Interleukin-6 triggers the association of its receptor with a possible signal transducer, gp130

T Taga, M Hibi, Y Hirata, K Yamasaki, K Yasukawa… - Cell, 1989 - cell.com
T Taga, M Hibi, Y Hirata, K Yamasaki, K Yasukawa, T Matsuda, T Hirano, T Kishimoto
Cell, 1989cell.com
Interleukin-6 mediates pleiotropic functions in various types of cells through its specific
receptor (IL-6-R) the cDNA of which has already been cloned. We report here that an 60 kd
single polypeptide chain (IL-6-R) is involved in IL-6 binding and that IL-6 triggers the
association of this receptor with a non-ligand-binding membrane glycoprotein, gp130. The
association takes place at 37 C within 5 min and is stable for at least 40 min in the presence
of IL-6, but does not occur at 0%. Human IL-6-R can associate with a murine gpl30 homolog …
Summary
Interleukin-6 mediates pleiotropic functions in various types of cells through its specific receptor (IL-6-R) the cDNA of which has already been cloned. We report here that an 60 kd single polypeptide chain (IL-6-R) is involved in IL-6 binding and that IL-6 triggers the association of this receptor with a non-ligand-binding membrane glycoprotein, gp130. The association takes place at 37 C within 5 min and is stable for at least 40 min in the presence of IL-6, but does not occur at 0%. Human IL-6-R can associate with a murine gpl30 homolog and is functional in murine cells. Mutant IL-6-R lacking the intracytoplasmic portion is functional, suggesting that the two polypeptide chains interact to involve their extracellular portion. In fact, a soluble IL-6-R lacking the transmembrane and intracytoplasmic domains can associate with gp130 in the presence of IL-6 and mediate its function. These findings indicate that the complex of IL-6 and IL-6-R can interact with a non-ligand-binding membrane glycoprotein, gp130, extracellularly and can provide the IL-6 signal.
cell.com