IndraLab

Statements


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sparser
"In order to figure out why USP53 will affect the expression of IκBα, we transfected Myc‐ub, HA‐IκBα, and FlagUSP53 into 293 cells, and then tested the effect of USP53 on the ubiquitination of IκBα by co‐immunoprecipitation and WB experiments."

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
"The results showed direct interaction between HA-RIPK1 and Flag-USP53 (Fig. xref E and F)."

sparser
"Similar results were found in human embryonic kidney (HEK)-293T cells transfected with hemagglutinin (HA)-RIPK1 and Flag-USP53, which showed colocalization of HA-RIPK1 and Flag-USP53 in cytoplasm (Fig. xref D)."

sparser
"By cotransfection of HA-RIPK1 with either Flag-USP53 or Flag-USP53-C41S in HEK-293T cells, we found that catalytic site-mutated USP53-C41S was unable to inhibit the ubiquitination of RIPK1 (Fig. xref B)."

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)."