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. Author manuscript; available in PMC: 2013 Jun 21.
Published in final edited form as: Cell. 2010 Aug 20;142(4):637–646. doi: 10.1016/j.cell.2010.07.014

Figure 6. Reciprocal Negative Regulation between the 26S Proteasome and Executioner Caspases.

Figure 6

(A) Novel and published proteasome subunits identified as caspase substrates are mapped to an inventory of 20S core, 19S lid/base and 11S activator subunits (left). Cleaved subunits (red) are also mapped onto a model of the fully assembled, multimeric 26S proteasome (right). (B) The Casp3-TevS-2 line was treated with 10nM Rap over a course of 8 hr and assayed for caspase activity with Caspase-Glo-3/-7 and protease activity with Proteasome-Glo (Chymotrypsin-Like). Data are presented as the average from an experiment performed in triplicate (Error Bars±SD; note different scales). (C) A model for reciprocal negative regulation between activated executioner caspases and the 26S proteasome-ubiquitin system predicts synergy between caspase activation and proteasome inhibition. (D) The Casp3-TevS-2 line was co-treated with the indicated concentrations of Rap (0-8nM) and MG-132 (0-5uM) for 4 hr and caspase activation was measured with Caspase-Glo-3/-7 in triplicate. See also Table S1.