Septin filaments exhibit a dynamic, paired organization that is conserved from yeast to mammals
Open accessAbstract
The septins are conserved, GTP-binding proteins important for cytokinesis, membrane compartmentalization, and exocytosis. However, it is unknown how septins are arranged within higher-order structures in cells. To determine the organization of septins in live cells, we developed a polarized fluorescence microscopy system to monitor the orientation of GFP dipole moments with high spatial and temporal resolution. When GFP was fused to septins, the arrangement of GFP dipoles reflected the underlying septin organization. We demonstrated in a filamentous fungus, a budding yeast, and a mammalian epithelial cell line that septin proteins were organized in an identical highly ordered fashion. Fluorescence anisotropy measurements indicated that septin filaments organized into pairs within live cells, just as has been observed in vitro. Additional support for the formation of pairs came from the observation of paired filaments at the cortex of cells using electron microscopy. Furthermore, we found that highly ordered septin structures exchanged subunits and rapidly rearranged. We conclude that septins assemble into dynamic, paired filaments in vivo and that this organization is conserved from yeast to mammals.
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Septins form short filaments that self-assemble into parallel arrays which are non-polar in nature.
“Septins form short filaments that self-assemble into parallel arrays which are non-polar in nature [50, 57, 58].”
From Tumor Treating Fields Perturb the Localization of Septins and Cause Aberrant Mitotic Exit (2015) · cites this paper as [58]
There must be lateral interactions between Septin fibers that stabilize their lattice-like structure.
“Since the Septin heterotirmeric subunits align parallel to each other within the ordered Septin structures that form during mitosis [57–59], there must be lateral interactions between the fibers that stabilize their lattice like structure.”
From Tumor Treating Fields Perturb the Localization of Septins and Cause Aberrant Mitotic Exit (2015) · cites this paper as [58]
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Tumor Treating Fields Perturb the Localization of Septins and Cause Aberrant Mitotic Exit
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- Authors
- DeMay, B. S., Bai, X., Howard, L., Occhipinti, P., Meseroll, R. A., Spiliotis, E. T., Oldenbourg, R., & Gladfelter, A. S.
- Affiliations
- Dartmouth College (US)
- Drexel University (US)
- Marine Biological Laboratory (US)
- Corresponding author
- Gladfelter, Amy S.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2011-06-13
- Volume
- 193
- Issue
- 6
- Pages
- 1065-1081
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC3115802
- OpenAlex
- W2136627895
- Cited by
- 122
- References
- 43
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 10 · 2023: 4 · 2022: 10 · 2021: 9 · 2020: 13 · 2019: 9 · 2018: 3 · 2017: 7 · 2016: 14 · 2015: 7 · 2014: 6 · 2013: 9 · 2012: 6
- FWCI
- 4.60
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Open Access Server of the Woods Hole Scientific Community (Woods Hole Scientific Community) (submittedVersion, cc-by-nc-sa)
- Funders
- National Institute of Neurological Disorders and Stroke (R56NS048090, NS48090-06A, R01NS048090)
- National Institute of Biomedical Imaging and Bioengineering (R01EB002583, EB002583)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- septins, septin filaments, G proteins, fluorescence anisotropy, cytokinesis, membrane compartmentalization, exocytosis, cell cortex, yeast, evolutionary conservation
- MeSH terms
- Animals, Cell Line, Cytoskeleton, Humans, Microscopy, Fluorescence, Microscopy, Polarization, Recombinant Fusion Proteins, Yeasts, Green Fluorescent Proteins, Protein Multimerization, Septins
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