The p.R393W variant in MRP2 facilitated protein degradation via the proteasomal pathway. (IMAGE)
Caption
(A–C) Half-life assay of the MRP2WT and MRP2R393W by using cycloheximide (CHX) to block protein synthesis and chase the remaining protein level by western blot at 0, 2.5, 5 and 7.5 hours. The half-life of MRP2WT was around 5 hours, whereas the MRP2R393W was almost depleted within 2.5 hours. Western blot (D–F) and immunofluorescence (G, H) results of MRP2WT and the MRP2R393W expression after MG132 treatment indicated that proteasome blockage MG132 accumulated MRP2R393W expression and attenuated the difference between the wild-type and mutant MRP2. (I, J) Whereas lysosome blockage chloroquine (CHL) failed to elevate the mutant MRP2 protein level. All data are expressed as mean±SEM Asterisks (*) represent statistically significant differences (**p<0.01, ****p<0.0001, n=3 replicates). ns, no significance.
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By Sun R, Chen Y, Zhu M, et al.
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