Leukemia inhibitory factor receptor

Leukemia inhibitory factor receptor (LIFR) is a type of protein that in humans is encoded by the LIFR gene. It is a part of the interleukin 6 receptor family. LIFR plays a crucial role in various biological processes, including cell differentiation, neuronal survival, and immune response.

Structure

The LIFR protein is a single-pass type I membrane protein. It is composed of an extracellular domain, a transmembrane domain, and an intracellular domain. The extracellular domain is responsible for binding to the leukemia inhibitory factor (LIF), while the intracellular domain is involved in signal transduction.

Function

LIFR is the receptor for the leukemia inhibitory factor, a cytokine involved in a variety of biological processes. Upon binding to LIF, LIFR forms a complex with the glycoprotein 130 (gp130) co-receptor, leading to the activation of various signal transduction pathways, including the JAK-STAT signaling pathway and the MAPK/ERK pathway. These pathways regulate gene expression and contribute to cell differentiation, survival, and proliferation.

Clinical significance

Mutations in the LIFR gene can lead to Stüve-Wiedemann syndrome, a rare autosomal recessive disorder characterized by skeletal abnormalities, respiratory distress, and an increased risk of malignant hyperthermia during anesthesia. In addition, LIFR has been implicated in the progression of several types of cancer, including breast cancer and colorectal cancer.

See also

• Leukemia inhibitory factor
• Interleukin 6
• Signal transduction
• Stüve-Wiedemann syndrome

References

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