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Cited by 724

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IL-6-Induced Homodimerization of gp130 and Associated Activation of a Tyrosine Kinase

Murakami, Masaaki, Hibi, Masahiko, Nakagawa, Naoko, Nakagawa, Toshimasa, Yasukawa, Kiyoshi, Yamanishi, Koichi, Taga, Tetsuya, Kishimoto, Tadamitsu·1993·Science

Abstract

The biological functions of interleukin-6 (IL-6) are mediated through a signal-transducing component of the IL-6 receptor, gp130, which is associated with the ligand-occupied IL-6 receptor (IL-6R) protein. Binding of IL-6 to IL-6R induced disulfide-linked homodimerization of gp130. Tyrosine kinase activity was associated with dimerized but not monomeric gp130 protein. Substitution of serine for proline residues 656 and 658 in the cytoplasmic motif abolished tyrosine kinase activation and cellular responses but not homodimerization of gp130. The IL-6-induced gp130 homodimer appears to be similar in function to the heterodimer formed between the leukemia inhibitory factor (LIF) receptor (LIFR) and gp130 in response to the LIF or ciliary neurotrophic factor (CNTF). Thus, a general first step in IL-6-related cytokine signaling may be the dimerization of signal-transducing molecules and activation of associated tyrosine kinases.

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Metadata

Authors
Murakami, M., Hibi, M., Nakagawa, N., Nakagawa, T., Yasukawa, K., Yamanishi, K., Taga, T., & Kishimoto, T.
Venue
Science
Published
1993-06-18
Volume
260
Issue
5115
Pages
1808-1810
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1971908211
Cited by
724
References
1
FWCI
30.62
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: IL-6-Induced Homodimerization of gp130 and Associated Activation of a Tyrosine Kinase. https://app.cochat.ai/papers/10.1126/science.8511589
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Murakami, M., Hibi, M., Nakagawa, N., Nakagawa, T., Yasukawa, K., Yamanishi, K., Taga, T., & Kishimoto, T. (1993). IL-6-Induced Homodimerization of gp130 and Associated Activation of a Tyrosine Kinase. Science. https://doi.org/10.1126/science.8511589

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