Fig. 2: Lysine 57 is the site of ubiquitylated of p11, but may not be involved in proteasomal degradation. | Cell Death & Disease

Fig. 2: Lysine 57 is the site of ubiquitylated of p11, but may not be involved in proteasomal degradation.

From: Regulation of cell surface protease receptor S100A10 by retinoic acid therapy in acute promyelocytic leukemia (APL)☆

Fig. 2

a Immunoblot analysis of HEK293T cells transiently transfected using pcDNA3.1-empty vector or pcDNA3.1-p11 vector alone or treated for 18 h using 3 µM lactacystin (LC), 1 mM NH4Cl, 1 µM MDL28170, or 1 µM calpain inhibitor IV (C.I.4). b Immunoblot analysis of HEK293T cells transiently transfected using pcDNA3.1-empty vector or pcDNA3.1-p11 vector alone or in combination with pRK5-HA-ubiquitin wild-type (ub-WT) or mutant, lysine-less ubiquitin (ub-K0). c Immunoblot analysis of HEK293T cells transiently expressing p11-wild type (p11WT) or p11 mutants (with Lys54 or Lys57 changed to arginine: p11K54R and p11K57R, respectively) alone or in combination with pRK5-HA-ub-K0. Cell lysates were prepared and the levels of the indicated proteins were examined by immunoblot analysis with β-actin used as a loading control. Data is expressed as the mean ± S.D. of three independent experiments. Statistical significance was determined using one-way ANOVA (with Tukey multiple comparisons), where *P < 0.05, **P < 0.01, ***P < 0.001, and ****P < 0.0001 are considered statistically significant

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