Recruitment of STAT2 to p-IFNAR1

Stable Identifier
Reaction [binding]
Homo sapiens
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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).

Literature References
PubMed ID Title Journal Year
17251292 Respiratory syncytial virus NS1 protein degrades STAT2 by using the Elongin-Cullin E3 ligase

Power, UF, Johnston, JA, Touzelet, O, Stevenson, NJ, Elliott, J, Boyd, CR, Buick, R, Lynch, OT, Suessmuth, Y, Burrows, JF, Qian, P, Gadina, M

J Virol 2007
8605876 Phosphorylated interferon-alpha receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein

Gupta, S, Greenlund, AC, Krolewski, JJ, Yan, H, Schreiber, RD, Schindler, CW, Lim, JT, Krishnan, K

EMBO J 1996
This event is regulated