Journal
NATURE COMMUNICATIONS
Volume 11, Issue 1, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-020-16368-5
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Funding
- FINOVI
- ANR [ANR-14-CE09-0003-01, ANR-15-CE11-0027-02]
- Institut Curie
- Centre National de la Recherche Scientifique (CNRS)
- FRISBI [ANR-10-INBS-05-02]
- GRAL, a project of the University Grenoble Alpes graduate school (Ecoles Universitaires de Recherche) CBH-EUR-GS [ANR-17-EURE-0003]
- Equipement d'excellence CACSICE
- FRM
- GIS IBiSA
- iNEXT - Horizon 2020 program of the European Union [653706]
- France-BioImaging [ANR10-INBS-04]
- Marie Curie actions (MSCA-IF-2016) [751715]
- Universite Pierre et Marie Curie/Sorbonne Universite
- Doctoral school Physique en Ile de France [ED-564]
- Fondation pour la Recherche Medicale
- Grenoble Instruct-ERIC center (ISBG) within the Grenoble Partnership for Structural Biology (PSB) [UMS 3518 CNRS-CEA-UGA-EMBL]
- Marie Curie Actions (MSCA) [751715] Funding Source: Marie Curie Actions (MSCA)
- Agence Nationale de la Recherche (ANR) [ANR-14-CE09-0003, ANR-15-CE11-0027] Funding Source: Agence Nationale de la Recherche (ANR)
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Endosomal sorting complexes for transport-III (ESCRT-III) assemble in vivo onto membranes with negative Gaussian curvature. How membrane shape influences ESCRT-III polymerization and how ESCRT-III shapes membranes is yet unclear. Human core ESCRT-III proteins, CHMP4B, CHMP2A, CHMP2B and CHMP3 are used to address this issue in vitro by combining membrane nanotube pulling experiments, cryo-electron tomography and AFM. We show that CHMP4B filaments preferentially bind to flat membranes or to tubes with positive mean curvature. Both CHMP2B and CHMP2A/CHMP3 assemble on positively curved membrane tubes. Combinations of CHMP4B/CHMP2B and CHMP4B/CHMP2A/CHMP3 are recruited to the neck of pulled membrane tubes and reshape vesicles into helical corkscrew-like membrane tubes. Sub-tomogram averaging reveals that the ESCRT-III filaments assemble parallel and locally perpendicular to the tube axis, highlighting the mechanical stresses imposed by ESCRT-III. Our results underline the versatile membrane remodeling activity of ESCRT-III that may be a general feature required for cellular membrane remodeling processes.
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