Fig. 7: The E3 ligase SIAH1 interacts with and ubiquitinates ADRM1 to promote its degradation in liver cancer cells. | Cell Death & Disease

Fig. 7: The E3 ligase SIAH1 interacts with and ubiquitinates ADRM1 to promote its degradation in liver cancer cells.

From: Deficiency of SIAH1 promotes the formation of filopodia by increasing the accumulation of FASN in liver cancer

Fig. 7

A TMT proteomics analysis comparing protein expression of empty-vector and overexpression of SIAH1 (−/ + MG132) in HepG2 cells. B, C Representative blots and quantification of ADRM1 and UCHL5 expression in human liver cancer cells overexpressing or silencing SIAH1. D Co-immunoprecipitation assay showed that SIAH1 interacted with ADRM1 in HepG2 and Huh7 cells. E Representative blots and quantification of ADRM1 expression in human liver cancer cells with a SIAH1 mutation. F Representative blots of ubiquitinated ADRM1 in human liver cancer cells with a SIAH1 mutation. G Representative blots of ubiquitination of FASN by SIAH1 in vitro. H SIAH1 ubiquitinated FASN through Lys33-linked ubiquitin chains. I Representative bolts and quantification showed overexpression of SIAH1 decreased the stability of ADRM1. J Representative blots and, K quantification of SIAH1 in human liver tumor tissues (n = 14) and normal liver tissues (n = 14). L The correlation of SIAH1 expression with ADRM1 in human normal liver tissues and liver cancer tissues. r = −0.5758; P = 0.0013. HepG2 and Huh7 cells were transfected with target plasmids. Twenty-four hours later, the cells were treated with MG132 (15 μM) for 8 h. *P < 0.05, **P < 0.01, ***P < 0.001.

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