Actin-binding protein drebrin regulates HIV-1-triggered actin polymerization and viral infection

Mónica Gordón-Alonso; Vera Rocha-Perugini; Susana Álvarez; Ángeles Ursa; Nuria Izquierdo-Useros; Javier Martinez-Picado; María A. Muñoz-Fernández; Francisco Sánchez-Madrid

doi:10.1074/jbc.M113.494906

Actin-binding protein drebrin regulates HIV-1-triggered actin polymerization and viral infection

Mónica Gordón-Alonso, Vera Rocha-Perugini, Susana Álvarez, Ángeles Ursa, Nuria Izquierdo-Useros, Javier Martinez-Picado, María A. Muñoz-Fernández, Francisco Sánchez-Madrid

Department of Medicine

Research output: Contribution to journal › Article › Research › peer-review

24 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	28382-28397
Journal	Journal of Biological Chemistry
Volume	288
Issue number	39
DOIs	https://doi.org/10.1074/jbc.M113.494906
Publication status	Published - 27 Sep 2013

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Gordón-Alonso, Mónica ; Rocha-Perugini, Vera ; Álvarez, Susana ; Ursa, Ángeles ; Izquierdo-Useros, Nuria ; Martinez-Picado, Javier ; Muñoz-Fernández, María A. ; Sánchez-Madrid, Francisco. / Actin-binding protein drebrin regulates HIV-1-triggered actin polymerization and viral infection. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 39. pp. 28382-28397.

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title = "Actin-binding protein drebrin regulates HIV-1-triggered actin polymerization and viral infection",

abstract = "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. {\textcopyright} 2013 by The American Society for Biochemistry and Molecular Biology, Inc.",

author = "M{\'o}nica Gord{\'o}n-Alonso and Vera Rocha-Perugini and Susana {\'A}lvarez and {\'A}ngeles Ursa and Nuria Izquierdo-Useros and Javier Martinez-Picado and Mu{\~n}oz-Fern{\'a}ndez, {Mar{\'i}a A.} and Francisco S{\'a}nchez-Madrid",

year = "2013",

month = sep,

day = "27",

doi = "10.1074/jbc.M113.494906",

language = "English",

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Actin-binding protein drebrin regulates HIV-1-triggered actin polymerization and viral infection. / Gordón-Alonso, Mónica; Rocha-Perugini, Vera; Álvarez, Susana; Ursa, Ángeles; Izquierdo-Useros, Nuria; Martinez-Picado, Javier; Muñoz-Fernández, María A.; Sánchez-Madrid, Francisco.

In: Journal of Biological Chemistry, Vol. 288, No. 39, 27.09.2013, p. 28382-28397.

Research output: Contribution to journal › Article › Research › peer-review

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 -