Membrane distal cytokine binding domain of LIFR interacts with soluble CNTFR in vitro

FEBS Letters

Gong, Ke²  Smith, David K¹  Ip, Nancy Y²  Zhu, Guang²  He, Wei² 

[1] Department of Biochemistry, University of Hong Kong, Hong Kong, PR China;Department of Biochemistry and Biotechnology Research Institute, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, PR China

关键词: Leukemia inhibitory factor receptor;    Ciliary neurotrophic factor receptor;    CNTF;    LIF;    Interleukin-6;    Cytokine;    CNTF;    ciliary neurotrophic factor;    sCNTFR;    soluble CNTF receptor α;    LIF;    leukemia inhibitory factor;    LIFR;    LIF receptor β;    IL-6;    interleukin-6;    IL-11;    interleukin-11;    OSM;    oncostatin M;    CT-1;    cardiotrophin-1;    CLC;    cardiotrophin-like cytokine;    NT-2;    human embryonal carcinoma cell line Ntera/D1;    CBD;    cytokine binding domain;    Ig;    immunoglobulin;    STAT;    signal transducer and activator of transcription;   

DOI  :  10.1016/S0014-5793(02)02367-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown