Negative regulation of RelA phosphorylation: Emerging players and their roles in cancer

Nuclear factor-kappa B (NF-κB) was discovered more than 20 years ago as a protein that when localized to the nucleus binds a response element the immunoglobulin κ enhancer to regulate expression of the κB light chain in B cells [1]. Dimerization of family members through Rel homology domain (RHD) is required for DNA binding and the transcription activation domain (TAD), present in RelA, c-Rel, and RelB, is necessary for upregulation of gene expression. Dimers composed of p50/p65, p50/c-rel, p65/p65, and p65/c-rel possess transcriptional potential, with the p50 and RelA being most intensively studied.
Source: Cytokine and Growth Factor Reviews - Category: Molecular Biology Authors: Tags: Mini review Source Type: research