Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation.

Autor: Bertin A; Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France. aurelie.bertin@curie.fr.; Sorbonne Université, 75005, Paris, France. aurelie.bertin@curie.fr., de Franceschi N; Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France. N.deFranceschi@tudelft.nl.; Sorbonne Université, 75005, Paris, France. N.deFranceschi@tudelft.nl.; Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, avenue des Martyrs, 38000, Grenoble, France. N.deFranceschi@tudelft.nl., de la Mora E; Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.; Sorbonne Université, 75005, Paris, France., Maity S; Moleculaire Biofysica, Zernike Instituut, Rijksuniversiteit Groningen, Nijenborgh 4, 9747, AG Groningen, The Netherlands., Alqabandi M; Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.; Sorbonne Université, 75005, Paris, France., Miguet N; Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, avenue des Martyrs, 38000, Grenoble, France., di Cicco A; Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.; Sorbonne Université, 75005, Paris, France., Roos WH; Moleculaire Biofysica, Zernike Instituut, Rijksuniversiteit Groningen, Nijenborgh 4, 9747, AG Groningen, The Netherlands., Mangenot S; Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France.; Sorbonne Université, 75005, Paris, France., Weissenhorn W; Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, avenue des Martyrs, 38000, Grenoble, France. winfried.weissenhorn@ibs.fr., Bassereau P; Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005, Paris, France. patricia.bassereau@curie.fr.; Sorbonne Université, 75005, Paris, France. patricia.bassereau@curie.fr.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2020 May 29; Vol. 11 (1), pp. 2663. Date of Electronic Publication: 2020 May 29.
DOI: 10.1038/s41467-020-16368-5
Abstrakt: 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.
Databáze: MEDLINE
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