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Membrane distal cytokine binding domain of LIFR interacts with soluble CNTFR in vitro
Author(s) -
He Wei,
Gong Ke,
Zhu Guang,
Smith David K,
Ip Nancy Y
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02367-0
Subject(s) - leukemia inhibitory factor receptor , ciliary neurotrophic factor , glycoprotein 130 , receptor , cytokine receptor , microbiology and biotechnology , leukemia inhibitory factor , cytokine , chemistry , biology , interleukin 6 , biochemistry , immunology , neurotrophic factors
Ciliary neurotrophic factor (CNTF) is a member of the gp130 family of cytokines. The functional receptor complex of CNTF is composed of the CNTF receptor α (CNTFR), gp130 and the leukemia inhibitory factor receptor (LIFR). Three regions on CNTF have been identified as binding sites for its receptors. The ligand–receptor interactions are mediated through the cytokine binding domains (CBDs) and/or the immunoglobulin‐like domains of the receptors. However, in the case of CNTF, the precise nature of the protein–protein contacts in the signaling complex has not yet been resolved. In this study, we provide the first demonstration that the membrane distal CBD (CBD1) of LIFR associates in vitro with soluble CNTFR in the absence of CNTF. Moreover, purified CBD1 partially blocks CNTF signaling, but not that of interleukin‐6 or LIF, in human embryonal carcinoma cell line Ntera/D1 cells. These data raise the possibility that LIFR has the capability to form a ligand‐free complex with CNTFR.