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HIV-1 capsids bind and exploit the kinesin-1 adaptor FEZ1 for inward movement to the nucleus

Author

Listed:
  • Viacheslav Malikov

    (Northwestern University Feinberg School of Medicine
    Columbia University)

  • Eveline Santos da Silva

    (Northwestern University Feinberg School of Medicine)

  • Vladimir Jovasevic

    (Northwestern University Feinberg School of Medicine)

  • Geoffrey Bennett

    (Columbia University
    Present address: Howard Hughes Medical Institute, Laboratory of RNA Molecular Biology, Rockefeller University, New York, New York 10065, USA)

  • Daniel A. de Souza Aranha Vieira

    (Albert Einstein College of Medicine)

  • Bianca Schulte

    (Albert Einstein College of Medicine)

  • Felipe Diaz-Griffero

    (Albert Einstein College of Medicine)

  • Derek Walsh

    (Northwestern University Feinberg School of Medicine)

  • Mojgan H. Naghavi

    (Northwestern University Feinberg School of Medicine
    Columbia University)

Abstract

Intracellular transport of cargos, including many viruses, involves directed movement on microtubules mediated by motor proteins. Although a number of viruses bind motors of opposing directionality, how they associate with and control these motors to accomplish directed movement remains poorly understood. Here we show that human immunodeficiency virus type 1 (HIV-1) associates with the kinesin-1 adaptor protein, Fasiculation and Elongation Factor zeta 1 (FEZ1). RNAi-mediated FEZ1 depletion blocks early infection, with virus particles exhibiting bi-directional motility but no net movement to the nucleus. Furthermore, both dynein and kinesin-1 motors are required for HIV-1 trafficking to the nucleus. Finally, the ability of exogenously expressed FEZ1 to promote early HIV-1 infection requires binding to kinesin-1. Our findings demonstrate that opposing motors both contribute to early HIV-1 movement and identify the kinesin-1 adaptor, FEZ1 as a capsid-associated host regulator of this process usurped by HIV-1 to accomplish net inward movement towards the nucleus.

Suggested Citation

  • Viacheslav Malikov & Eveline Santos da Silva & Vladimir Jovasevic & Geoffrey Bennett & Daniel A. de Souza Aranha Vieira & Bianca Schulte & Felipe Diaz-Griffero & Derek Walsh & Mojgan H. Naghavi, 2015. "HIV-1 capsids bind and exploit the kinesin-1 adaptor FEZ1 for inward movement to the nucleus," Nature Communications, Nature, vol. 6(1), pages 1-13, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7660
    DOI: 10.1038/ncomms7660
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    Cited by:

    1. Alex Kleinpeter & Donna L. Mallery & Nadine Renner & Anna Albecka & J. Ole Klarhof & Eric O. Freed & Leo C. James, 2024. "HIV-1 adapts to lost IP6 coordination through second-site mutations that restore conical capsid assembly," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Feng Gu & Marie Boisjoli & Mojgan H. Naghavi, 2023. "HIV-1 promotes ubiquitination of the amyloidogenic C-terminal fragment of APP to support viral replication," Nature Communications, Nature, vol. 14(1), pages 1-19, December.

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