Nuclear factor NF-kappa-B subunit c-Rel (c-Rel)

Nuclear factor NF-kappa-B subunit c-Rel (commonly abbreviated as c-Rel) is a member of the NF-κB transcription factor family, which also includes RelA (p65), RelB, NF-κB1 (p50), and NF-κB2 (p52)[3][6][8]. c-Rel is encoded by the REL gene and is characterized by the Rel homology domain, which mediates dimerization and DNA binding[2][5]. c-Rel is unique among mammalian NF-κB subunits in its ability to transform lymphoid cells, and is closely related to the viral oncoprotein v-Rel[1][2]. c-Rel plays a critical regulatory role in immune system development and function, controlling genes involved in cell survival, proliferation, apoptosis, and inflammation[3][5]. Amplification or dysregulation of REL is implicated in several forms of cancer, especially B-cell lymphomas such as germinal center B-cell-like diffuse large B-cell lymphoma, and is associated with other disorders involving chronic inflammation and autoimmunity (e.g., rheumatoid arthritis, ulcerative colitis)[1][2][5]. c-Rel is a complex regulator, and therapeutic targeting poses challenges due to its essential normal physiological roles and redundancy with other NF-κB subunits[1][2][4][5].

Other names

RELproto-oncogene c-Relc-Rel transcription factor

Inhibitors act by blocking nuclear translocation, DNA binding, or dimerization of c-Rel, or by general inhibition of NF-κB pathway activation[1][2][4]. Targeting upstream kinases, degradation pathways, or direct DNA binding inhibition.