Tumor necrosis factor receptor 1

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Tumor necrosis factor receptor 1 (TNFR1), also known as TNF receptor superfamily member 1A (TNFRSF1A), is a protein that in humans is encoded by the TNFRSF1A gene. This receptor is primarily involved in the regulation of immune system responses and apoptosis.

Structure[edit | edit source]

TNFR1 is a type I transmembrane protein with a molecular weight of approximately 55 kDa. It is composed of 455 amino acids and has a single transmembrane domain. The extracellular region of TNFR1 contains four cysteine-rich domains (CRDs), which are necessary for the binding of tumor necrosis factor (TNF).

Function[edit | edit source]

TNFR1 is one of the two receptors that bind with TNF, a powerful proinflammatory cytokine. This binding can trigger several different signal transduction pathways, leading to various outcomes such as apoptosis, cell survival, inflammation, and immune response regulation. The specific outcome depends on the cellular context and the engagement of specific adaptor proteins.

Clinical significance[edit | edit source]

Mutations in the TNFRSF1A gene have been associated with multiple diseases, including autoimmune diseases and cancer. For example, mutations in this gene are responsible for the autosomal dominant periodic fever syndrome known as Tumor necrosis factor receptor-associated periodic syndrome (TRAPS).

Research[edit | edit source]

Research is ongoing to develop drugs that can modulate the activity of TNFR1, with the aim of treating diseases associated with excessive or insufficient TNF signaling.

File:Tumor necrosis factor receptor 1.png
Structure of the extracellular portion of human tumor necrosis factor receptor 1.

See also[edit | edit source]

References[edit | edit source]


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Contributors: Prab R. Tumpati, MD