Fig. 3: DYRK2 regulates USP28 stability via the ubiquitin-proteasome system.
From: A novel feedback loop between DYRK2 and USP28 regulates cancer homeostasis and DNA damage signaling
A Dimerization of USP28 assayed by co-immunoprecipitation of HEK-293T cells transfected with the indicated plasmids. The presence of the proteins in both in input lysates and the immunoprecipitates is shown by WB. B HeLa cells were transfected with the indicated plasmids and treated or not with MG-132 (10 μM) for 12 h. Protein levels were determined by WB. C HEK-293T cells were transfected with the indicated plasmids. Flag-USP28 inactive mutant (C171A) was immunoprecipitated and its ubiquitination profile was determined by WB. In A and C, extracts were prepared from cells treated with the proteasome inhibitor MG-132 (10 μM) for 12 h. D, E HEK-293T cells were transfected with the indicated plasmids and analyzed by WB. Note: all experiments were performed at least 3 times, and a representative blot is shown.
