Il23r from Il23:Il23 receptor complex is phosphorylated

Stable Identifier
R-MMU-8950679
Type
Reaction [omitted]
Species
Mus musculus
Compartment
General
SVG |   | PPTX  | SBGN
Il23r from Il23:Il23 receptor complex is phosphorylated

Interleukin-23 receptor subunit (Il23r) can be phosphoryated in different intracellular Tyrosin residues. Tyr-542 and Tyr-626 aminoacid residues in murine Il23r are important for SH2 domain dependent Signal transducer and activator of transcription 3 (Stat3) activation . Moreover Western blot data demostrated Interleukin-23 dependent trysoine phosphorylation of Stat3 in cotransfected parental cell lines(2C4, 2fTGH) and Tyrosine-protein kinase JAK1(Jak1)-deficient cells (U4C) (Floss et al. 2016).
As it is not clear about the pattern of phosphorylations this reaction is represented here as a black box event.

Literature References
PubMed ID Title Journal Year
23673666 Identification of canonical tyrosine-dependent and non-canonical tyrosine-independent STAT3 activation sites in the intracellular domain of the interleukin 23 receptor

Floss, DM, Mrotzek, S, Klöcker, T, Schröder, J, Grötzinger, J, Rose-John, S, Scheller, J

J. Biol. Chem. 2013
27193299 Defining the functional binding sites of interleukin 12 receptor β1 and interleukin 23 receptor to Janus kinases

Floss, DM, Klöcker, T, Schröder, J, Lamertz, L, Mrotzek, S, Strobl, B, Hermanns, H, Scheller, J

Mol. Biol. Cell 2016
Participants
Orthologous Events
Authored
Reviewed
Created