The Interferon-α/β Receptor 1 (IFN-α/β R1) is a receptor which binds Type I Interferons including Interferon-α and -β. It is a cell surface receptor and heteromeric receptor composed of one chain with two subunits referred to as IFNAR1 and IFNAR2. IFN-α/β R1, in association with IFN-α/β R2, is required for propagating antiviral signal transduction triggered by IFN-α and IFN-β. IFN-α/β R1 interacts very weakly or not at all with type 1 interferons and does not stably interact with IFN-α/β R2. Ligands associate with IFN-α/β R2, and this complex subsequently forms a stable ternary assembly with IFN-α/β R1. IFN-α/β R1 also associates with IFN-γ R2 even in the absence of IFN-γ stimulation. Human IFN-α/β R1 contains a nuclear localization signal in its extracellular domain that is required for receptor translocation to the nucleus following interaction with ligand. Interferon stimulation results in an immunologic response that is especially associated with viruses.
Component of the receptor for type I interferons, including interferons alpha, IFNB1 and IFNW1. Functions in general as heterodimer with IFNAR2 . Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha-and beta-subunits themselves. Can form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway.
Interferon-alpha/beta receptor beta chain (IFNAR2) is a type I membrane protein that forms one of the two chains of a receptor for interferons alpha and beta. Binding and activation of the receptor stimulates Janus protein kinases; which in turn phosphorylate several proteins; including STAT1 and STAT2. Initial cell-surface IFNAR2 expression at diagnosis assessed by flow cytometry widely distributed but showed overall significantly higher expression in CML patients when compared with normal controls. In 15 fresh patients who subsequently received IFNα therapy; IFNAR2 expression at diagnosis was significantly higher in cytogenetic good responders than in poor responders. Down-regulation of IFNAR2 expression during IFNα therapy was observed only in good responders but not in poor responders. The encoded protein also functions as an antiviral factor. IFNAR2 may associate with IFNAR1 to form the type I interferon receptor. This protein serves as a receptor for interferons alpha and beta. IFNAR2 is also involved in IFN-mediated STAT1; STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase; JAK1. Isoform 3 is a potent inhibitor of type I IFN receptor activity. Following binding of IFNα2; IFNAR2 is internalized; but; instead of being routed towards degradation as it is when complexed to IFNβ; it recycles back to the cell surface.
Interferon α/β Receptor 2 (IFN-α/β R2) is a single-pass type I membrane protein which belongs to the type II cytokine receptor family. It complexes with IFN-α/β R1 to form the signaling receptor complex for the family of α and β IFN subtypes. By alternative splicing; IFN-α/β R2 can exist as a secreted soluble protein or as a type I membrane protein. IFN-α/β R2 is the principal ligand binding subunit of the receptor. Ligand binding is stabilized by the subsequent association with IFN-α/β R1; resulting in the formation of a signaling ternary receptor complex. IFNAR2 was detected in most lymphocytes; monocytes; and granulocytes; although IFNAR2 expression was higher in the monocytes and granulocytes than in the lymphocytes. Among the lymphocyte subsets; IFNAR2 showed high expression in natural killer (NK) cells and low expression in T lymphocytes. Isoform 1 and isoform 3 of IFNAR2 are directly involved in signal transduction due to their interaction with the TYR kinase; JAK1. Isoform 1 also interacts with the transcriptional factors; STAT1 and STAT2. Both forms are potent inhibitors of type I IFN activity.
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