Fig. 4: Glycosylation plays an important role in PD-L1 homodimerization. | Communications Biology

Fig. 4: Glycosylation plays an important role in PD-L1 homodimerization.

From: Homodimerized cytoplasmic domain of PD-L1 regulates its complex glycosylation in living cells

Fig. 4

a, b Defect of PD-L1 glycosylation result in PD-L1 homodimerization attenuated. a PD-L1 and PD-L1-3NQ/4NQ mutants were incorporated with Azi. Azi introduced positions are indicated in the upper row. Cells were treated with UV for 20 min before collecting. b Tunicamycin (TM) suppresses PD-L1 homodimerization. Cells expressing PD-L1-V76Azi were treated with 5 µM tunicamycin for 24 h before collection. c The number of glycosylated residues affects homodimerization of PD-L1. Azi was incorporated into V76 of WT PD-L1-Flag or PD-L1-Flag mutants. All samples were treated with PNGase F to remove the N-glycan.

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