Dynamic Association between HIV-1 Gag and Membrane Domains.
Dynamic Association between HIV-1 Gag and Membrane Domains.
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DOI：
10.1155/2012/979765
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发表时间：
2012-01-01
期刊：
影响因子：
--
通讯作者：
Ono, Akira
中科院分区：
文献类型：
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作者：
Hogue, Ian B;Llewellyn, G Nicholas;Ono, Akira
HIV-1粒子组装由结构蛋白Gag驱动。Gag与质膜的内小叶结合并在其上多聚化，最终导致形成球形颗粒。在病毒在T细胞中传播期间，Gag积累到质膜结构域，其与靶细胞膜一起形成称为病毒学突触的细胞连接。虽然Gag与质膜微区的关联已经涉及病毒组装和细胞到细胞的传播，但最近的研究表明，Gag不仅仅积累到预先存在的微区，而是通过其多聚化活性在重组微区中发挥积极作用。在本文中，我们将讨论这一新兴的加格微区相互作用的观点。Gag多聚化和微结构域协会之间的关系将进一步讨论的背景下，Gag本地化的T细胞uropods和病毒突触。
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.