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. Author manuscript; available in PMC: 2013 Nov 20.
Published in final edited form as: Mol Biosyst. 2010 Oct 4;7(2):10.1039/c0mb00074d. doi: 10.1039/c0mb00074d

Fig. 4.

Fig. 4

Degradation of the ER by PROTACs is proteasome-dependent and E3 ligase recognition residue-dependent. A. PROTAC-mediated ER degradation is inhibited in a dose-dependent manner by the general proteasome inhibitor, epoxomicin. B. The hydroxyproline residue is critical for pVHL recognition of the PROTAC, as a mutant containing norleucine (17) is unable to degrade the ER. C. Immunofluorescence data supporting the western blotting results of A and B. Epoxomicin causes the accumulation of the ER (green), while 17 does not cause ER degradation when compared to controls. Blue staining (DAPI) indicates the nucleus.