ArticleProtein science : a publication of the Protein Society2020
Mechanisms of negative membrane curvature sensing and generation by ESCRT III subunit Snf7.
Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Functional reconstitution of bacterial ESCRT-III protein PspA identifies key regions in membrane binding and remodeling.Protein science : a publication of the Protein Society · 2025Article
- CHARMM at 45: Enhancements in Accessibility, Functionality, and Speed.The journal of physical chemistry. B · 2024Review
- Therapeutic Potential of Mesenchymal Stem Cell-Derived Exosomes as Nanomedicine for Peripheral Nerve Injury.International journal of molecular sciences · 2024Review
- Simulations suggest a scaffolding mechanism of membrane deformation by the caveolin 8S complex.Biophysical journal · 2023Article
- Insights into the function of ESCRT and its role in enveloped virus infection.Frontiers in microbiology · 2023Review
- Mechanism of negative membrane curvature generation by I-BAR domains.Structure (London, England : 1993) · 2021Article
- Mechanisms of negative membrane curvature sensing and generation by ESCRT III subunit Snf7.Protein science : a publication of the Protein Society · 2020Article
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Authors and funding
3 authors.
Funding
Abstract
Certain proteins have the propensity to bind to negatively curved membranes and generate negative membrane curvature. The mechanism of action of these proteins is much less studied and understood than those that sense and generate positive curvature. In this work, we use implicit membrane modeling to explore the mechanism of an important negative curvature sensing and generating protein: the main ESCRT III subunit Snf7. We find that Snf7 monomers alone can sense negative curvature and that curvature sensitivity increases for dimers and trimers. We have observed spontaneous bending of Snf7 oligomers into circular structures with preferred radius of ~20 nm. The preferred curvature of Snf7 filaments is further confirmed by the simulations of preformed spirals on a cylindrical membrane surface. Snf7 filaments cannot bind with the same interface to flat and curved membranes. We find that even when a filament has the preferred radius, it is always less stable on the flat membrane surface than on the interior cylindrical membrane surface. This provides an additional energy for membrane bending which has not been considered in the spiral spring model. Furthermore, the rings on the cylindrical spirals are bridged together by helix 4 and hence are extra stabilized compared to the spirals on the flat membrane surface.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.