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Death Receptor & Ligand Proteins

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Death Receptor & Ligand Proteins

Death Receptor & Ligand Proteins Background

The death receptor is a group of cell surface markers discovered in recent years. It belongs to the tumor necrosis factor receptor superfamily. After binding to the corresponding ligands, it can transmit the apoptotic signal to the interior of the cell through a series of signal transduction processes.

Apoptosis is an active, signal-dependent process that can be induced by many factors, such as radiation exposure, toxins, drugs, ischemia and hypoxia, viral infections, and so on. Studies have found that most of these factors trigger the mechanism of apoptosis by activating death receptors. The death receptor is a group of cell surface markers discovered in recent years. It belongs to the tumor necrosis factor receptor superfamily. After binding to the corresponding ligands, it can transmit the apoptotic signal to the interior of the cell through a series of signal transduction processes. This process involves at least 4 families of proteins, including DR3, DR-4, DR-5, and DR-6, which ultimately cause activation of the caspase protease family of apoptosis performers, which cleave the corresponding substrates and cause apoptosis.

Death receptor 3 (DR3)

Death receptor 3 (DR3) is the only known TNFSF ligand that is TNF-like protein 1A (TL1A). The receptor is preferably expressed by activated and antigen-experienced T lymphocytes. FoxP3 positive regulatory T lymphocytes also highly expressed TNFRSF25. TNFRSF25 is activated by a monogamous ligand called TL1A (TNFSF15), which rapidly upregulates in antigen presenting cells and certain endothelial cells upon activation of Toll-like receptors or Fc receptors. This receptor has been shown to express NF-κB activity signaling via the TRADD adaptor molecule or to stimulate caspase activation and regulate apoptosis via the FADD adaptor molecule.

Death receptor 4 (DR4)

Death receptor 4 (DR4 is the cell surface of the TNF receptor superfamily that binds to TRAIL and mediates apoptosis. Receptor. The protein encoded by this gene is a member of the TNF receptor superfamily. This receptor is activated by a tumor necrosis factor-related apoptosis-inducing ligand (TNFSF10/TRAIL), which transduces cell death signals and induces apoptosis.

Death receptor 5 (DR5)

Death Receptor 5 (DR5) is the cell surface of the TNF receptor superfamily that binds to TRAIL and mediates apoptosis. Receptor. The protein encoded by this gene is a member of the TNF receptor superfamily and contains an intracellular death domain. This receptor can be activated by a tumor necrosis factor-related apoptosis-inducing ligand (TNFSF10/TRAIL/APO-2L) and transduce an apoptotic signal. The mouse has the homologous gene tnfrsf10b, which is essential in elucidating the function of this gene in humans. Studies in FADD-deficient mice indicate that FADD, a death domain containing adaptor proteins, is required for this protein-mediated apoptosis.

Figure 1. Structure of the Death receptor 5 (DR5).

Death receptor 6 (DR6)

Death receptor 6 (DR6) is mainly expressed in the thymus, spleen and white blood cells. The protein encoded by this gene is a member of the TNF receptor superfamily. This receptor activates NF-κB and MAPK8 / JNK and induces apoptosis. Through its death domain, this receptor interacts with the TRADD protein, and the TRADD protein acts as an adaptor that mediates TNF receptor signaling. Knockout studies in mice indicate that this gene plays a role in T helper cell activation and may be involved in inflammation and immune regulation. DR6 is an alpha-helical integrated membrane receptor protein that has been shown to be involved in inhibiting the formation of blood vessels on tumors, thereby allowing them to grow. Death receptor 6 acquires chemical information and initiates a signaling pathway leading to apoptosis (also known as cell death). It is also expressed in endothelial cells. Tumor cells can induce DR6-mediated proliferation of endothelial cell necrosis by exposure to amyloid precursor protein (APP), thereby allowing tumor metastasis.

Figure 2. Structure of the Death receptor 6 (DR6).

References:

1. Pan G.; et al. Identification and functional characterization of DR6, a novel death domain-containing TNF receptor. FEBS Letters. 1998,431 (3): 351–356.

2. Mungall AJ.; et al. The DNA sequence and analysis of human chromosome 6. Nature. 2003,425 (6960): 805–811.

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