Abstract
Viruses are obligatory cellular parasites. Their mission is to enter a host cell, to transfer the viral genome, and to replicate progeny whilst diverting cellular immunity. The role of ubiquitin is to regulate fundamental cellular processes such as endocytosis, protein degradation, and immune signaling. Many viruses including influenza A virus (IAV) usurp ubiquitination and ubiquitin-like modifications to establish infection. In this focused review, we discuss how ubiquitin and unanchored ubiquitin regulate IAV host cell entry, and how histone deacetylase 6 (HDAC6), a cytoplasmic deacetylase with ubiquitin-binding activity, mediates IAV capsid uncoating. We also discuss the roles of ubiquitin in innate immunity and its implications in the IAV life cycle.
Highlights
histone deacetylase 6 (HDAC6), unanchored ubiquitin chains are implicated in retinoic acid-inducible gene 1 (RIG-I) immune signaling and NACHT, LRR and PYD
This is because DUBs such as ataxin-3 [63] and Poh1 [12] that generate unanchored ubiquitin chains are required for HDAC6-mediated aggresome processing
influenza A virus (IAV) cleaves off the HDAC6 ZnF-ubiquitin binding proteins (UBPs) by activating caspase 3 [83], which prevents premature capsid uncoating
Summary
8.5 kDa protein composed of 76 amino acids expressed in different tissues and present in different subcellular compartments. E3 ligases can be ubiquitin‐binding and substrate binding domains reside on separate polypeptides brought together single- or multi-subunit enzymes; in the second case ubiquitin-binding and substrate binding domains by adaptor proteins. Ubiquitinated substrates are subsequently recognized by a large number of proteins that contain different ubiquitin‐binding domains; among these are DUBs, a group of about 100 enzymes in different ubiquitin-binding domains;linkages amongbetween these are DUBs, moieties, a grouporofbetween about 100 enzymes mammals that hydrolyze isopeptide ubiquitin ubiquitin and in mammals that hydrolyze isopeptide linkages between ubiquitin or between ubiquitin and the the substrate. Hydrolytic activity of DUBs leads to recycling of Viruses 2016, 8, 293 mono-ubiquitin in the cell, and to generation of free ubiquitin chains, which regulate aggresome formation and innate immune signaling [12,13]
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