The activated protein phosphatase 2A then dephosphorylates Bad on ser112, resulting in its dissociation from 14-3-3 chaperone protein and its translocation to the mitochondria, where it acts as a sensitizer by binding to antiapoptotic proteins such as Bcl-2 in leukemic cells and Mcl-1 in multiple myeloma cells, and releasing Bim from its association with these proteins. This evidence concerns the gene MCL1 and plasma cell myeloma.