Anisotropic ESCRT-III architecture governs helical membrane tube formation. Moser von Filseck, J.; Barberi, L.; Talledge, N.; Johnson, I. E.; Frost, A.; Lenz, M.; and Roux, A. Nature Communications, 11(1):1516, May, 2020. Number: 1 Publisher: Nature Publishing Group
Anisotropic ESCRT-III architecture governs helical membrane tube formation [link]Paper  doi  abstract   bibtex   
ESCRT-III proteins assemble into ubiquitous membrane-remodeling polymers during many cellular processes. Here we describe the structure of helical membrane tubes that are scaffolded by bundled ESCRT-III filaments. Cryo-ET reveals how the shape of the helical membrane tube arises from the assembly of two distinct bundles of helical filaments that have the same helical path but bind the membrane with different interfaces. Higher-resolution cryo-EM of filaments bound to helical bicelles confirms that ESCRT-III filaments can interact with the membrane through a previously undescribed interface. Mathematical modeling demonstrates that the interface described above is key to the mechanical stability of helical membrane tubes and helps infer the rigidity of the described protein filaments. Altogether, our results suggest that the interactions between ESCRT-III filaments and the membrane could proceed through multiple interfaces, to provide assembly on membranes with various shapes, or adapt the orientation of the filaments towards the membrane during membrane remodeling.
@article{moser_von_filseck_anisotropic_2020,
	title = {Anisotropic {ESCRT}-{III} architecture governs helical membrane tube formation},
	volume = {11},
	copyright = {2020 The Author(s)},
	issn = {2041-1723},
	url = {https://www.nature.com/articles/s41467-020-15327-4},
	doi = {10.1038/s41467-020-15327-4},
	abstract = {ESCRT-III proteins assemble into ubiquitous membrane-remodeling polymers during many cellular processes. Here we describe the structure of helical membrane tubes that are scaffolded by bundled ESCRT-III filaments. Cryo-ET reveals how the shape of the helical membrane tube arises from the assembly of two distinct bundles of helical filaments that have the same helical path but bind the membrane with different interfaces. Higher-resolution cryo-EM of filaments bound to helical bicelles confirms that ESCRT-III filaments can interact with the membrane through a previously undescribed interface. Mathematical modeling demonstrates that the interface described above is key to the mechanical stability of helical membrane tubes and helps infer the rigidity of the described protein filaments. Altogether, our results suggest that the interactions between ESCRT-III filaments and the membrane could proceed through multiple interfaces, to provide assembly on membranes with various shapes, or adapt the orientation of the filaments towards the membrane during membrane remodeling.},
	language = {en},
	number = {1},
	urldate = {2020-05-29},
	journal = {Nature Communications},
	author = {Moser von Filseck, Joachim and Barberi, Luca and Talledge, Nathaniel and Johnson, Isabel E. and Frost, Adam and Lenz, Martin and Roux, Aurélien},
	month = may,
	year = {2020},
	note = {Number: 1
Publisher: Nature Publishing Group},
	pages = {1516}
}
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