The tumour necrosis factor (TNF) receptor (TNFR) superfamily comprises more than 20 type-I transmembrane proteins. Family members are defined based on similarity in their extracellular domain - a region that contains many cysteine residues arranged in a specific repetitive pattern [7917108]. The cysteines allow formation of an extended rod-like structure, responsible for ligand binding [8387891].
Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences [15500863]. Activation of TNFRs can therefore induce a range of disparate effects, including cell proliferation, differentiation, survival, or apoptotic cell death, depending upon the receptor involved [11239407,9826575].
TNFRs are widely distributed and play important roles in many crucial biological processes, such as lymphoid and neuronal development, innate and adaptive immunity, and maintenance of cellular homeostasis [15500863]. Drugs that manipulate their signalling have potential roles in the prevention and treatment of many diseases, such as viral infections, coronary heart disease, transplant rejection, and immune disease [9826574].
TNF receptor 3 (also known as lymphotoxin-beta receptor) acts as a receptor for the heterotrimer of lymphotoxin-alpha and beta, and also for the TNF ligand LIGHT. Activation of the receptor promotes apoptosis via recruitment of TNFR-associated factor 3 (TRAF3) [9122217].
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