Obtain This Scoop On The GPX5 Before You're Too Late

, 2001). This inhibition can be attributed to the fact that TMEV infection disallows the formation of IRF-3 dimers, which normally translocate to the nucleus to regulate transcription of antiviral genes (IFN-��/�� as well as ISGs) in response to infection. Because infection with TMEV containing a mutation in the zinc finger motif of L or a partial deletion of L allows the dimerization of IRF-3 but wild type TMEV infection does not, the inability of this nuclear translocation and subsequent antiviral protein production can be attributed to antagonizing this pathway by the L protein. Moreover, disruptions in nucleocytoplasmic trafficking and the block to mRNA export from the nucleus correlate with Nup 98 hyper-phosphorylation (Ricour et al., 2009a). The leader protein of mengovirus has also been demonstrated to inhibit IFN-��/�� expression in infected cells by suppressing the activation of NF-��B, a suppression dependent upon phosphorylation of Thr-47 in the L protein (Zoll et al., 2002). Interestingly, negative-sense RNA complementary to the L coding region of the EMCV genome was recently shown to be a determinant of MDA-5 mediated interferon production (Deddouche et al., 2014). Finally, the L proteinase of FMDV functions in the inhibition of IFN-�� mRNA induction. However, this inhibition is not dependent upon the dysregulation of cellular nucleocytoplasmic trafficking because FMDV does not target these pathways. Instead, the FMDV L proteinase enters the nucleus and promotes the degradation of an NF-��B component (De Los Santos et al., 2006, 2007). The redistribution of cellular proteins as a result of infection is not necessarily specific Because fundamental components and regulatory mechanisms of nucleocytoplasmic trafficking are disrupted during picornavirus infection, some proteins that relocalize to the GPX5 cytoplasm of infected cells have no known function in viral replication, and in some instances even have antiviral roles. AU-rich binding factor 1 (AUF1, also known as hnRNP D0) binds with high affinity to RNA molecules containing AU-rich elements (usually in the 3�� non-translated region), is a predominantly nuclear-resident protein that shuttles to the cytoplasm, and promotes mRNA turnover (reviewed in Gratac��s and Brewer, 2010). AUF1 relocalizes from the nucleus to the cytoplasm of poliovirus, HRV 14, and HRV 16 infected cells in a 2A-driven manner and binds to S-L IV within the IRES of poliovirus RNA (Rozovics et al., 2012; Cathcart et al., 2013). The presence of this protein inhibits poliovirus translation in a dose dependent manner in vitro, and cells lacking AUF1 produce higher titers of poliovirus, CVB3, and HRV 1a (Cathcart et al., 2013). The enteroviral proteinase precursor 3CD and mature 3C cleave AUF1 in vitro, leading to a decrease in the affinity of AUF1 for poliovirus S-L IV (Cathcart et al., 2013; Wong et al., 2013).