Fig. 6: Acetylation of ERRα facilitated its transactivation and proteasome-dependent degradation. | Cell Death & Disease

Fig. 6: Acetylation of ERRα facilitated its transactivation and proteasome-dependent degradation.

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

Fig. 6

A Western blot determined the half-life times of WT or 4KR ERRα under treatment with CHX. Line chart indicated the relative protein intensity of WT or 4KR normalized with GAPDH. B Cycloheximide chase assays revealed the effect of MG-132 and Baf-A1 on the stability of WT or 4KR proteins. C IP assay showed the different ubiquitination modification of WT and 4KR under the treatment with MG132. D Six kidney tumor tissues and their paired conjugated normal tissues were analyzed to show a reverse tendency between acetylation and ubiquitination of ERRα. E The schematic diagram illustrated the major acetylated sites of ERRα located in its DBD domain that contains two Zinc-finger domains. Green cycle labeled-A indicated the lysine modified with acetyl. F Reporter luciferase assay tested the transcription activity of WT or 4KR ERRα under hypoxic or normoxic conditions. *p < 0.05, **p < 0.01. G ChIP evaluated the enrichment of WT, 4KR and 4KQ on the promoters of LAMP2 and VAMP8, ***p < 0.001. H Western blot revealed the effect of rescued expression of ERRα WT and 4KR on the protein levels of LAMP2 and VAMP8 in Caki-1 with or without ERRα knockdown. I The interaction between endogenous PGC1β and exogenous WT or 4KR ERRα were determined by IP.

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