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. 2015 Jun 23;6(24):19990–20001. doi: 10.18632/oncotarget.4598

Figure 4. Synoviolin promotes IRE1α degradation in a wild-type p53-dependent manner.

Figure 4

A. SYVN1 suppresses IRE1α protein expression in wild-type p53 cells. HCT116 p53+/+ or HCT116 p53−/− cells were transfected with siControl (−) or siSYVN1 (+) and cultured for 24 h. Cell lysates were analyzed using western blotting with indicated the antibodies (left panel). The intensities of the SYVN1 bands were quantified. The levels of SYVN1 are reported relative to those of β-actin (right panel). The blot was cut based on the size of proteins or stripped and reprobed. B. IRE1α and SYVN1 interaction is suppressed in p53-deficient cells. Proteins were cross-linked with DSP before protein extraction. Coimmunoprecipitation was performed with cell lysate using an IRE1α or an SYVN1 antibody. C. SYVN1 interacts with wild-type p53. H1299 cells transiently expressed wild-type p53, p53-R248S, or p53-R273H. Coimmunoprecipitation experiments were performed using the anti-p53 antibody. D. p53-SYVN1-IRE1α complex is observed by treatment with proteasome inhibitor. H1299 cells transiently expressing wild-type p53 (left panel) or HCT116 p53+/+ (right panel) cells were treated with 50 μM MG132 for 3 h. Coimmunoprecipitation experiments were performed using the anti-p53 antibody.