Posttranslational Modifications of HIV-1 Integrase by Various Cellular Proteins during Viral Replication

Viruses

Yingfeng Zheng¹ 

[1] Laboratory of Molecular Human Retrovirology, Department of Medical Microbiology, University of Manitoba, 508-730 William Avenue, Winnipeg, R3E 0W3, Canada; E-Mail

关键词: HIV;    integrase;    posttranslational modification;    ubiquitination;    SUMOylation;    acetylation;    phosphorylation;   

DOI  :  10.3390/v5071787

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland.