Three-dimensional ultrastructure of the septin filament network in Saccharomyces cerevisiae
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Septins are conserved GTP-binding proteins involved in membrane compartmentalization and remodeling. In budding yeast, five mitotic septins localize at the bud neck, where the plasma membrane is enriched in phosphatidylinositol-4,5-bisphosphate (PtdIns4,5P(2)). We previously established the subunit organization within purified yeast septin complexes and how these hetero-octamers polymerize into filaments in solution and on PtdIns4,5P(2)-containing lipid monolayers. How septin ultrastructure in vitro relates to the septin-containing filaments observed at the neck in fixed cells by thin-section electron microscopy was unclear. A morphological description of these filaments in the crowded space of the cell is challenging, given their small cross section. To examine septin organization in situ, sections of dividing yeast cells were analyzed by electron tomography of freeze-substituted cells, as well as by cryo-electron tomography. We found networks of filaments both perpendicular and parallel to the mother-bud axis that resemble septin arrays on lipid monolayers, displaying a repeat pattern that mirrors the molecular dimensions of the corresponding septin preparations in vitro. Thus these in situ structures most likely represent septin filaments. In viable mutants lacking a single septin, in situ filaments are still present, although more disordered, consistent with other evidence that the in vivo function of septins requires filament formation.
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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 [57]
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 [57]
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Septins modulate the autophagy response after nutrient starvation
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- Authors
- Bertin, A., McMurray, M. A., Pierson, J., Thai, L., McDonald, K. L., Zehr, E. A., García, G., Peters, P., Thorner, J., & Nogales, E.
- Affiliations
- University of California, Berkeley (US)
- The Netherlands Cancer Institute (NL)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Nogales, Eva
- ORCID
- Venue
- Molecular Biology of the Cell
- Published
- 2012-02
- Volume
- 23
- Issue
- 3
- Pages
- 423-432
- ISSN
- 1059-1524 (ISSN-L)
- 1939-4586
- PMC
- PMC3268722
- OpenAlex
- W2013196716
- Cited by
- 106
- References
- 64
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 5 · 2023: 5 · 2022: 5 · 2021: 10 · 2020: 8 · 2019: 3 · 2018: 8 · 2017: 4 · 2016: 14 · 2015: 12 · 2014: 9 · 2013: 7 · 2012: 6
- FWCI
- 2.85
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- Molecular Biology of the Cell (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of General Medical Sciences (R00GM086603, K99 GM86603, R01GM21841, R01GM101314, K99GM086603, R01GM021841)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- 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
- Keywords
- septins, Saccharomyces cerevisiae, bud neck, membrane compartmentalization, electron tomography, cryo-electron tomography, thin section electron microscopy, filament polymerization
- MeSH terms
- Cytoskeleton, Mutation, Saccharomyces cerevisiae, Imaging, Three-Dimensional, Saccharomyces cerevisiae Proteins, Septins
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