LIFR:JAKs bind gp130:JAKs:CNTFR

Stable Identifier
Reaction [binding]
Homo sapiens
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The cytokine receptor gp130 is the shared signalling subunit of the interleukin (IL)-6-type cytokines. IL-6 and IL-11 signal through gp130 homodimer whereas leukaemia inhibitory factor (LIF), ciliary neurotrophic factor receptor (CNTFR), Cardiotrophin-like cytokine factor 1 (CLCF1), Cardiotrophin-1 (CT-1) and Oncostatin-M (OSM) exerts its action through a heterodimer of gp130 and the LIF receptor (LIFR) (Heinrich et al. 2003, Giese et al. 2005). LIFR beta structure closely resembles that of gp130 and upon ligand binding forms gp130:LIFR beta heterodimer. Finally CNTFR alpha complexed with this signal transducing heterodimer converts into functional tripartite CNTF receptor and induces phosphorylation of both gp130 and LIFR beta (Davis et al. 1993, Stahl & Yancopoulos 1994). Formation of the tripartite complex then leads to activation of Janus family kinases, JAK1, 2, 3, and TYK2 and phosphorylation of tyrosine residues on the cytoplasmic domain of gp130 (Kass 2011).

Literature References
PubMed ID Title Journal Year
16051226 The N-terminal cytokine binding domain of LIFR is required for CNTF binding and signaling

Smith, DK, Ip, NY, Gong, K, He, W

FEBS Lett. 2005
9238703 Expression of leukaemia inhibitory factor receptor subunits LIFR beta and gp130 in human oocytes and preimplantation embryos

Mummery, CL, Junca, AM, Plachot, M, Belaisch-Allart, J, van Eijk, MJ, Salat-Baroux, J, Mandelbaum, J

Mol. Hum. Reprod. 1996
8390097 LIFR beta and gp130 as heterodimerizing signal transducers of the tripartite CNTF receptor

Kishimoto, T, Stahl, N, Pan, L, Ip, NY, Yancopoulos, GD, Davis, S, Taga, T, Aldrich, TH

Science 1993
11943154 Membrane distal cytokine binding domain of LIFR interacts with soluble CNTFR in vitro

Smith, DK, Ip, NY, Gong, K, Zhu, G, He, W

FEBS Lett. 2002
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