Abstract
Ubiquitination is a post-translational modification regulating critical cellular processes such as protein degradation, trafficking and signaling pathways, including activation of the innate immune response. Therefore, viruses, and particularly influenza A virus (IAV), have evolved different mechanisms to counteract this system to perform proper infection. Among IAV proteins, the non-structural protein NS1 is shown to be one of the main virulence factors involved in these viral hijackings. NS1 is notably able to inhibit the host’s antiviral response through the perturbation of ubiquitination in different ways, as discussed in this review.
Highlights
Cell Biology Laboratory, Research Institute for Biosciences, Research Institute for Health Sciences and Technology, Abstract: Ubiquitination is a post-translational modification regulating critical cellular processes such as protein degradation, trafficking and signaling pathways, including activation of the innate immune response
K48-linked poly-ubiquitination leads to targeted protein degradation by the 26S proteasome, releasing free ubiquitins, The number of each enzyme implied in this system reflects their specificity: to date, which are reincorporated in loop used other pathways
These activated factors associate with IRF9 to form an ISG factor 3 (ISGF3) complex that translocates into the nucleus where it binds to IFN-stimulated response element (ISRE) sequences in ISG promoters to induce their transcription (Figure 2) [164,166]
Summary
Ubiquitin is a small 8.5 kDa protein consisting of 76 amino acids, expressed in almost every cell type and largely conserved through eukaryotes. The ubiquitin ligase E3 catalyzes an isopeptide bond between the ubiquitin molecule and a lysine on the protein substrate [3,4,5]. DUBs are able to hydrolyze isopeptide bonds formed between ubiquitin and the protein substrate or between ubiquitin moieties, with substrate and linkage specificity [10,11]. This allows the recycling of ubiquitin molecules in the cell and other crucial cellular. K48-linked poly-ubiquitination leads to targeted protein degradation by the 26S proteasome, releasing free ubiquitins, The number of each enzyme implied in this system reflects their specificity: to date, which are reincorporated in loop used other pathways. Besides the UPS, there are other systems implying ubiquitin-like and E1, E2 and E3 enzyme-like proteins, such as SUMOylation, ISGylation or NEDDylation [27]
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