OASL binds DDX58

Stable Identifier
R-HSA-8985153
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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Interferon-dependent antiviral mechanisms trigger activation of 5'-triphosphorylated 2'-5'oligoadenylate synthetase (OAS) proteins which bind double-stranded RNA and catalyze the synthesis of 5'-triphosphorylated 2'-5' oligoadenylates from ATP (Kristiansen et al. 2011). The p59 protein encoded by the OAS-like (OASL) gene is an atypical member of the OAS family in the sense that it lacks the characteristic 2'-5' oligoadenylate synthetase activity (Hartmann et al. 1998; Rebouillat et al. 1998). Furthermore, OASL contains two tandem ubiquitin-like domains (UBL) in the C-terminus, which are absent in other OAS proteins (Hartmann et al. 1998; Rebouillat et al. 1998). OASL is rapidly induced by virus infection via interferon regulatory factor 3 (IRF3) as well as by IFN signaling and has been shown to have antiviral activities, which requires the UBL domain (Melchjorsen et al. 2009; Sarkar and Sen 2004; Marques et al. 2008; Schoggins et al. 2011). OASL is thought to interact with and enhance RIG1 (DDX58) signaling through its C-terminal ubiquitin-like domain (UBL) by mimicking polyubiquitin (Zhu J et al. 2014). Loss of OASL expression reduced DDX58 signaling and enhanced virus replication in human cells. Conversely, OASL expression suppressed replication of a number of viruses in a DDX58-dependent manner and enhanced DDX58-mediated IFN induction (Zhu J et al. 2014).

Literature References
PubMed ID Title Journal Year
24931123 Antiviral activity of human OASL protein is mediated by enhancing signaling of the RIG-I RNA sensor

Zhu, J, Zhang, Y, Ghosh, A, Cuevas, RA, Forero, A, Dhar, J, Ibsen, MS, Schmid-Burgk, JL, Schmidt, T, Ganapathiraju, MK, Fujita, T, Hartmann, R, Barik, S, Hornung, V, Coyne, CB, Sarkar, SN

Immunity 2014
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