OASL binds DDX58

Stable Identifier
Reaction [binding]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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

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

Immunity 2014
Orthologous Events
Cite Us!