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Filamin-A regulates actin-dependent clustering of HIV receptors

AutorJiménez Baranda, Sonia; Gómez Moutón, Concepción; Rojas, A. M. ; Mira, Emilia; Lacalle, Rosa Ana; Valencia, Alfonso; Martínez-A, Carlos; Mañes, Santos
Fecha de publicaciónjul-2007
EditorNature Publishing Group
CitaciónNature Cell Biology 9(7): 838-846 (2007)
ResumenHuman immunodeficiency virus (HIV)-1 infection requires envelope (Env) glycoprotein gp120-induced clustering of CD4 and coreceptors (CCR5 or CXCR4) on the cell surface; this enables Env gp41 activation and formation of a complex that mediates fusion between Env-containing and target-cell membranes1. Kinetic studies show that viral receptors are actively transported to the Env-receptor interface in a process that depends on plasma membrane composition and the actin cytoskeleton2, 3, 4, 5, 6, 7. The mechanisms by which HIV-1 induces F-actin rearrangement in the target cell remain largely unknown. Here, we show that CD4 and the coreceptors interact with the actin-binding protein filamin-A, whose binding to HIV-1 receptors regulates their clustering on the cell surface. We found that gp120 binding to cell receptors induces transient cofilin-phosphorylation inactivation through a RhoA–ROCK-dependent mechanism. Blockade of filamin-A interaction with CD4 and/or coreceptors inhibits gp120-induced RhoA activation and cofilin inactivation. Our results thus identify filamin-A as an adaptor protein that links HIV-1 receptors to the actin cytoskeleton remodelling machinery, which may facilitate virus infection.
Versión del editorhttp://doi.org/10.1038/ncb1610
URIhttp://hdl.handle.net/10261/153672
DOI10.1038/ncb1610
ISSN1465-7392
E-ISSN1476-4679
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