Fig. 4: Hypoxia induced transcriptional activity and proteasome-dependent degradation of ERRα via enhancing its acetylation in RCC cells. | Cell Death & Disease

Fig. 4: Hypoxia induced transcriptional activity and proteasome-dependent degradation of ERRα via enhancing its acetylation in RCC cells.

From: Hypoxia-triggered ERRα acetylation enhanced its oncogenic role and promoted progression of renal cell carcinoma by coordinating autophagosome-lysosome fusion

Fig. 4

A Western blot detected the protein levels of ERRα and HIF-2α in normal kidney cell and RCC cells. B Western blot and qPCR revealed the protein and mRNA levels of ERRα in Caki-1 and ACHN cells under hypoxic or normoxic conditions, ns p > 0.05. C Western blot found a decreased protein abundance of ERRα in RCC tissues compared with normal tissues. D Tissue microarry staining showed a significant downregulation of ERRα in renal tumor tissues when compared to normal kidney tissues, ***p < 0.001. E Cycloheximide chase assays revealed the half-life of ERRα proteins in Caki-1 under hypoxic or normoxic condition. F CoIP assays indicated the discrepant poly-ubiquitination of ERRα under hypoxic or normaxic condition. G Reporter luciferase assay showed the transactivation of ERRα on the luciferase activity in hypoxic or normoxic condition. *p < 0.05, ***p < 0.001. H IP assays showed the interaction between ERRα with p300 or CBP in Caki-1 under hypoxia or normoxia. I IP assay found that hypoxia enhanced the acetylation of ERRα in Caki-1 cells. J IP assays revealed that the interaction between ERRα and Parkin was increased in hypoxic condition.

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