Reactome | Recruitment of IFNAR1

Recruitment of IFNAR1

Stable Identifier

R-HSA-909724

Type

Reaction [binding]

Species

Homo sapiens

Compartment

plasma membrane

ReviewStatus

5/5

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The extracellular domain of IFNAR1 is atypical, consisting of a tandem array of four FNIII domains and the first three N-terminal FNIII domains are involved in ligand recognition. IFNAR1 is recruited to the binary complex (IFNA/B:IFNAR2) on the membrane to form the ternary complex (IFNAR2:IFNA/B:IFNAR1). TYK2 kinase is pre-associated with IFNAR1 and JAK1 with IFNAR2. The binding of IFNA/B to IFNA receptors brings these JAK kinase together, allowing cross-phosphorylation and kinase activation.

Literature References

PubMed ID	Title	Journal	Year
16171819	Mutational analysis of the IFNAR1 binding site on IFNalpha2 reveals the architecture of a weak ligand-receptor binding-site Jaitin, DA, Schreiber, G, Roisman, LC, Baker, DP	J Mol Biol	2005
15449939	Identification of residues of the IFNAR1 chain of the type I human interferon receptor critical for ligand binding and biological activity Sempé, P, Gallet, X, Nardeux, PC, Guymarho, J, Eid, P, Tovey, MG, Cajean-Feroldi, C, Escary, JL, Nosal, F, Baychelier, F	Biochemistry	2004
17969444	The receptor of the type I interferon family Pellegrini, S, Piehler, J, Schreiber, G, Uzé, G	Curr Top Microbiol Immunol	2007
15312780	Ligand-induced assembling of the type I interferon receptor on supported lipid bilayers Piehler, J, Gavutis, M, Lata, S, Lamken, P	J Mol Biol	2004