Glycoprotein 130

Glycoprotein 130 (also known as gp130, IL6ST, IL6-beta or Interleukin-6 receptor subunit beta) is a transmembrane protein which is the founding member of the class of all cytokine receptors. It forms one subunit of the type I interleukin-6 (IL-6) receptor complex.

Structure

Gp130 is a 130 kDa glycoprotein. It is a type I transmembrane protein that possesses a large extracellular domain, a single transmembrane domain, and an intracellular domain. The extracellular domain is composed of a number of fibronectin type III domains and is involved in ligand binding. The intracellular domain is involved in signal transduction and contains a number of tyrosine residues that are phosphorylated following ligand binding.

Function

Gp130 is a signal-transducing receptor subunit shared by many cytokines, including interleukin 6 (IL-6), ciliary neurotrophic factor (CNTF), leukemia inhibitory factor (LIF), and oncostatin M (OSM). These cytokines are involved in the regulation of a variety of biological processes including immune responses, hematopoiesis, inflammation and neuronal development.

Clinical significance

Alterations in the function of gp130 and its ligands are implicated in a variety of diseases, including rheumatoid arthritis, inflammatory bowel disease, cancer, and neuropathies.

See also

• Interleukin-6 receptor
• Cytokine receptor
• Signal transduction

References

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