Anisotropic ESCRT-III architecture governs helical membrane tube formation
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.
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2020-05-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-15327-4 |
| _version_ | 1818991392978894848 |
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| author | Joachim Moser von Filseck Luca Barberi Nathaniel Talledge Isabel E. Johnson Adam Frost Martin Lenz Aurélien Roux |
| author_facet | Joachim Moser von Filseck Luca Barberi Nathaniel Talledge Isabel E. Johnson Adam Frost Martin Lenz Aurélien Roux |
| author_sort | Joachim Moser von Filseck |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-20T20:09:33Z |
| format | Article |
| id | doaj.art-ffbbce3ca19e4ccbb4dd18d0ff5b656f |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-20T20:09:33Z |
| publishDate | 2020-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-ffbbce3ca19e4ccbb4dd18d0ff5b656f2022-12-21T19:27:52ZengNature PortfolioNature Communications2041-17232020-05-011111910.1038/s41467-020-15327-4Anisotropic ESCRT-III architecture governs helical membrane tube formationJoachim Moser von Filseck0Luca Barberi1Nathaniel Talledge2Isabel E. Johnson3Adam Frost4Martin Lenz5Aurélien Roux6Biochemistry Department, University of GenevaLPTMS, CNRS, Université Paris-Sud, Université Paris-SaclayDepartment of Biochemistry and Biophysics, University of California, San FranciscoDepartment of Biochemistry and Biophysics, University of California, San FranciscoDepartment of Biochemistry and Biophysics, University of California, San FranciscoLPTMS, CNRS, Université Paris-Sud, Université Paris-SaclayBiochemistry Department, University of GenevaESCRT-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.https://doi.org/10.1038/s41467-020-15327-4 |
| spellingShingle | Joachim Moser von Filseck Luca Barberi Nathaniel Talledge Isabel E. Johnson Adam Frost Martin Lenz Aurélien Roux Anisotropic ESCRT-III architecture governs helical membrane tube formation Nature Communications |
| title | Anisotropic ESCRT-III architecture governs helical membrane tube formation |
| title_full | Anisotropic ESCRT-III architecture governs helical membrane tube formation |
| title_fullStr | Anisotropic ESCRT-III architecture governs helical membrane tube formation |
| title_full_unstemmed | Anisotropic ESCRT-III architecture governs helical membrane tube formation |
| title_short | Anisotropic ESCRT-III architecture governs helical membrane tube formation |
| title_sort | anisotropic escrt iii architecture governs helical membrane tube formation |
| url | https://doi.org/10.1038/s41467-020-15327-4 |
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