Recruitment of STAT2 to p-IFNAR1

Phosphorylated tyrosine residue 466 on IFNAR1 acts as a docking site for STAT2. Latent STAT2 is recruited to this phosphotyrosine residue via its SH2 domain (Yan et al, 1996). Infection by human respiratory syncytial virus (hRSV) leads to loss of STAT2 by ubiquitination, catalyzed by a hRSV NS1 complex with elongin C (ELOC) and cullin-5 (CUL5) acting as an E3 ubiquitin ligase, and subsequent proteasomal STAT2 degradation (Elliott et al, 2007).

在IFNAR1上的磷酸化酪氨酸残基466充当STAT2的对接位点。隐匿状态的STAT2通过其SH2结构域（Yan et al, 1996）被招募至该磷酸化酪氨酸残基。人类呼吸道合胞病毒（hRSV）的感染导致STAT2通过泛素化丢失，此过程由hRSV NS1复合物与 elongin C（ELOC）和 cullin-5（CUL5）共同催化，其中ELOC和CUL5作为E3泛素连接酶，随后引发蛋白酶体介导的STAT2降解（Elliott et al, 2007）。