Bours V, Azarenko V, Dejardin E, Siebenlist U
Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892.
Oncogene. 1994 Jun;9(6):1699-702.
RelB belongs to the family of Rel-related proteins, dimers of which determine NF-kappa B activity. The murine RelB protein has been reported to be a dimerizing partner in kappa B-binding complexes which are capable of transactivation. On the other hand, the I-Rel protein, the presumed human homolog of RelB, was proposed to be an inhibitor whose presence in dimeric complexes interfered with their kappa B binding and therefore interfered also with transactivation. We demonstrate that human RelB (I-Rel) forms with p50 and p52 (p50B) kappa B-binding heterodimeric complexes which potently transactivate kappa B-dependent constructs in transfection studies. It is concluded that human RelB (I-Rel) and murine RelB can both function as transactivators and that no significant species-specific differences exist.
RelB属于Rel相关蛋白家族，该家族蛋白的二聚体决定核因子-κB（NF-κB）的活性。据报道，小鼠RelB蛋白是κB结合复合物中的二聚化伴侣，能够进行反式激活。另一方面，I-Rel蛋白被认为是RelB的人类同源物，被提出是一种抑制剂，其在二聚体复合物中的存在会干扰它们与κB的结合，因此也会干扰反式激活。我们证明，在转染研究中，人类RelB（I-Rel）与p50和p52（p50B）形成κB结合异源二聚体复合物，该复合物能有效反式激活κB依赖的构建体。得出的结论是，人类RelB（I-Rel）和小鼠RelB都可以作为反式激活因子发挥作用，并且不存在显著的物种特异性差异。
