ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural basis for the geometry-driven localization of a small protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.bioRxiv : the preprint server for biology · 2026Article
- Lipid packing and local geometry influence septin curvature sensing.The Journal of cell biology · 2026Article
- To Sporulate or Not to Sporulate: Developmental Checkpoints MonitoringAnnual review of microbiology · 2025Review
- Real-time nanoscale investigation of spore coat assembly in Bacillus subtilis.Communications biology · 2025Article
- Exploration and analytical techniques for membrane curvature-sensing proteins in bacteria.Journal of bacteriology · 2025Review
- Charge distribution and helicity tune the binding of septin's amphipathic helix domain to membranes.Biophysical journal · 2025Article
- Large Roles of Small Proteins.Annual review of microbiology · 2024Review
- Identification of membrane curvature sensing motifs essential for VPS37A phagophore recruitment and autophagosome closure.Communications biology · 2024Article
- Assembling the Bacillus subtilis Spore Coat Basement Layer on Spherical Supported Lipid Bilayers.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Multifaceted membrane interactions of human Atg3 promote LC3-phosphatidylethanolamine conjugation during autophagy.Nature communications · 2023Article
- Curvature sensing as an emergent property of multiscale assembly of septins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cell-specific cargo delivery using synthetic bacterial spores.Cell reports · 2023Article
- Bacterial developmental checkpoint that directly monitors cell surface morphogenesis.Developmental cell · 2022Article
- Bacterial Small Membrane Proteins: the Swiss Army Knife of Regulators at the Lipid Bilayer.Journal of bacteriology · 2022Review
- Small Proteins; Big Questions.Journal of bacteriology · 2022Article
- Article
- Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling.Molecular biology of the cell · 2021Article
- An N-terminal conserved region in human Atg3 couples membrane curvature sensitivity to conjugase activity during autophagy.Nature communications · 2021Article
- SR7 - a dual-function antisense RNA fromRNA biology · 2021Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
In bacteria, certain shape-sensing proteins localize to differently curved membranes. During sporulation in Bacillus subtilis, the only convex (positively curved) surface in the cell is the forespore, an approximately spherical internal organelle. Previously, we demonstrated that SpoVM localizes to the forespore by preferentially adsorbing onto slightly convex membranes. Here, we used NMR and molecular dynamics simulations of SpoVM and a localization mutant (SpoVM(P9A)) to reveal that SpoVM's atypical amphipathic α-helix inserts deeply into the membrane and interacts extensively with acyl chains to sense packing differences in differently curved membranes. Based on binding to spherical supported lipid bilayers and Monte Carlo simulations, we hypothesize that SpoVM's membrane insertion, along with potential cooperative interactions with other SpoVM molecules in the lipid bilayer, drives its preferential localization onto slightly convex membranes. Such a mechanism, which is distinct from that used by high curvature-sensing proteins, may be widely conserved for the localization of proteins onto the surface of cellular organelles.
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