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چکیده
ARF-BP1 enhances p42 ubiquitination To explore whether ARF-BP1 mediates p42 ubiquitination, we cotransfected GST-p42 and HAubiquitin into HEK293 cells in the presence of ARF-BP1 or MDM2, followed by MG132 treatment. ARF-BP1 strongly stimulated p42 polyubiquitination, whereas MDM2 barely influenced its ubiquitination. MG132 treatment further elevated the ubiquitination effect (Supplemental Figure 2A, top left panel). Cotransfection of ARF-BP1 but not MDM2 also upregulated GST-p42 polyubiquitination by the endogenous ubiquitin (data not shown). To investigate whether ARF-BP1 interacts with p42, we conducted a GST-pull down assay. Compared with GST control, GST-p42 robustly associated with ARF-BP1, but it was unable to bind MDM2 (Supplemental Figure 2B, top left and middle panels). Interestingly, S360D mutant exhibited even stronger affinity than wild-type p42, whereas S360A failed to bind Arf-BP1, suggesting that Ebp1 phosphorylation promotes its association with ARF-BP1 (Supplemental Figure 2B, right panels). However, ablation of ARF-BP1 did not induce p42 expression in human cancer cells (Supplemental Figure 2C). These data suggest that ARF-BP1 might not be the physiological E3 ubiquitin ligase for p42.
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