p-S276-RELA binds RELB

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).

磷酸化的RELA在由组蛋白乙酰转移酶（HATs）CBP和p300进一步乙酰化的同时，亦与RELB形成复合体，从而构成无活性的RELA-RELB二聚体，此类二聚体无法与DNA结合。鉴于RELB需要p50或p52作为二聚化伴侣以与DNA结合，RELA可能通过将RELB从其复合体伴侣p50和p52中隔离出来，从而解释了RELB与DNA结合能力的缺失。RELA-RELB二聚体在dectin-1介导的非典型NF-kB途径中具有重要的调控后果。无活性的p65-RELB二聚体阻碍了RELB-p52与趋化因子基因CCL17（CC-趋化因子配体17）和CCL22启动子的结合，进而阻断趋化因子的表达（Gringhuis等，2009）。