Publication

VPS4 triggers constriction and cleavage of ESCRT-III helical filaments

Maity, S., Caillat, C., Miguet, N., Sulbaran, G., Effantin, G., Schoehn, G., Roos, W. H. & Weissenhorn, W., 3-Apr-2019, In : Science Advances. 5, 4, p. eaau7198

Research output: Contribution to journalArticleAcademicpeer-review

APA

Maity, S., Caillat, C., Miguet, N., Sulbaran, G., Effantin, G., Schoehn, G., ... Weissenhorn, W. (2019). VPS4 triggers constriction and cleavage of ESCRT-III helical filaments. Science Advances, 5(4), eaau7198. https://doi.org/10.1126/sciadv.aau7198

Author

Maity, Sourav ; Caillat, Christophe ; Miguet, Nolwenn ; Sulbaran, Guidenn ; Effantin, Gregory ; Schoehn, Guy ; Roos, Wouter H ; Weissenhorn, Winfried. / VPS4 triggers constriction and cleavage of ESCRT-III helical filaments. In: Science Advances. 2019 ; Vol. 5, No. 4. pp. eaau7198.

Harvard

Maity, S, Caillat, C, Miguet, N, Sulbaran, G, Effantin, G, Schoehn, G, Roos, WH & Weissenhorn, W 2019, 'VPS4 triggers constriction and cleavage of ESCRT-III helical filaments', Science Advances, vol. 5, no. 4, pp. eaau7198. https://doi.org/10.1126/sciadv.aau7198

Standard

VPS4 triggers constriction and cleavage of ESCRT-III helical filaments. / Maity, Sourav; Caillat, Christophe; Miguet, Nolwenn; Sulbaran, Guidenn; Effantin, Gregory; Schoehn, Guy; Roos, Wouter H; Weissenhorn, Winfried.

In: Science Advances, Vol. 5, No. 4, 03.04.2019, p. eaau7198.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Maity S, Caillat C, Miguet N, Sulbaran G, Effantin G, Schoehn G et al. VPS4 triggers constriction and cleavage of ESCRT-III helical filaments. Science Advances. 2019 Apr 3;5(4):eaau7198. https://doi.org/10.1126/sciadv.aau7198


BibTeX

@article{9741907306614a12a78d8de5d4aa9f18,
title = "VPS4 triggers constriction and cleavage of ESCRT-III helical filaments",
abstract = "Many cellular processes such as endosomal vesicle budding, virus budding, and cytokinesis require extensive membrane remodeling by the endosomal sorting complex required for transport III (ESCRT-III). ESCRT-III protein family members form spirals with variable diameters in vitro and in vivo inside tubular membrane structures, which need to be constricted to proceed to membrane fission. Here, we show, using high-speed atomic force microscopy and electron microscopy, that the AAA-type adenosine triphosphatase VPS4 constricts and cleaves ESCRT-III CHMP2A-CHMP3 helical filaments in vitro. Constriction starts asymmetrically and progressively decreases the diameter of CHMP2A-CHMP3 tubular structure, thereby coiling up the CHMP2A-CHMP3 filaments into dome-like end caps. Our results demonstrate that VPS4 actively constricts ESCRT-III filaments and cleaves them before their complete disassembly. We propose that the formation of ESCRT-III dome-like end caps by VPS4 within a membrane neck structure constricts the membrane to set the stage for membrane fission.",
author = "Sourav Maity and Christophe Caillat and Nolwenn Miguet and Guidenn Sulbaran and Gregory Effantin and Guy Schoehn and Roos, {Wouter H} and Winfried Weissenhorn",
year = "2019",
month = "4",
day = "3",
doi = "10.1126/sciadv.aau7198",
language = "English",
volume = "5",
pages = "eaau7198",
journal = "Science Advances",
issn = "2375-2548",
publisher = "AMER ASSOC ADVANCEMENT SCIENCE",
number = "4",

}

RIS

TY - JOUR

T1 - VPS4 triggers constriction and cleavage of ESCRT-III helical filaments

AU - Maity, Sourav

AU - Caillat, Christophe

AU - Miguet, Nolwenn

AU - Sulbaran, Guidenn

AU - Effantin, Gregory

AU - Schoehn, Guy

AU - Roos, Wouter H

AU - Weissenhorn, Winfried

PY - 2019/4/3

Y1 - 2019/4/3

N2 - Many cellular processes such as endosomal vesicle budding, virus budding, and cytokinesis require extensive membrane remodeling by the endosomal sorting complex required for transport III (ESCRT-III). ESCRT-III protein family members form spirals with variable diameters in vitro and in vivo inside tubular membrane structures, which need to be constricted to proceed to membrane fission. Here, we show, using high-speed atomic force microscopy and electron microscopy, that the AAA-type adenosine triphosphatase VPS4 constricts and cleaves ESCRT-III CHMP2A-CHMP3 helical filaments in vitro. Constriction starts asymmetrically and progressively decreases the diameter of CHMP2A-CHMP3 tubular structure, thereby coiling up the CHMP2A-CHMP3 filaments into dome-like end caps. Our results demonstrate that VPS4 actively constricts ESCRT-III filaments and cleaves them before their complete disassembly. We propose that the formation of ESCRT-III dome-like end caps by VPS4 within a membrane neck structure constricts the membrane to set the stage for membrane fission.

AB - Many cellular processes such as endosomal vesicle budding, virus budding, and cytokinesis require extensive membrane remodeling by the endosomal sorting complex required for transport III (ESCRT-III). ESCRT-III protein family members form spirals with variable diameters in vitro and in vivo inside tubular membrane structures, which need to be constricted to proceed to membrane fission. Here, we show, using high-speed atomic force microscopy and electron microscopy, that the AAA-type adenosine triphosphatase VPS4 constricts and cleaves ESCRT-III CHMP2A-CHMP3 helical filaments in vitro. Constriction starts asymmetrically and progressively decreases the diameter of CHMP2A-CHMP3 tubular structure, thereby coiling up the CHMP2A-CHMP3 filaments into dome-like end caps. Our results demonstrate that VPS4 actively constricts ESCRT-III filaments and cleaves them before their complete disassembly. We propose that the formation of ESCRT-III dome-like end caps by VPS4 within a membrane neck structure constricts the membrane to set the stage for membrane fission.

U2 - 10.1126/sciadv.aau7198

DO - 10.1126/sciadv.aau7198

M3 - Article

VL - 5

SP - eaau7198

JO - Science Advances

JF - Science Advances

SN - 2375-2548

IS - 4

ER -

ID: 80390498