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Review Article

Inside job: how the ESCRTs release HIV-1 from infected cells

James H. Hurley, A. King Cada
Biochemical Society Transactions Aug 28, 2018, 46 (5) 1029-1036; DOI: 10.1042/BST20180019
James H. Hurley
Department of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, U.S.A.Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, U.S.A.
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  • For correspondence: jimhurley@berkeley.edu
A. King Cada
Department of Molecular and Cell Biology and California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, U.S.A.
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Abstract

Human immunodeficiency virus type 1 (HIV-1) hijacks the host endosomal sorting complex required for transport (ESCRT) proteins in order to release infectious viral particles from the cell. ESCRT recruitment is virtually essential for the production of infectious virus, despite that the main structural protein of HIV-1, Gag, is capable of self-assembling and eventually budding from membranes on its own. Recent data have reinforced the paradigm of ESCRT-dependent particle release while clarifying why this rapid release is so critical. The ESCRTs were originally discovered as integral players in endosome maturation and are now implicated in many important cellular processes beyond viral and endosomal budding. Nearly all of these roles have in common that membrane scission occurs from the inward face of the membrane neck, which we refer to as ‘reverse topology’ scission. A satisfactory mechanistic description of reverse-topology membrane scission by ESCRTs remains a major challenge both in general and in the context of HIV-1 release. New observations concerning the fundamental scission mechanism for ESCRTs in general, and the process of HIV-1 release specifically, have generated new insights in both directions, bringing us closer to a mechanistic understanding.

  • in vitro reconstitution
  • live cell imaging
  • membrane biophysics
  • membrane curvature
  • membrane scission
  • retroviruses
  • Abbreviations

    AAA+,
    ATPases associated with various cellular activities;
    ALIX,
    apoptosis-linked gene 2-interacting protein X;
    CA,
    capsid protein p24;
    CHMP,
    charged multivesicular body protein;
    ESCRT,
    endosomal sorting complex required for transport;
    HIV-1,
    Human immunodeficiency virus type 1;
    MA,
    matrix protein p17;
    NC,
    nucleocapsid protein p7;
    PI(4,5)P2,
    phosphatidylinositol (4,5)-bisphosphate;
    PM,
    plasma membrane;
    PR,
    viral protease;
    RT,
    reverse-transcriptase;
    TSG101,
    tumor susceptibility gene 101;
    UBD,
    ubiquitin binding domain;
    UEV,
    ubiquitin-conjugating enzyme E2 variant;
    VLP,
    virus-like particle;
    VPS,
    vacuolar protein sorting-associated protein
    • © 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
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    October 2018

    Volume: 46 Issue: 5

    Biochemical Society Transactions: 46 (5)
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    Inside job: how the ESCRTs release HIV-1 from infected cells
    James H. Hurley, A. King Cada
    Biochemical Society Transactions Oct 2018, 46 (5) 1029-1036; DOI: 10.1042/BST20180019
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    Inside job: how the ESCRTs release HIV-1 from infected cells
    James H. Hurley, A. King Cada
    Biochemical Society Transactions Oct 2018, 46 (5) 1029-1036; DOI: 10.1042/BST20180019

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    • Article
      • Abstract
      • Introduction and history
      • Why bother with ESCRTs?
      • Circuitry of ESCRT recruitment
      • The topology of ESCRTs in HIV budding
      • How do ESCRTs cut membrane necks?
      • Concluding remarks
      • Funding
      • Competing Interests
      • Acknowledgements
      • References
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    Keywords

    in vitro reconstitution
    live cell imaging
    membrane biophysics
    membrane curvature
    membrane scission
    retroviruses

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