Abstract
HIV-1 integrase (IN) is a key viral enzyme during HIV-1 replication that catalyzes the insertion of viral DNA into the host genome. Recent studies have provided important insights into the multiple posttranslational modifications (PTMs) of IN (e.g., ubiquitination, SUMOylation, acetylation and phosphorylation), which regulate its multifaceted functions. A number of host cellular proteins, including Lens Epithelium‑derived Growth factor (LEDGF/p75), p300 and Ku70 have been shown to interact with IN and be involved in the PTM process of IN, either facilitating or counteracting the IN PTMs. Although previous studies have revealed much about the important roles of IN PTMs, how IN functions are fine-tuned by these PTMs under the physiological setting still needs to be determined. Here, we review the advances in the understanding of the mechanisms and roles of multiple IN PTMs.
Highlights
Proteins translated from mRNA undergo various posttranslational modifications (PTMs) [1]
During HIV-1 infection, several viral proteins, including proteases, envelope glycoprotein, Tat and integrase (IN) undergo different types of PTMs, which greatly impact the different steps of viral replication [5,6,7,8,9,10,11,12]
This study provides direct evidence that IN is degraded through the K48-linked polyubiquitination proteasome pathway
Summary
Proteins translated from mRNA undergo various posttranslational modifications (PTMs) [1]. 15 of 20 amino acids (aa) can be modified in different ways (e.g., phosphorylation, methylation, acetylation, ADP-ribosylation, glycosylation, ubiquitination, SUMOylation and lipid additions) [1]. These modifications increase the functional diversity of the proteome and play crucial roles in the normal cell biology and disease outcomes. PTMs on IN play central roles in the functions of IN and viral replication, affecting the stability and conformational structure of IN, DNA binding of IN, integration and infection of the virus [5,10,11,12,18].
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