◆ Selected as 2016: Signaling Breakthroughs of the year by Sci Signaling

In this study, we discovered that glycosylation and stabilization of programmed death ligand-1 (PD-L1) suppress T-cell killing activity. We identified a new interchange between glycosylation and phosphorylation regulating ubiquitination and degradation of PD-L1 is critical for basal-like breast cancer cells to escape immune surveillance via PD-L1/PD-1 interaction. Furthermore, inhibition of EGF-mediated PD-L1 stabilization enhances therapeutic efficacy of PD-1 blockade to promote-tumor infiltrating cytotoxic T-cell immune response. Thus, targeting PD-L1 stabilization provides a new strategy to combat BLBC-mediated immunosuppression and may potentially apply to other cancer types.