ArticleJournal of molecular biology2010
Phosphatidylinositol-4,5-bisphosphate promotes budding yeast septin filament assembly and organization.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.
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Who cites it
137 citing papers in PubMed, 272 citations in OpenAlex.
- Septin-mediated coupling of protein import and division during chloroplast evolution.bioRxiv : the preprint server for biology · 2026Article
- Coiled-coil homo-oligomerization and disaggregase Hsp104 act in parallel to stabilize orphan septins.bioRxiv : the preprint server for biology · 2026Article
- Local PI(4,5)PNature communications · 2026Article
- Mechanically-induced Septin Networks Protect Nuclear Integrity.bioRxiv : the preprint server for biology · 2026Article
- Lipid packing and local geometry influence septin curvature sensing.The Journal of cell biology · 2026Article
- Article
- Regulation of phosphatidylinositol-(4,5)-bisphosphate and active-Rho1p levels and distribution is crucial for correct spatio-temporal cytokinesis and echinocandin responses inAntimicrobial agents and chemotherapy · 2025Article
- Beyond division and morphogenesis: Considering the emerging roles of septins in plasma membrane homeostasis and cell wall integrity in human fungal pathogens.PLoS pathogens · 2025Article
- Septin higher-order structure on yeast membranes in vitro.Nature communications · 2025Article
- Central Role of the Actomyosin Ring in Coordinating Cytokinesis Steps in Budding Yeast.Journal of fungi (Basel, Switzerland) · 2024Review
- Article
- Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024Review
- Sur7 mediates a novel pathway for PIMolecular biology of the cell · 2024Article
- Phosphorylation of the F-BAR protein Hof1 drives septin ring splitting in budding yeast.Nature communications · 2024Article
- The Evolutionary Origins and Ancestral Features of Septins.bioRxiv : the preprint server for biology · 2024Article
- The MoLfa1 Protein Regulates Fungal Development and Septin Ring Formation inInternational journal of molecular sciences · 2024Article
- The Roles of Septins in Regulating Fission Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024Review
- The structure of a tetrameric septin complex reveals a hydrophobic element essential for NC-interface integrity.Communications biology · 2024Article
- Septins modulate the autophagy response after nutrient starvation.Molecular biology of the cell · 2024Article
- The evolutionary origins and ancestral features of septins.Frontiers in cell and developmental biology · 2024Article
77 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Septins are a conserved family of GTP-binding proteins that assemble into symmetric linear heterooligomeric complexes, which in turn are able to polymerize into apolar filaments and higher-order structures. In budding yeast (Saccharomyces cerevisiae) and other eukaryotes, proper septin organization is essential for processes that involve membrane remodeling, such as the execution of cytokinesis. In yeast, four septin subunits form a Cdc11-Cdc12-Cdc3-Cdc10-Cdc10-Cdc3-Cdc12-Cdc11 heterooctameric rod that polymerizes into filaments thought to form a collar around the bud neck in close contact with the inner surface of the plasma membrane. To explore septin-membrane interactions, we examined the effect of lipid monolayers on septin organization at the ultrastructural level using electron microscopy. Using this methodology, we have acquired new insights into the potential effect of septin-membrane interactions on filament assembly and, more specifically, on the role of phosphoinositides. Our studies demonstrate that budding yeast septins interact specifically with phosphatidylinositol-4,5-bisphosphate (PIP2) and indicate that the N terminus of Cdc10 makes a major contribution to the interaction of septin filaments with PIP2. Furthermore, we found that the presence of PIP2 promotes filament polymerization and organization on monolayers, even under conditions that prevent filament formation in solution or for mutants that prevent filament formation in solution. In the extreme case of septin complexes lacking the normally terminal subunit Cdc11 or the normally central Cdc10 doublet, the combination of the PIP2-containing monolayer and nucleotide permitted filament formation in vitro via atypical Cdc12-Cdc12 and Cdc3-Cdc3 interactions, respectively.
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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.