v5.1.0.3
Cicer data from the Legume Information System
Type | Family |
Description | 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 [ ]. The cysteines allow formation of an extended rod-like structure, responsible for ligand binding []. Upon receptor activation, different intracellular signalling complexes are assembled for different members of the TNFR superfamily, depending on their intracellular domains and sequences [ ]. 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 [, ]. 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 [ ]. 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 []. TNF receptor 10 is activated by TNF-related apoptosis-inducing ligand (TRAIL). Four subtypes of the receptor have been identified: TNF receptors 10A and 10B (also known as death receptor 4 and 5, respectively), which contain a death domain within their C-terminal regions, and TNF receptors 10C and 10D, in which the death domain is not present or is truncated. It has been suggested that the function of the latter two receptors may be to inhibit TRAIL cytotoxicity by competing with the other TRAIL receptors for binding of the ligand [ , ]. |
Short Name | TNFR_10 |