HIV-1, ubiquitin and ubiquitin-like proteins: The dialectic interactions of a virus with a sophisticated network of post-translational modifications

摘要

The modification of intracellular proteins by ubiquitin (Ub) and ubiquitin-like (UbL) proteins is a central mechanism for regulating and fine-tuning all cellular processes. Indeed, these modifications are widely used to control the stability, activity and localisation of many key proteins and, therefore, they are instrumental in regulating cellular functions as diverse as protein degradation, cell signalling, vesicle trafficking and immune response. It is thus no surprise that pathogens in general, and viruses in particular, have developed multiple strategies to either counteract or exploit the complex mechanisms mediated by the Ub and UbL protein conjugation pathways. The aim of this review is to provide an overview on the intricate and conflicting relationships that intimately link HIV-1 and these sophisticated systems of post-translational modifications. For productive infection, HIV-1 must deal with the sophisticated systems of post-translational modifications employing ubiquitin and ubiquitin-like proteins, which are instrumental for the control of most cellular processes, including protein degradation, cell signalling, transcriptional regulation, vesicle trafficking and immune response. This review aims at providing an integrated view of the many strategies that the virus developed to either counteract or exploit these complex mechanisms.