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. 2020 May 27;117(23):13023–13032. doi: 10.1073/pnas.2002567117

Fig. 1.

Fig. 1.

USP37 interacts with HIF2α and regulates HIF2α protein degradation. (A) Immunoblots of whole cell extracts (WCE) and immunoprecipitations (IP) from 293T cells transfected with Flag-tagged proteins as indicated and then treated with 10 μM MG132 under confluent condition. (B) Immunoblots of lysates from 293T cells transfected with HA-tagged proteins and then treated with 10 μM MG132 as indicated. Cells were treated under confluent condition to accumulate a high amount of HIF2α. (C) Immunoblots of lysates from 293T cells transfected with Flag-USP37 and then treated with 1 μM MLN4924 as indicated. (D) Immunoblots of lysates from 293T cells transfected with EV, WT, or CD form of USP37 and then treated with 1 μM MLN4924 as indicated. (E and F) Immunoblots of lysates from HA-VHL restored UMRC2 or 786-O cells infected with lentivirus encoding either EV, WT, or CD form of USP37 and then treated with 10 μM MG132 as indicated. (G–I) Immunoblots of WCE and IP from 786-O cells infected with lentivirus encoding either EV, HA-USP37, or Flag-HA-HIF2α as indicated. (J) Immunoblots of lysates from 293T cells transfected with EV, WT, or CD form of USP37 and then treated with 10 μg/mL CHX for indicated time. (K) Quantification of HIF2α expression level shown in J. (L and M) Immunoblots of WCE, nickel nitrilotriacetic acid (Ni-NTA) pull-down, or IP from 293T cells transfected with indicated plasmids and then treated with 10 μM MG132 as indicated.