IndraLab
Statements
sparser
"We mutated lysine (K) to arginine (R) to generate point mutants of RIPK1, including HA-RIPK1-K302R, HA-RIPK1-K306R, HA-RIPK1-K316R, and HA-RIPK1-K377R. By cotransfection of Flag-USP53, Myc-Ub, and each RIPK1 mutant in HEK-293T cells, we observed that the K377R mutation effectively inhibited the USP53-induced RIPK1 deubiquitination, whereas K302R, K306R, and K316R did not affect this process (Fig. xref G)."
sparser
"By cotransfection of Flag-USP53 and RIPK1 mutants in AC16 cells, we observed that overexpression of USP53 significantly augmented EtOH-induced RIPK1 autophosphorylation, while K377R mutation effectively blocked the up-regulation of pRIPK1 Ser 166 mediated by USP53 (Fig. xref H and Fig. xref H)."