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Dynamic Association between HIV-1 Gag and Membrane Domains

HIV-1 particle assembly is driven by the structural protein Gag. Gag binds to and multimerizes on the inner leaflet of the plasma membrane, eventually resulting in formation of spherical particles. During virus spread among T cells, Gag accumulates to the plasma membrane domain that, together with t...

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Detalles Bibliográficos
Autores principales: Hogue, Ian B., Llewellyn, G. Nicholas, Ono, Akira
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3399408/
https://www.ncbi.nlm.nih.gov/pubmed/22830021
http://dx.doi.org/10.1155/2012/979765
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author Hogue, Ian B.
Llewellyn, G. Nicholas
Ono, Akira
author_facet Hogue, Ian B.
Llewellyn, G. Nicholas
Ono, Akira
author_sort Hogue, Ian B.
collection PubMed
description HIV-1 particle assembly is driven by the structural protein Gag. Gag binds to and multimerizes on the inner leaflet of the plasma membrane, eventually resulting in formation of spherical particles. During virus spread among T cells, Gag accumulates to the plasma membrane domain that, together with target cell membrane, forms a cell junction known as the virological synapse. While Gag association with plasma membrane microdomains has been implicated in virus assembly and cell-to-cell transmission, recent studies suggest that, rather than merely accumulating to pre-existing microdomains, Gag plays an active role in reorganizing the microdomains via its multimerization activity. In this paper, we will discuss this emerging view of Gag microdomain interactions. Relationships between Gag multimerization and microdomain association will be further discussed in the context of Gag localization to T-cell uropods and virological synapses.
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spelling pubmed-33994082012-07-24 Dynamic Association between HIV-1 Gag and Membrane Domains Hogue, Ian B. Llewellyn, G. Nicholas Ono, Akira Mol Biol Int Review Article HIV-1 particle assembly is driven by the structural protein Gag. Gag binds to and multimerizes on the inner leaflet of the plasma membrane, eventually resulting in formation of spherical particles. During virus spread among T cells, Gag accumulates to the plasma membrane domain that, together with target cell membrane, forms a cell junction known as the virological synapse. While Gag association with plasma membrane microdomains has been implicated in virus assembly and cell-to-cell transmission, recent studies suggest that, rather than merely accumulating to pre-existing microdomains, Gag plays an active role in reorganizing the microdomains via its multimerization activity. In this paper, we will discuss this emerging view of Gag microdomain interactions. Relationships between Gag multimerization and microdomain association will be further discussed in the context of Gag localization to T-cell uropods and virological synapses. Hindawi Publishing Corporation 2012 2012-07-05 /pmc/articles/PMC3399408/ /pubmed/22830021 http://dx.doi.org/10.1155/2012/979765 Text en Copyright © 2012 Ian B. Hogue et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Hogue, Ian B.
Llewellyn, G. Nicholas
Ono, Akira
Dynamic Association between HIV-1 Gag and Membrane Domains
title Dynamic Association between HIV-1 Gag and Membrane Domains
title_full Dynamic Association between HIV-1 Gag and Membrane Domains
title_fullStr Dynamic Association between HIV-1 Gag and Membrane Domains
title_full_unstemmed Dynamic Association between HIV-1 Gag and Membrane Domains
title_short Dynamic Association between HIV-1 Gag and Membrane Domains
title_sort dynamic association between hiv-1 gag and membrane domains
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3399408/
https://www.ncbi.nlm.nih.gov/pubmed/22830021
http://dx.doi.org/10.1155/2012/979765
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