IL27RA and IL6ST are phosphorylated after IL27:IL27 receptor interaction and JAK's phosphorylation

Stable Identifier
Reaction [omitted]
Homo sapiens
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Interleukin-27 receptor is formed by Interleukin-27 receptor subunit alpha (IL27RA, WSX-1) and Interleukin-27 receptor subunit beta (IL6ST, gp130). Both subunits can be tyrosine phosphorylated after ligand-receptor interaction (Pflanz et al. 2004, Takeda et al. 2003). There is general agreement that ligand binding to cytokine receptors results in the activation of prebound Jak kinases, which auto- and transphosphorylate then phosphorylate key tyrosine residues on the receptor (O'Shea et al 2002), but for the interleukin-27 receptor the pattern of phosphorylations is not clear, hence this is represented as a black box event.
Literature References
PubMed ID Title Journal Year
12734330 Cutting edge: role of IL-27/WSX-1 signaling for induction of T-bet through activation of STAT1 during initial Th1 commitment

Mak, TW, Ishibashi, T, Takeda, A, Hanada, T, Yoshida, H, Yoshimura, A, Hamano, S, Yamanaka, A

J. Immunol. 2003
18389480 IL-12, IL-23, and IL-27 enhance human beta-defensin-2 production in human keratinocytes

Kanda, N, Watanabe, S

Eur. J. Immunol. 2008
14764690 WSX-1 and glycoprotein 130 constitute a signal-transducing receptor for IL-27

Kastelein, RA, Phillips, JH, Vaisberg, E, Rosales, R, Hibbert, L, Pflanz, S, Bazan, JF, Mattson, J, de Waal Malefyt, R, McClanahan, TK

J Immunol 2004
Catalyst Activity

transmembrane receptor protein tyrosine kinase activity of IL27:EBI3:IL27RA:p-JAK1:IL6ST:p-JAK1,p-JAK2,p-TYK2 [plasma membrane]

Orthologous Events
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