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Interferon alpha/beta receptor 2

Definition:

Together with IFNAR1, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response. Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another. The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (STAT1, STAT2 and STAT). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes.; [Isoform 3]: Potent inhibitor of type I IFN receptor activity.

References:

[1]. D Russell-Harde, et al. Formation of a uniquely stable type I interferon receptor complex by interferon beta is dependent upon particular interactions between interferon beta and its receptor and independent of tyrosine phosphorylation. Biochem Biophys Res Commun. 1999 Feb 16;255(2):539-44. [Content Brief]

[2]. Sharlene Velichko, et al. STAT3 activation by type I interferons is dependent on specific tyrosines located in the cytoplasmic domain of interferon receptor chain 2c. Activation of multiple STATS proceeds through the redundant usage of two tyrosine residues. J Biol Chem. 2002 Sep 20;277(38):35635-41. [Content Brief]

[3]. Jyothi Kumaran, et al. A structural basis for interferon-alpha-receptor interactions. FASEB J. 2007 Oct;21(12):3288-96. [Content Brief]

[4]. D Novick, et al. Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor. J Leukoc Biol. 1995 May;57(5):712-8. [Content Brief]

[5]. D Novick, et al. The human interferon alpha/beta receptor: characterization and molecular cloning. Cell. 1994 May 6;77(3):391-400. [Content Brief]

[6]. Christopher J A Duncan, et al. Human IFNAR2 deficiency: Lessons for antiviral immunity. Sci Transl Med. 2015 Sep 30;7(307):307ra154. [Content Brief]

[7]. Qian Zhang, et al. Inborn errors of type I IFN immunity in patients with life-threatening COVID-19. Science. 2020 Oct 23;370(6515):eabd4570. [Content Brief]

[8]. Christoph Thomas, et al. Structural linkage between ligand discrimination and receptor activation by type I interferons. Cell. 2011 Aug 19;146(4):621-32. [Content Brief]

[9]. Kei-Ichiro Arimoto, et al. STAT2 is an essential adaptor in USP18-mediated suppression of type I interferon signaling. Nat Struct Mol Biol. 2017 Mar;24(3):279-289. [Content Brief]

[10]. X Li, et al. Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling. Mol Cell Biol. 1997 Apr;17(4):2048-56. [Content Brief]

[11]. J Piehler, et al. Mutational and structural analysis of the binding interface between type I interferons and their receptor Ifnar2. J Mol Biol. 1999 Nov 19;294(1):223-37. [Content Brief]

[12]. E Croze, et al. The human type I interferon receptor. Identification of the interferon beta-specific receptor-associated phosphoprotein. J Biol Chem. 1996 Dec 27;271(52):33165-8. [Content Brief]

[13]. P Domanski, et al. Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling. J Biol Chem. 1995 Sep 15;270(37):21606-11. [Content Brief]

[14]. T Charis Wagner, et al. Interferon signaling is dependent on specific tyrosines located within the intracellular domain of IFNAR2c. Expression of IFNAR2c tyrosine mutants in U5A cells. J Biol Chem. 2002 Jan 11;277(2):1493-9. [Content Brief]

[15]. L C Platanias, et al. Differences in interferon alpha and beta signaling. Interferon beta selectively induces the interaction of the alpha and betaL subunits of the type I interferon receptor. J Biol Chem. 1996 Sep 27;271(39):23630-3. [Content Brief]

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