FIGURE 2.

Preferential cleavage of Lys⁶³-linked tri-Ub by the AMSH-STAM complex. A, Coomassie-stained gel showing Lys⁶³ di/tri-Ub (4 μm) cleavage by AMSH (50 nm) and STAM1 (5 μm). B and C, steady-state kinetic saturation curves for cleavage of Lys⁶³-linked di-Ub (B) and Lys⁶³-linked tri-Ub (C) by AMSH (50 nm) and STAM2 (5 μm). Each rate was measured in two sets of experiments with quadruplicate measurements in each experiment, and error bars represent the mean ± S.E. for each measurement.