In the resting state, ASC appears in both the nucleus and the cytoplasm. Upon stimulation, it oligomerizes in the cytoplasm to assemble the inflammasome complex5–8. We discover that the zinc-finger and BTB domain-containing protein 16 (ZBTB16), also known as promyelocytic leukemia zinc-finger (PLZF), interacts with ASC in the nucleus to control the conjugation of the Small Ubiquitin-like Modifier (SUMO) to ASC. Post-translational modification of the inflammasome subunits is emerging as a key determinant of activity9,10. Although ASC has previously been identified to be phosphorylated and ubiquitylated11,12, the impact of SUMOylation was unknown.
