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The N‐terminal cytokine binding domain of LIFR is required for CNTF binding and signaling
Author(s) -
He Wei,
Gong Ke,
Smith David K.,
Ip Nancy Y.
Publication year - 2005
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/j.febslet.2005.06.061
Subject(s) - leukemia inhibitory factor receptor , oncostatin m , glycoprotein 130 , ciliary neurotrophic factor , leukemia inhibitory factor , receptor , cytokine receptor , microbiology and biotechnology , chemistry , cytokine , interleukin 6 , signal transduction , biology , biochemistry , immunology , neurotrophic factors , stat3
Ciliary neurotrophic factor (CNTF) forms a functional receptor complex containing the CNTF receptor, gp130, and the leukemia inhibitory factor receptor (LIFR). However, the nature and stoichiometry of the receptor‐mediated interactions in this complex have not yet been fully resolved. We show here that signaling by CNTF, but not by LIF or oncostatin M (OSM), was abolished in cells overexpressing a LIFR mutant with the N‐terminal cytokine binding domain deleted. Our results illustrate molecular differences between the CNTF active receptor complex and those of LIF and OSM and provide further support for the hexameric model of the CNTF receptor complex.