Fig. 8: SIAH1 directly ubiquitinates FASN to promote its degradation in liver cancer cells. | Cell Death & Disease

Fig. 8: SIAH1 directly ubiquitinates FASN 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. 8

A, B Representative blots and quantification of FASN expression in human liver cancer cells overexpressing or silencing SIAH1. C Co-immunoprecipitation assay showed that SIAH1 interacted with FASN in HepG2 and Huh7 cells. D Representative bolts and quantification of FASN expression in liver cancer cells transfected with His-SIAH1 plasmid (+CHL). E Representative blots and quantification showed that MG132 could block the degradation of FASN in SIAH1-upregulated cells. F Representative blots and quantification of FASN expression in human liver cancer cells with a SIAH1 mutation. G Representative blots of ubiquitinated FASN in human liver cancer cells with a SIAH1 mutation. H Representative blots of ubiquitination of FASN by SIAH1 in vitro. I SIAH1 ubiquitinated FASN through Lys33-linked ubiquitin chains in HepG2 and Huh7 cells. J Representative bolts and quantification showed overexpression of SIAH1 decreased the stability of FASN. K The correlation of SIAH1 expression with ADRM1 in human normal liver tissues and liver cancer tissues. r = −0.4591; P = 0.014. 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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