TY - JOUR
T1 - Actin-binding protein drebrin regulates HIV-1-triggered actin polymerization and viral infection
AU - Gordón-Alonso, Mónica
AU - Rocha-Perugini, Vera
AU - Álvarez, Susana
AU - Ursa, Ángeles
AU - Izquierdo-Useros, Nuria
AU - Martinez-Picado, Javier
AU - Muñoz-Fernández, María A.
AU - Sánchez-Madrid, Francisco
PY - 2013/9/27
Y1 - 2013/9/27
N2 - Background: Drebrin binds to F-actin and CXCR4 in T cells. Thus, it is a potential candidate for the modulation of HIV-1 infection. Results: Drebrin and CXCR4 accumulate at viral attachment areas. Drebrin knockdown decreases F-actin polymerization, and increases local profilin accumulation and HIV-1 infection. Conclusion: Drebrin inhibits HIV-1 entry by stabilizing HIV-1-triggered F-actin polymerization. Significance: Modulation of actin dynamics differentially regulates each viral step for an effective viral infection. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
AB - Background: Drebrin binds to F-actin and CXCR4 in T cells. Thus, it is a potential candidate for the modulation of HIV-1 infection. Results: Drebrin and CXCR4 accumulate at viral attachment areas. Drebrin knockdown decreases F-actin polymerization, and increases local profilin accumulation and HIV-1 infection. Conclusion: Drebrin inhibits HIV-1 entry by stabilizing HIV-1-triggered F-actin polymerization. Significance: Modulation of actin dynamics differentially regulates each viral step for an effective viral infection. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
U2 - 10.1074/jbc.M113.494906
DO - 10.1074/jbc.M113.494906
M3 - Article
VL - 288
SP - 28382
EP - 28397
IS - 39
ER -
