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

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 phosp...

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Autores principales: Zheng, Yingfeng, Yao, Xiaojian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3738961/
https://www.ncbi.nlm.nih.gov/pubmed/23863879
http://dx.doi.org/10.3390/v5071787
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author Zheng, Yingfeng
Yao, Xiaojian
author_facet Zheng, Yingfeng
Yao, Xiaojian
author_sort Zheng, Yingfeng
collection PubMed
description 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.
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spelling pubmed-37389612013-08-09 Posttranslational Modifications of HIV-1 Integrase by Various Cellular Proteins during Viral Replication Zheng, Yingfeng Yao, Xiaojian Viruses Review 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. MDPI 2013-07-16 /pmc/articles/PMC3738961/ /pubmed/23863879 http://dx.doi.org/10.3390/v5071787 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Zheng, Yingfeng
Yao, Xiaojian
Posttranslational Modifications of HIV-1 Integrase by Various Cellular Proteins during Viral Replication
title Posttranslational Modifications of HIV-1 Integrase by Various Cellular Proteins during Viral Replication
title_full Posttranslational Modifications of HIV-1 Integrase by Various Cellular Proteins during Viral Replication
title_fullStr Posttranslational Modifications of HIV-1 Integrase by Various Cellular Proteins during Viral Replication
title_full_unstemmed Posttranslational Modifications of HIV-1 Integrase by Various Cellular Proteins during Viral Replication
title_short Posttranslational Modifications of HIV-1 Integrase by Various Cellular Proteins during Viral Replication
title_sort posttranslational modifications of hiv-1 integrase by various cellular proteins during viral replication
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3738961/
https://www.ncbi.nlm.nih.gov/pubmed/23863879
http://dx.doi.org/10.3390/v5071787
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