Reactome | Recruitment of STAT2 to p-IFNAR1

Recruitment of STAT2 to p-IFNAR1

Stable Identifier

R-HSA-909719

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cytosol, plasma membrane

ReviewStatus

5/5

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Disease (Homo sapiens)

- Infectious disease (Homo sapiens)
  - Viral Infection Pathways (Homo sapiens)
    - Respiratory Syncytial Virus Infection Pathway (Homo sapiens)
      - RSV-host interactions (Homo sapiens)
        
        Evasion by RSV of host interferon responses (Homo sapiens)
        
        Recruitment of STAT2 to p-IFNAR1 (Homo sapiens)

General

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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 Elliott, J, Lynch, OT, Suessmuth, Y, Qian, P, Boyd, CR, Burrows, JF, Buick, R, Stevenson, NJ, Touzelet, O, Gadina, M, Power, UF, Johnston, JA	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 Yan, H, Krishnan, K, Greenlund, AC, Gupta, S, Lim, JT, Schreiber, RD, Schindler, CW, Krolewski, JJ	EMBO J	1996