ArticleJournal of cell science2023
A human septin octamer complex sensitive to membrane curvature drives membrane deformation with a specific mesh-like organization.
Article in Journal of cell science, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Bottom-up reconstitution of model membrane systems: a mini-review.Biochemical Society transactions · 2026Review
- Local RhoA activation induces anillin-independent septin recruitment in interphase cells.Molecular biology of the cell · 2026Article
- Study of Protein-Protein Interactions in Septin Assembly: Multiple amphipathic helix domains cooperate in binding to the lipid membrane.PLoS computational biology · 2026Article
- Septin-mediated coupling of protein import and division during chloroplast evolution.bioRxiv : the preprint server for biology · 2026Article
- Mechanically-induced Septin Networks Protect Nuclear Integrity.bioRxiv : the preprint server for biology · 2026Article
- Reduction of bacterial colonization on buckling-induced wrinkled surfaces under fluid shear.Nature communications · 2026Article
- Local RhoA activation induces septin recruitment.bioRxiv : the preprint server for biology · 2025Article
- A single septin from a polyextremotolerant yeast recapitulates many canonical functions of septin hetero-oligomers.Molecular biology of the cell · 2024Article
- Principles and regulation of mechanosensing.Journal of cell science · 2024Review
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Septins are cytoskeletal proteins interacting with the inner plasma membrane and other cytoskeletal partners. Being key in membrane remodeling processes, they often localize at specific micrometric curvatures. To analyze the behavior of human septins at the membrane and decouple their role from other partners, we used a combination of bottom-up in vitro methods. We assayed their ultrastructural organization, their curvature sensitivity, as well as their role in membrane reshaping. On membranes, human septins organize into a two-layered mesh of orthogonal filaments, instead of generating parallel sheets of filaments observed for budding yeast septins. This peculiar mesh organization is sensitive to micrometric curvature and drives membrane reshaping as well. The observed membrane deformations together with the filamentous organization are recapitulated in a coarse-grained computed simulation to understand their mechanisms. Our results highlight the specific organization and behavior of animal septins at the membrane as opposed to those of fungal proteins.
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Registered trials
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 OpenQuestion graph.