Fig. 3: USP5 removes K27-linked polyubiquitin moieties from γc. | Cell Research

Fig. 3: USP5 removes K27-linked polyubiquitin moieties from γc.

From: PD-1 signaling negatively regulates the common cytokine receptor γ chain via MARCH5-mediated ubiquitination and degradation to suppress anti-tumor immunity

Fig. 3

a USP5 removes K27-linked polyubiquitin moieties from γc. HEK293 cells were transfected with the indicated plasmids for 24 h before immunoblotting analysis with the indicated antibodies. b Association of γc with USP5. Jurkat-PD-1 cells were stimulated with PHA (50 ng/mL) in the presence of plate-bound hPD-L1-Fc fusion protein for the indicated times before co-immunoprecipitation and immunoblotting analysis with the indicated antibodies. c USP5 but not its enzymatic inactive mutant USP5C335A removes K27-linked polyubiquitin moieties from γc. HEK293 cells were transfected with the indicated plasmids for 24 h before co-immunoprecipitation and immunoblotting analysis with the indicated antibodies. d USP5 removes K27-linked polyubiquitin moieties of γc catalyzed by MARCH5. HEK293 cells were transfected with the indicated plasmids for 24 h before immunoblotting analysis with the indicated antibodies. e USP5-deficiency enhances PD-1 ligation-induced K27-linked polyubiquitination of γc. Control or USP5-deficient Jurkat-PD-1 cells were stimulated with PHA (50 ng/mL) in the presence of plate-bound hPD-L1-Fc fusion protein for the indicated times before co-immunoprecipitation and immunoblotting analysis with the indicated antibodies. All the experiments were repeated for at least two times with similar results.

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