Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair
File(s)
Published version
Author(s)
Type
Journal Article
Abstract
The ESCRT-III-like protein Vipp1 couples filament polymerization with membrane remodeling. It assembles planar sheets as well as 3D rings and helical polymers, all implicated in mitigating plastid-associated membrane stress. The architecture of Vipp1 planar sheets and helical polymers remains unknown, as do the geometric changes required to transition between polymeric forms. Here we show how cyanobacterial Vipp1 assembles into morphologically-related sheets and spirals on membranes in vitro. The spirals converge to form a central ring similar to those described in membrane budding. Cryo-EM structures of helical filaments reveal a close geometric relationship between Vipp1 helical and planar lattices. Moreover, the helical structures reveal how filaments twist—a process required for Vipp1, and likely other ESCRT-III filaments, to transition between planar and 3D architectures. Overall, our results provide a molecular model for Vipp1 ring biogenesis and a mechanism for Vipp1 membrane stabilization and repair, with implications for other ESCRT-III systems.
Date Issued
2025-03-01
Date Acceptance
2024-09-11
Citation
Nature Structural and Molecular Biology, 2025, 32 (3), pp.571-584
ISSN
1545-9993
Publisher
Nature Research
Start Page
571
End Page
584
Journal / Book Title
Nature Structural and Molecular Biology
Volume
32
Issue
3
Copyright Statement
© The Author(s) 2024 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
License URL
Identifier
https://www.ncbi.nlm.nih.gov/pubmed/39528797
PII: 10.1038/s41594-024-01401-8
Subjects
Biochemistry & Molecular Biology
Biophysics
Cell Biology
ESCHERICHIA-COLI
IN-VITRO
Life Sciences & Biomedicine
OLIGOMERIZATION
PHAGE-SHOCK-PROTEIN
PLASTIDS 1
PSPA
REVEALS
Science & Technology
STRESS-PROTEIN
SYNECHOCYSTIS
VESICLE-INDUCING PROTEIN
Publication Status
Published
Coverage Spatial
United States
Date Publish Online
2024-11-11