ArticleThe Journal of biological chemistry2015
A Förster Resonance Energy Transfer (FRET)-based System Provides Insight into the Ordered Assembly of Yeast Septin Hetero-octamers.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 43 citations in OpenAlex.
- Septins associate with AP-3 to support trafficking to the vacuole/lysosome in yeast.Molecular biology of the cell · 2026Article
- Septins associate with AP-3 to support trafficking to the vacuole/lysosome in yeast.bioRxiv : the preprint server for biology · 2026Article
- Bni5 regulates and coordinates septin architecture and myosin-II functions at the cell division site.The Journal of cell biology · 2025Article
- Central Role of the Actomyosin Ring in Coordinating Cytokinesis Steps in Budding Yeast.Journal of fungi (Basel, Switzerland) · 2024Review
- Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024Review
- Revised subunit order of mammalian septin complexes explains their in vitro polymerization properties.Molecular biology of the cell · 2021Article
- Reconstructed evolutionary history of the yeast septins Cdc11 and Shs1.G3 (Bethesda, Md.) · 2021Article
- Septin Assembly and Remodeling at the Cell Division Site During the Cell Cycle.Frontiers in cell and developmental biology · 2021Review
- Production and analysis of a mammalian septin hetero-octamer complex.Cytoskeleton (Hoboken, N.J.) · 2020Article
- The hierarchical assembly of septins revealed by high-speed AFM.Nature communications · 2020Article
- Septin-associated proteins Aim44 and Nis1 traffic between the bud neck and the nucleus in the yeast Saccharomyces cerevisiae.Cytoskeleton (Hoboken, N.J.) · 2019Article
- Quantifying site-specific chromatin mechanics and DNA damage response.Scientific reports · 2018Article
- Control of septin filament flexibility and bundling by subunit composition and nucleotide interactions.Molecular biology of the cell · 2018Article
- Article
- Analysis of Septin Reorganization at Cytokinesis Using Polarized Fluorescence Microscopy.Frontiers in cell and developmental biology · 2017Article
- Effects of Bni5 Binding on Septin Filament Organization.Journal of molecular biology · 2016Article
- Detection of protein-protein interactions at the septin collar in Saccharomyces cerevisiae using a tripartite split-GFP system.Molecular biology of the cell · 2016Article
- Coordinate action of distinct sequence elements localizes checkpoint kinase Hsl1 to the septin collar at the bud neck in Saccharomyces cerevisiae.Molecular biology of the cell · 2016Article
- Actomyosin ring driven cytokinesis in budding yeast.Seminars in cell & developmental biology · 2016Review
- Micron-scale plasma membrane curvature is recognized by the septin cytoskeleton.The Journal of cell biology · 2016Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Prior studies in both budding yeast (Saccharomyces cerevisiae) and in human cells have established that septin protomers assemble into linear hetero-octameric rods with 2-fold rotational symmetry. In mitotically growing yeast cells, five septin subunits are expressed (Cdc3, Cdc10, Cdc11, Cdc12, and Shs1) and assemble into two types of rods that differ only in their terminal subunit: Cdc11-Cdc12-Cdc3-Cdc10-Cdc10-Cdc3-Cdc12-Cdc11 and Shs1-Cdc12-Cdc3-Cdc10-Cdc10-Cdc3-Cdc12-Shs1. EM analysis has shown that, under low salt conditions, the Cdc11-capped rods polymerize end to end to form long paired filaments, whereas Shs1-capped rods form arcs, spirals, and rings. To develop a facile method to study septin polymerization in vitro, we exploited our previous work in which we generated septin complexes in which all endogenous cysteine (Cys) residues were eliminated by site-directed mutagenesis, except an introduced E294C mutation in Cdc11 in these experiments. Mixing samples of a preparation of such single-Cys containing Cdc11-capped rods that have been separately derivatized with organic dyes that serve as donor and acceptor, respectively, for FRET provided a spectroscopic method to monitor filament assembly mediated by Cdc11-Cdc11 interaction and to measure its affinity under specified conditions. Modifications of this same FRET scheme also allow us to assess whether Shs1-capped rods are capable of end to end association either with themselves or with Cdc11-capped rods. This FRET approach also was used to follow the binding to septin filaments of a septin-interacting protein, the type II myosin-binding protein Bni5.
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