Phosphorylated RELA besides undergoing further acetylation by the histone acetyltransferases (HATs) CBP and p300 also forms a complex with RELB to form inactive RELA-RELB dimers that cannot bind DNA. Because RELB requires p50 or p52 as a dimerization partner to bind DNA, it is possible that sequestration of RELB from its complex partners p50 and p52 by RELA might account for the lack of RELB DNA binding. RELA-RELB dimers have important regulatory consequences on dectin-1 mediated non-canonical NF-kB pathway. Inactive p65-RELB dimers blocks binding of RELB-p52 to the promoters of the chemokine genes CCL17 (CC-chemokine ligand 17) and CCL22, thereby blocking chemokine expression (Gringhuis et al. 2009).
den Dunnen, J,
van der Vlist, M