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Cited by 163Microtubule and mitosis dynamicsCellular transport and secretionUbiquitin and proteasome pathways

ALIX and ESCRT-I/II function as parallel ESCRT-III recruiters in cytokinetic abscission

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Christ, Liliane, Wenzel, Eva M., Liestøl, Knut, Raiborg, Camilla, Campsteijn, Coen, Stenmark, Harald·2016·Journal of Cell Biology
DOI 10.1083/jcb.201507009PMC PMC4772496
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Abstract

Cytokinetic abscission, the final stage of cell division where the two daughter cells are separated, is mediated by the endosomal sorting complex required for transport (ESCRT) machinery. The ESCRT-III subunit CHMP4B is a key effector in abscission, whereas its paralogue, CHMP4C, is a component in the abscission checkpoint that delays abscission until chromatin is cleared from the intercellular bridge. How recruitment of these components is mediated during cytokinesis remains poorly understood, although the ESCRT-binding protein ALIX has been implicated. Here, we show that ESCRT-II and the ESCRT-II–binding ESCRT-III subunit CHMP6 cooperate with ESCRT-I to recruit CHMP4B, with ALIX providing a parallel recruitment arm. In contrast to CHMP4B, we find that recruitment of CHMP4C relies predominantly on ALIX. Accordingly, ALIX depletion leads to furrow regression in cells with chromosome bridges, a phenotype associated with abscission checkpoint signaling failure. Collectively, our work reveals a two-pronged recruitment of ESCRT-III to the cytokinetic bridge and implicates ALIX in abscission checkpoint signaling.

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  • ESCRT-I-ALIX interaction is essential to cytokinesis.

    “the ESCRT-I-ALIX interaction is essential to cytokinesis”

    From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [13]

    The Discussion (Figure 8 model; page not provided) describes ALIX and ESCRT-I as parallel recruitment arms, not an essential ESCRT-I–ALIX interaction. In the Results section on abscission timing, cells depleted of either ALIX or the ESCRT-I subunit TSG101 still completed abscission, albeit with delays; depleting both caused a much greater delay. (LLM, conf=0.86)

    Checked by a reasoning model — may be wrong.

    Experimental — accuracy not yet measured

  • Loss of ALIX recruitment to viral budding sites or cytokinetic bridges impairs but does not terminate these events.

    “the loss of ALIX recruitment to viral budding sites through HIV L domain deletion or to cytokinetic bridges via cellular depletion by RNA interference (RNAi) impairs but does not terminate these events.”

    From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [13]

    The Results section, “Relation between CHMP4B midbody recruitment and abscission timing” (page unavailable), reports that ALIX knockdown delayed cytokinetic abscission but did not prevent the measured cells from reaching it. The paper does not report whether deleting the HIV L domain impairs viral budding without terminating it, so the viral-budding part is unsupported by our copy. (LLM, conf=0.87)

    Experimental — accuracy not yet measured

  • Cytokinesis depends on cooperativity between TSG101 and ALIX.

    “cytokinesis, a process that displays many parallels with retroviral budding, depends on cooperativity between both TSG101 and ALIX”

    From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [13]

  • Retroviral budding and cytokinesis culminate with a topologically similar membrane abscission process.

    “Both processes of retroviral budding and cytokinesis culminate with a topologically similar membrane abscission process that separates progeny virions from host cell membranes and daughter cells from one another after cell division [13,14,15].”

    From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [13]

  • Redundant and parallel ESCRT-III recruiting axes are mandated.

    “This mandates the presence of redundant and parallel ESCRT-III recruiting axes perhaps fulfilled by the intermediary ESCRT-II complex [13,17,18] or additional ALIX homologs and orthologs [19,20,21].”

    From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [13]

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Authors
Christ, L., Wenzel, E. M., Liestøl, K., Raiborg, C., Campsteijn, C., & Stenmark, H.
Affiliations
  • Oslo University Hospital (NO)
  • University of Oslo (NO)
Corresponding author
  • Campsteijn, Coen
  • Stenmark, Harald
ORCID
Venue
Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2016-02-29
Volume
212
Issue
5
Pages
499-513
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
DOI
10.1083/jcb.201507009
PMC
PMC4772496
OpenAlex
W2292328544
Cited by
163
References
85
Citations by year
2026: 15 · 2025: 16 · 2024: 14 · 2023: 10 · 2022: 13 · 2021: 20 · 2020: 19 · 2019: 17 · 2018: 18 · 2017: 13 · 2016: 8
FWCI
12.86
Type
journal article
Language
en
Open access
Licence
cc-by-nc-sa
Locations
  • The Journal of Cell Biology (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
  • Helse Sør-Øst RHF (2015014)
  • Norwegian Cancer Society (4541899, 605009)
  • European Research Council (233146)
  • Norges Forskningsråd (179571)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords
cytokinetic abscission, ESCRT machinery, Alix, ESCRT-I, ESCRT-II, ESCRT-III, CHMP4B, CHMP4C, chromosome bridges, cytokinesis, protein recruitment
MeSH terms
Calcium-Binding Proteins, HeLa Cells, Humans, Tumor Cells, Cultured, Cell Cycle Proteins, Cytokinesis, Endosomal Sorting Complexes Required for Transport

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