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These covalent changes—including those at key residues like serine‑536, lysine‑310, and specific cysteines—not only regulate RELA’s release from inhibitors and its association with cofactors, but also promote its eventual removal from chromatin via proteasomal degradation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its modulation by covalent modifications, RELA drives diverse gene‐expression programs that underlie inflammatory responses, cell survival, and oncogenic processes. It induces the transcription of key mediators such as chemokine receptors and antiapoptotic factors—thereby promoting metastatic cell motility and organ‐specific homing in cancer—and participates in cross‑talk with other transcriptional regulators like Nrf2, which it can repress by interfering with coactivator binding. In many tumor types, aberrant or constitutive activation of RELA sustains inflammatory gene networks and fosters cellular resistance to apoptosis. Moreover, targeted interventions (including the use of small inhibitory peptides, RNA interference strategies, and manipulation of interacting oncoproteins) reveal that modulating RELA’s activity can re‐sensitize cells to chemotherapeutic agents while antagonizing its tumor‑promoting effects."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nRELA also functions within broader regulatory networks by interacting with accessory factors and noncoding RNAs, thereby integrating external signals with internal transcriptional outputs. 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