HSP70 is ubiquitinated in RPL11 invalidated cells before proteasomal degradation. Left panel: Immunoprecipitation (IP) of ubiquitinated stained proteins (ubiquitin lanes) compared with the immunoprecipitation with an immunoglobulin G (IgG) control antibody (IgG lanes) in UT-7 cells cultured under EPO and infected with either the shRPS19 or the shRPL11, compared with the SCRamble (shSCR). Proteins after immunoprecipitation have been revealed with an antibody against HSP70. shRPL11 cells were treated or not with MG132 at 10 µM for 5 hours. HSP70 expression has been analyzed in the total cell lysate (INPUT) to validate that the HSP70 protein is present in all the studied samples. IgG lane: IgG control antibody; ubiquitin lane: anti-ubiquitin specific antibody in order to immunoprecipitate the ubiquitinated proteins; IgG+MG132 lane: IgG control antibody immunoprecipitation after cell treatment with the proteasome inhibitor, MG132; ubiquitin+MG132: anti-ubiquitin specific antibody for ubiquitinated proteins after cell treatment with the proteasome inhibitor, MG132. Right panel: Immunoprecipitation of HSP70 stained protein. The proteins have been then revealed by an antibody against ubiquitin (top of the western blot) and against HSP70 (bottom of the western blot) in UT-7 cells cultured under EPO and infected with either the shRPS19 or the shRPL11, compared with the SCRamble (shSCR) and noninfected cells (Co). These cells were also treated or not with MG132 at 10 µM for 5 hours. IgG lane: IgG control antibody; HSP70 IP lanes: HSP70 specific antibody in order to immunoprecipitate HSP70 proteins in depleted RPS19, RPL11 after or not MG132 cell treatment and compare with the SCRamble (shSCR) and noninfected cells (Co).