The role of tumour necrosis factor related apoptosis-inducing ligand receptor signalling in tumour immune interactions
Twohig, Margaret
Twohig, Margaret
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Publication Date
2023-09-18
Type
Thesis
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Abstract
Death receptors are members of the tumor necrosis factor receptor (TNFR) superfamily, characterised by the presence of an intracellular alpha helical fold domain, called the death domain (DD) [1][2]. There are 8 death receptors known in humans (Table 2.1), which are all cell surface, transmembrane proteins. The extracellular domain, located at the N-terminus is the ligand binding fragment and is comprised of between 3 - 4 cysteine rich domains (CRD) [3,4]. A single-pass transmembrane domain links the extracellular part of the receptor to the intracellular segment that consists of a short juxtamembrane- and a membrane-proximal region, followed by the DD on the C-terminus. The DD is approximately 80 amino acids long and its main role is to serve as a docking platform for intracellular signal transducers. Because all death receptors evolved from a common ancestral TNF receptor, they have similar functions to other members of this family, including control of cell differentiation, cell survival and inflammation, but due to the presence of a DD, they gained an additional function, which is the ability to induce cell death. Induction of cell death by DRs is considered as their canonical function and induction of pathways, other than cell death are typically known as non-canonical.
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NUI Galway