Fig. 5: ERRα was acetylated by p300/CBP at K100, K125, K138, K146 residues. | Cell Death & Disease

Fig. 5: ERRα was acetylated by p300/CBP at K100, K125, K138, K146 residues.

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

Fig. 5

A CoIP assays showed the acetylation of endogenous ERRα in renal normal cell and RCC cells in presence with TSA and NAM. B IP assay revealed the acetylation of ERRα when ERRα coexpressed with different acetyltransferases. C, D CoIP assay confirmed the endogenous (C) and exogenous (D) interaction between ERR and p300/CBP. The endogenous IP was conducted in Caki-1 and exogenous IP was conducted in HEK-293T cells. E IP assay evaluated the effect of p300/CBP inhibitors on the acetylation of ERRα. F The diagram illustrated the procedure of identification for acetylated sites of ERRα by IP and MS. G IP assay showed the main acetylated sites of ERRα were located at K100, K125, K138 and K146. I The diagrams stimulated the domain location (left section) and evolutionary conservation (right section) of four acetylated sites of ERRα. H The result of IP found the acetylation levels of WT or 4KR ERRα in presence with TSA and NAM.

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