protein
| associating with TYK2 and positively influencing ligand binding to the receptor complex (catalytic activation of TYK2 is not essential for IFNAR1 internalization, but is required for ligand-induced IFNAR1 serine phosphorylation, ubiquitination and efficient lysosomal proteolysis) |
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TRAF2 rapidly binds to the IFNAR1 subunit of the IFN receptor upon IFN binding (role of TRAF2 binding to the type I interferon receptor in alternative NF kappaB activation and antiviral response) |
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intercating with IFNA1 (palmitoylation of IFNAR1 is required for the activation of STAT1 and STAT2 by IFNA1) |
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expression and kinase activity of PRKD2 are required for the ligand-inducible stimulation of IFNAR1 ubiquitination and endocytosis and for accelerated proteolytic turnover of IFNAR1 |
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PTPN1 is a specific regulator of IFNAR1 endocytosis stimulated by IFN1, but not by ligand-independent inducers of IFNAR1 ubiquitination |
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. PTPN1 is a specific regulator of IFNAR1 endocytosis stimulated by IFN1, but not by ligand-independent inducers of IFNAR1 ubiquitination |
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IFNB1 can uniquely and specifically ligate to IFNAR1 in an IFNAR2-independent manner |
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TYK2-IFNAR1 interface reveals an unexpected receptor-binding mode that mimics a SH2 domain-phosphopeptide interaction, with a glutamate replacing the canonical phosphotyrosine residue |
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ZG16B conferred resistance to pancreatic cancer cells against oncolytic parvovirus H-1 infection through IFNAR1-mediated signaling |