Fig. 7: K383 acetylation inhibits FBXO10-mediated ubiquitination degradation of ACSL4. | Cell Death & Disease

Fig. 7: K383 acetylation inhibits FBXO10-mediated ubiquitination degradation of ACSL4.

From: HAT1/HDAC2 mediated ACSL4 acetylation confers radiosensitivity by inducing ferroptosis in nasopharyngeal carcinoma

Fig. 7

A E3 ligase in protein mass spectrometry data pulled down by ACSL4 antibody. B GSE12452 data was used to analyze the expression of FBXO10. C After overexpression of FBXO10 in NPC cells and treated with MG-132 (20 μM) for 24 h, the protein expression of ACSL4 was detected by western blot. D Flag-ACSL4 and His-FBXO10 plasmids were transfected into 293 T cells, and the interaction between ACSL4 and FBXO10 was detected by IP assay. E IP assay was used to detect the interaction between ACSL4 and FBXO10 in NPC cells. F Molecular docking analysis of the interaction between ACSL4 and FBXO10. G The subcellular localization of ACSL4 and FBXO10 was detected by IF assay. H After overexpression of FBXO10 and treated with MG-132 (20 μM) in NPC cells for 10 h, the ubiquitination of ACSL4 was detected by IP assay. I After transfection of Flag-ACSL4 plasmids and His-FBXO10 into 293 T cells and treated with MG-132 (20 μM) for 10 h, the ubiquitination of ACSL4 was detected by IP assay. J, K Indicated plasmids were transfected into 293 T cells, and treated with MG-132 (20 μM) for 10 h, the ubiquitination of ACSL4 was detected by IP assay. L Indicated plasmids were transfected into 293 T cells, the interaction between FBXO10 and ACSL4 was detected by IP assay. The error line is expressed as mean ± SD. *p < 0.05.

Back to article page