tumor necrosis factor receptor binding

Definition

Target type: molecularfunction

Binding to a tumor necrosis factor receptor. [GOC:ai]

Tumor necrosis factor receptor (TNFR) binding is a crucial process in the regulation of immune responses, inflammation, and cell survival. TNFRs are transmembrane proteins that belong to the TNF receptor superfamily. They play a central role in mediating the biological effects of TNF-α, a pleiotropic cytokine involved in various cellular processes.

The interaction between TNF-α and TNFRs initiates a complex signaling cascade, ultimately leading to the activation of downstream transcription factors and signaling pathways. This intricate interplay between TNF-α and TNFRs is essential for maintaining cellular homeostasis and regulating inflammatory responses.

TNF-α binds to its receptor TNFR1 (also known as p55), which is expressed on various cell types, including immune cells, endothelial cells, and fibroblasts. This interaction triggers the recruitment of adaptor proteins, such as TRADD and TRAF2, to the cytoplasmic domain of TNFR1. The assembly of these adaptor proteins leads to the activation of downstream signaling pathways, including the NF-κB pathway and the MAPK pathway.

The NF-κB pathway is a crucial regulator of gene expression, promoting the production of pro-inflammatory cytokines, chemokines, and cell adhesion molecules. Activation of the NF-κB pathway contributes to the inflammatory response by recruiting immune cells to the site of inflammation and promoting the expression of genes involved in immune defense.

The MAPK pathway is another important signaling pathway activated by TNFR1 engagement. MAPKs, such as ERK, JNK, and p38, are involved in regulating cell growth, differentiation, and apoptosis. Activation of the MAPK pathway by TNFR1 can promote cell survival or induce apoptosis, depending on the cellular context and the specific MAPKs involved.

TNF-α can also bind to TNFR2 (also known as p75). TNFR2 is primarily expressed on immune cells and plays a role in regulating apoptosis and immune cell differentiation. However, unlike TNFR1, TNFR2 does not directly activate the NF-κB pathway. Instead, TNFR2 signaling primarily involves the activation of the MAPK pathway and the induction of apoptosis.

In addition to its role in immune responses, TNFR signaling has been implicated in various pathological conditions, including cancer, autoimmune diseases, and neurodegenerative diseases. Dysregulation of TNFR signaling can contribute to the development and progression of these diseases. Therefore, targeting TNFR signaling pathways has emerged as a promising therapeutic strategy for treating these conditions.

In summary, TNFR binding is a complex molecular function that plays a critical role in regulating immune responses, inflammation, and cell survival. The interaction between TNF-α and its receptors triggers a cascade of signaling events, ultimately leading to the activation of various downstream pathways involved in cellular function and response to stress.'
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Proteins (5)

Compounds (51)