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. Author manuscript; available in PMC: 2018 Nov 20.
Published in final edited form as: Curr Biol. 2017 Nov 2;27(22):3454–3467.e8. doi: 10.1016/j.cub.2017.10.014

Figure 6. PER is stabilized in β-Trcp1/2 double mutant cells.

Figure 6

(A) PER stability was measured after CHX treatment. Data are mean+/-SEM, n=3 each. (B) PER can be robustly ubiquitinated in the β-Trcp1/2 double mutant cells. PER degradation and ubiquitination were induced by b-AP15 treatment as in control cells. The arrow in the bottom blots indicates the boundary between stacking and resolving gel. (C) β-TRCP is in excess to PER. Per2Luc homozygous knockin MEFs were used for the wt control, but wt Per2 allele (+/+) was used for β-Trcp2 ko cells. Note that endogenous and exogenous PER2 proteins are different in size in wt control cells but the same in the mutant cells. (D) Hyperphosphorylated PER is more unstable. Comparable amounts of hypo-and hyperphosphorylated PER2 was expressed in the inducible Per2 MEFs before CHX treatment. The solid and broken lines represent hypo- and hyper-phosphorylated PER2 samples, respectively. Mean+/-SEM, n=3.