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. 2020 Jan 22;59(14):5595–5601. doi: 10.1002/anie.201913904

Figure 2.

Figure 2

Concentration‐ and time‐dependent degradation of PDEδ by PROTAC 3. A) Jurkat cells were treated for 24 or 48 h with 1 μm of PROTAC 1, 2, or 3 or DMSO as a control. Cells were lysed and proteins were subjected to immunoblotting using specific antibodies for PDEδ and β‐tubulin as a reference protein. B) Quantification of band intensities from (A). Data are mean values±SD (n=3). C) Panc Tu‐I cells were treated for 24 h with different concentrations of PROTAC 3 or 4 and DMSO as a control. Cells were lysed and proteins were subjected to immunoblotting using specific antibodies for PDEδ and β‐tubulin as a reference protein. D) Dose–response curve for PROTAC 3 mediated degradation of PDEδ as quantified by immunoblotting. Data are mean values±SD (n=3). E) Panc Tu‐I cells were treated for different time periods with 1 μm of the active PROTAC 3 or the inactive PROTAC 4. Cellular PDEδ levels are visualized using immunoblotting. F) Quantification of PDEδ abundance using immunoblotting after treatment with PROTAC 3. Data are mean values±SD (n=3). G) Panc Tu‐I cells were treated with 1 μm of PROTAC 3 and 10 μm of the proteasome inhibitor MG132 for 3 h. Cell lysate were subjected to immunoblotting to visualize PDEδ and β‐tubulin as a reference protein as described in (C).