{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRELB, a member of the noncanonical NF‑κB pathway, plays a pivotal role in immune cell differentiation and the establishment of endotoxin tolerance. In dendritic cells, for example, a slowly activating p52/RelB dimer gradually displaces the rapidly induced p50/RelA complex during maturation, thereby fine‐tuning the temporal profile of target gene activation despite the resynthesis of inhibitory IκB proteins. In models of endotoxin tolerance, RELB upregulation correlates with the repression of acute proinflammatory cytokine genes through direct interactions with chromatin modifiers such as the histone H3K9 methyltransferase G9a and heterochromatin protein 1, while concurrently supporting the sustained expression of anti‑inflammatory proteins such as IκBα."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn cancer, aberrant RELB activity contributes to tumorigenesis and therapy resistance by promoting survival and aggressive phenotypes. In prostate and breast cancer cells, elevated RELB supports resistance to radiation and chemotherapeutic stress by inducing the antioxidant enzyme manganese superoxide dismutase and upregulating pro‑survival cytokines such as interleukin‑8. In the tumor microenvironment, RELB participates in immunosuppressive circuits—such as driving indoleamine 2,3-dioxygenase (IDO) expression in myeloid-derived suppressor cells—and it is upregulated via CD40 signaling and adhesion receptor pathways to enhance lymphoma cell survival. In diffuse large B-cell lymphoma, for instance, constitutive RELB activation is linked to poor clinical outcomes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThe regulation of RELB involves diverse upstream signals and cross‑talk with other transcriptional regulators. Activation of the aryl hydrocarbon receptor (AhR) can lead to the formation of AhR/RELB complexes that drive chemokine transcription, whereas proteolytic processing by MALT1 controls RELB stability and thus modulates canonical NF‑κB activation. Additionally, IKKα‑dependent signaling and CD40 stimulation promote RELB-dependent transcription—such as the induction of cell cycle regulators like skp2—while Rac1 GTPase activity facilitates the nuclear translocation of RELB. Moreover, interactions with co‑regulatory factors such as the REQ adaptor link RELB/p52 dimers with chromatin remodeling complexes to induce downstream gene expression."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its central roles in immunity and oncogenesis, RELB participates in additional physiological processes and is subject to further layers of regulation. In fibroblasts, RELB acts as a repressor of circadian transcription by interacting with clock activators such as BMAL1, and specific phosphorylation events (for example, at conserved serine residues) are critical for its dimerization and for regulating the processing of its NF‑κB precursors. In esophageal squamous cell carcinoma, NF‑κB p65/RELB binding sites in the promoter of the riboflavin transporter gene SLC52A3 mediate aberrant gene transcription linked to tumor progression, while in pulmonary epithelial cells, hypercapnic exposure leads to the proteasome-dependent cleavage and nuclear translocation of RELB that contributes to protection against lung injury. In the placenta, RELB cooperates with NF‑κB2 to regulate corticotropin-releasing hormone expression, and in antigen-presenting cells, RELB-containing dimers modulate cytokine production and can attenuate interferon‑β expression during viral sensing. Finally, autophagy‐dependent degradation of signaling scaffolds in RAS mutant cancers results in selective RELB activation, which in turn represses certain TGF‑β target genes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Simona Saccani, Serafino Pantano, Gioacchino Natoli "}, {"type": "b", "children": [{"type": "t", "text": "Modulation of NF-kappaB activity by exchange of dimers."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s1097-2765(03)00227-2"}], "href": "https://doi.org/10.1016/s1097-2765(03"}, {"type": "t", "text": "00227-2) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12820969"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12820969"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Pedro J Cejas, Louise M Carlson, Despina Kolonias, et al. 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