Promyelocytic leukemia (PML) and a suite of other proteins form nuclear bodies (NBs) where SUMOylation of PML and tumor suppression events occur in response to arsenite (As) treatment. Soluble PML is rapidly modified to the insoluble form in response to As, yet the relationship between the solubility change and nuclear localization of PML and PML-nuclear body (PML-NB) proteins remained elusive. We have investigated differences in the solubility change of well-known PML-NB proteins such as death-associated protein 6 (DAXX), SUMO, and PML in genetically engineered HEK293, and Jurkat and HL60 cells. The solubility of PML and SUMO2/3 monomers in RIPA solution decreased in 2 h in response to As. Live image analysis of GFP-PML revealed that extranuclear PML was insoluble in RIPA irrespective of the As-treatment and PML in PML-NBs, which was soluble in the untreated cells, was converted to insoluble forms by As. The solubility of DAXX was not changed by As, even though PML and DAXX co-localized completely in the subcellular compartments. Murine double mutant 2 (MDM2), which is known to interacts with intranuclear PML, did not affect the As-induced solubility change of PML. These results indicate that As selectively reorganizes PML and SUMO2/3 monomers into insoluble forms in PML-NBs, and then PML SUMOylation proceeds.
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