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Post-Translational Modifications of Retroviral HIV-1 Gag Precursors: An Overview of Their Biological Role
Protein post-translational modifications (PTMs) play key roles in eukaryotes since they finely regulate numerous mechanisms used to diversify the protein functions and to modulate their signaling networks. Besides, these chemical modifications also take part in the viral hijacking of the host, and a...
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| Published in: | International journal of molecular sciences 2021-03, Vol.22 (6), p.2871 |
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| container_title | International journal of molecular sciences |
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| creator | Bussienne, Charlotte Marquet, Roland Paillart, Jean-Christophe Bernacchi, Serena |
| description | Protein post-translational modifications (PTMs) play key roles in eukaryotes since they finely regulate numerous mechanisms used to diversify the protein functions and to modulate their signaling networks. Besides, these chemical modifications also take part in the viral hijacking of the host, and also contribute to the cellular response to viral infections. All domains of the human immunodeficiency virus type 1 (HIV-1) Gag precursor of 55-kDa (Pr55
), which is the central actor for viral RNA specific recruitment and genome packaging, are post-translationally modified. In this review, we summarize the current knowledge about HIV-1 Pr55
PTMs such as myristoylation, phosphorylation, ubiquitination, sumoylation, methylation, and ISGylation in order to figure out how these modifications affect the precursor functions and viral replication. Indeed, in HIV-1, PTMs regulate the precursor trafficking between cell compartments and its anchoring at the plasma membrane, where viral assembly occurs. Interestingly, PTMs also allow Pr55
to hijack the cell machinery to achieve viral budding as they drive recognition between viral proteins or cellular components such as the ESCRT machinery. Finally, we will describe and compare PTMs of several other retroviral Gag proteins to give a global overview of their role in the retroviral life cycle. |
| doi_str_mv | 10.3390/ijms22062871 |
| format | article |
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), which is the central actor for viral RNA specific recruitment and genome packaging, are post-translationally modified. In this review, we summarize the current knowledge about HIV-1 Pr55
PTMs such as myristoylation, phosphorylation, ubiquitination, sumoylation, methylation, and ISGylation in order to figure out how these modifications affect the precursor functions and viral replication. Indeed, in HIV-1, PTMs regulate the precursor trafficking between cell compartments and its anchoring at the plasma membrane, where viral assembly occurs. Interestingly, PTMs also allow Pr55
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), which is the central actor for viral RNA specific recruitment and genome packaging, are post-translationally modified. In this review, we summarize the current knowledge about HIV-1 Pr55
PTMs such as myristoylation, phosphorylation, ubiquitination, sumoylation, methylation, and ISGylation in order to figure out how these modifications affect the precursor functions and viral replication. Indeed, in HIV-1, PTMs regulate the precursor trafficking between cell compartments and its anchoring at the plasma membrane, where viral assembly occurs. Interestingly, PTMs also allow Pr55
to hijack the cell machinery to achieve viral budding as they drive recognition between viral proteins or cellular components such as the ESCRT machinery. 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Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bussienne, Charlotte</au><au>Marquet, Roland</au><au>Paillart, Jean-Christophe</au><au>Bernacchi, Serena</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Post-Translational Modifications of Retroviral HIV-1 Gag Precursors: An Overview of Their Biological Role</atitle><jtitle>International journal of molecular sciences</jtitle><addtitle>Int J Mol Sci</addtitle><date>2021-03-11</date><risdate>2021</risdate><volume>22</volume><issue>6</issue><spage>2871</spage><pages>2871-</pages><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Protein post-translational modifications (PTMs) play key roles in eukaryotes since they finely regulate numerous mechanisms used to diversify the protein functions and to modulate their signaling networks. Besides, these chemical modifications also take part in the viral hijacking of the host, and also contribute to the cellular response to viral infections. All domains of the human immunodeficiency virus type 1 (HIV-1) Gag precursor of 55-kDa (Pr55
), which is the central actor for viral RNA specific recruitment and genome packaging, are post-translationally modified. In this review, we summarize the current knowledge about HIV-1 Pr55
PTMs such as myristoylation, phosphorylation, ubiquitination, sumoylation, methylation, and ISGylation in order to figure out how these modifications affect the precursor functions and viral replication. Indeed, in HIV-1, PTMs regulate the precursor trafficking between cell compartments and its anchoring at the plasma membrane, where viral assembly occurs. Interestingly, PTMs also allow Pr55
to hijack the cell machinery to achieve viral budding as they drive recognition between viral proteins or cellular components such as the ESCRT machinery. Finally, we will describe and compare PTMs of several other retroviral Gag proteins to give a global overview of their role in the retroviral life cycle.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>33799890</pmid><doi>10.3390/ijms22062871</doi><orcidid>https://orcid.org/0000-0003-1647-8917</orcidid><orcidid>https://orcid.org/0000-0001-6223-4476</orcidid><orcidid>https://orcid.org/0000-0003-2824-8326</orcidid><orcidid>https://orcid.org/0000-0002-4209-3976</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Biochemistry, Molecular Biology Cell Membrane - metabolism Cell Membrane - virology Endosomal Sorting Complexes Required for Transport - genetics Eukaryotes gag Gene Products, Human Immunodeficiency Virus - genetics gag Gene Products, Human Immunodeficiency Virus - metabolism Gag protein Genomes HIV HIV-1 - genetics HIV-1 - metabolism Human immunodeficiency virus Humans Life Sciences Localization Membranes Methylation Microbiology and Parasitology Myristoylation Packaging Peptides Phosphorylation Post-translation Precursors Protein Precursors - genetics Protein Precursors - metabolism Protein Processing, Post-Translational Proteins Review Reviews RNA, Viral - genetics RNA, Viral - metabolism SUMO protein Translation Ubiquitination Virology Virus Assembly - genetics Virus Replication - genetics Viruses |
| title | Post-Translational Modifications of Retroviral HIV-1 Gag Precursors: An Overview of Their Biological Role |
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