The PDZ-adaptor protein syntenin-1 regulates HIV-1 entry

Mónica Gordón-Alonso, Vera Rocha-Perugini, Susana Álvarez, Olga Moreno-Gonzalo, Ángeles Ursa, Soraya López-Martín, Nuria Izquierdo-Useros, Javier Martínez-Picado, Maria Ángeles Muñoz-Fernández, María Yáñez-Mó, Francisco Sánchez-Madrid

Research output: Contribution to journalArticleResearchpeer-review

31 Citations (Scopus)


Syntenin-1 is a cytosolic adaptor protein involved in several cellular processes requiring polarization. Human immunodeficiency virus type 1 (HIV-1) attachment to target CD4 + T-cells induces polarization of the viral receptor and coreceptor, CD4/CXCR4, and cellular structures toward the virus contact area, and triggers local actin polymerization and phosphatidylinositol 4,5-bisphosphate (PIP 2) production, which are needed for successful HIV infection. We show that syntenin-1 is recruited to the plasma membrane during HIV-1 attachment and associates with CD4, the main HIV-1 receptor. Syntenin-1 overexpression inhibits HIV-1 production and HIV-mediated cell fusion, while syntenin depletion specifically increases HIV-1 entry. Down-regulation of syntenin-1 expression reduces F-actin polymerization in response to HIV-1. Moreover, HIV-induced PIP 2 accumulation is increased in syntenin-1-depleted cells. Once the virus has entered the target cell, syntenin-1 polarization toward the viral nucleocapsid is lost, suggesting a spatiotemporal regulatory role of syntenin-1 in actin remodeling, PIP2 production, and the dynamics of HIV-1 entry. © 2012 Gordón-Alonso et al.
Original languageEnglish
Pages (from-to)2253-2263
JournalMolecular Biology of the Cell
Issue number12
Publication statusPublished - 15 Jun 2012


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