Table of Contents
Molecular Biology International
Volume 2012, Article ID 979765, 13 pages
http://dx.doi.org/10.1155/2012/979765
Review Article

Dynamic Association between HIV-1 Gag and Membrane Domains

1Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109, USA
2Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA
3Cellular and Molecular Biology Program, University of Michigan Medical School, Ann Arbor, MI 48109, USA
4Department of Molecular Microbiology and Immunology, University of Southern California, Los Angeles, CA 90033, USA

Received 8 April 2012; Accepted 1 June 2012

Academic Editor: Abdul A. Waheed

Copyright © 2012 Ian B. Hogue et al. 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.

Abstract

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.