confirmed by IP (HEK293T cell lysate, 400 μg/lane). c ERK3 interacted with cullin 1. The participation of ERK3 in a cullin 1 complex was confirmed by IP (HEK293T cell lysate, 400 μg/lane). d Specificity of the ERK3 binding of cullin members. Specific ERK3 binding with cullin members was evaluated by IP. e ERK3 bound specifically to FBXW7 among FBXW subfamily members. Specific binding between ERK3 and FBXW subfamily members was evaluated by IP. f Specific ERK3 binding with FBXW7 and FBXO subfamily members. Specific ERK3 binding with FBXW7 and FBXO subfamily members was evaluated by IP. b–f β-Actin was used as the internal control to ensure equal protein loading. WCL, whole-cell lysate.
