RELA (NF-κB subunit p65) (p65)

RELA, also known as the p65 subunit of NF-κB, is a key transcription factor that forms homo- or heterodimers, most commonly with p50, to regulate gene expression critical for inflammation, immune responses, cell proliferation, survival, and apoptosis. It contains an N-terminal Rel homology domain (RHD) for DNA binding, dimerization, and interaction with inhibitors like IκB, plus a C-terminal transactivation domain (TAD) that recruits coactivators such as CBP/p300 to activate target genes. In unstimulated cells, RELA is sequestered in the cytoplasm by IκB proteins; upon stimuli like TNF-α or LPS, IκB degradation allows nuclear translocation, where post-translational modifications including phosphorylation at sites like Ser276 enhance its transcriptional activity. RELA binds κB sites in promoters of genes involved in leukocyte activation, chemotaxis, and metabolism. Dysregulated RELA activation contributes to pathologies like cancer and chronic inflammation, positioning it as a central node in NF-κB signaling with interactions involving co-regulators like RFC p140 and p53.

Other names

NF-κB p65RelAp65 subunit of NF-κB