Il23r from Il23:Il23 receptor complex is phosphorylated

Stable Identifier
R-MMU-8950679
Type
Reaction [omitted]
Species
Mus musculus
Compartment
cytosol, plasma membrane, extracellular region
ReviewStatus
5/5
General
SVG | 
PNG
Low
Medium
High
 | 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
27193299 Defining the functional binding sites of interleukin 12 receptor β1 and interleukin 23 receptor to Janus kinases

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

Mol. Biol. Cell 2016
23673666 Identification of canonical tyrosine-dependent and non-canonical tyrosine-independent STAT3 activation sites in the intracellular domain of the interleukin 23 receptor

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

J. Biol. Chem. 2013
Participants
Input
Output
Orthologous Events
IL23R in IL23:IL23 receptor complex is phosphorylated (Homo sapiens)
Authored
Duenas, C  (2016-12-02)
Reviewed
van de Vosse, E  (2017-05-12)
Created
Duenas, C  (2016-12-02)
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