Death receptor 3

Death receptor 3 (DR3), also known as TNFRSF25 (Tumor Necrosis Factor Receptor Superfamily Member 25), is a protein that in humans is encoded by the TNFRSF25 gene. It is a member of the tumor necrosis factor receptor superfamily, which is a group of proteins that play a crucial role in controlling cell survival and death.

Structure

DR3 is a type 1 transmembrane protein, which means it spans the cell membrane once and has its N-terminus on the outside of the cell. It is composed of an extracellular domain, a transmembrane domain, and an intracellular domain. The extracellular domain is responsible for binding to its ligand, while the intracellular domain is responsible for transmitting the signal into the cell.

Function

The primary function of DR3 is to regulate immune system responses. It does this by binding to its ligand, TL1A, which triggers a cascade of intracellular events leading to the activation of NF-kappaB, a protein complex that controls the transcription of DNA. This activation can lead to a variety of responses, including cell proliferation, differentiation, and apoptosis (programmed cell death).

Clinical significance

Alterations in the function of DR3 have been implicated in a variety of diseases. For example, overexpression of DR3 has been observed in several types of cancer, including breast cancer and colorectal cancer. In addition, mutations in the TNFRSF25 gene have been associated with susceptibility to autoimmune diseases, such as rheumatoid arthritis and lupus.

Research

Research into DR3 is ongoing, with a focus on understanding its role in disease and developing potential therapies. For example, drugs that target DR3 are being investigated for their potential to treat autoimmune diseases and cancer.

See also

• Tumor necrosis factor receptor
• TL1A
• NF-kappaB
• Autoimmune disease
• Cancer