Anisotropic ESCRT-III architecture governs helical membrane tube formation

Joachim Moser von Filseck; Luca Barberi; Nathaniel Talledge; Isabel E. Johnson; Adam Frost; Martin Lenz; Aurélien Roux

doi:10.1038/s41467-020-15327-4

Nature Communications (May 2020)

Anisotropic ESCRT-III architecture governs helical membrane tube formation

Joachim Moser von Filseck,
Luca Barberi,
Nathaniel Talledge,
Isabel E. Johnson,
Adam Frost,
Martin Lenz,
Aurélien Roux

Affiliations

Joachim Moser von Filseck: Biochemistry Department, University of Geneva
Luca Barberi: LPTMS, CNRS, Université Paris-Sud, Université Paris-Saclay
Nathaniel Talledge: Department of Biochemistry and Biophysics, University of California, San Francisco
Isabel E. Johnson: Department of Biochemistry and Biophysics, University of California, San Francisco
Adam Frost: Department of Biochemistry and Biophysics, University of California, San Francisco
Martin Lenz: LPTMS, CNRS, Université Paris-Sud, Université Paris-Saclay
Aurélien Roux: Biochemistry Department, University of Geneva

DOI: https://doi.org/10.1038/s41467-020-15327-4
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 9

Abstract

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ESCRT-III proteins assemble into ubiquitous membrane-remodeling polymers during many cellular processes. Here, the authors use cryo-ET, cryo-EM and mathematical modeling to reveal how the shape of the helical membrane tube arises from the assembly of two distinct bundles of helical filaments.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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