RELA, also called NFKB3 or NFKB, p65 subunit is part of the NF-kB complex. The complex is inhibited by I-kappa-B proteins, which inactivates NFkB by trapping it in the cytoplasm. The p65 heterodimer is the most abundant form of NF-kB. It is a nonhistone substrate of HDAC3 and that IKBA-dependent nuclear export of the HDAC3-deacetylated RELA replenishes the depleted cytoplasmic pool of latent NFKB-IKBA complexes for subsequent NF-kB responses. Its nucleocytoplasmic redistribution coincided with export of PPARG, and immunoprecipitation analysis indicated that PPARG-RELA association was dependent on the PPARG C-terminal ligand-binding domain. IKK-dependent phosphorylation of RELA on Ser468 enhanced binding of GCN5 to RELA and its ubiquitination.