ArticleMolecular and cellular biology2010
Role of septins in the orientation of forespore membrane extension during sporulation in fission yeast.
Article in Molecular and cellular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
33 citing papers in PubMed, 55 citations in OpenAlex.
- Cellularization in chytrid fungi uses distinct mechanisms from conventional cytokinesis and cellularization in animals and yeast.Current biology : CB · 2026Article
- Localization and function of septins are susceptible to epitope tagging.Molecular biology of the cell · 2025Article
- Cellularization in chytrid fungi uses distinct mechanisms from conventional cytokinesis and cellularization in animals and yeast.bioRxiv : the preprint server for biology · 2025Article
- Article
- Localization and function of septins are susceptible to epitope tagging.bioRxiv : the preprint server for biology · 2025Article
- Localizations of the septin Spn4 tagged with GFP and mEGFP in fission yeast.microPublication biology · 2025Article
- Quantitative proteomics and phosphoproteomics profiling of meiotic divisions in the fission yeast Schizosaccharomyces pombe.Scientific reports · 2024Article
- Membrane and organelle rearrangement during ascospore formation in budding yeast.Microbiology and molecular biology reviews : MMBR · 2024Review
- The Evolutionary Origins and Ancestral Features of Septins.bioRxiv : the preprint server for biology · 2024Article
- The Roles of Septins in Regulating Fission Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024Review
- The evolutionary origins and ancestral features of septins.Frontiers in cell and developmental biology · 2024Article
- Evolutionary degeneration of septins into pseudoGTPases: impacts on a hetero-oligomeric assembly interface.Frontiers in cell and developmental biology · 2023Article
- Sporulation: A response to starvation in the fission yeast Schizosaccharomyces pombe.MicrobiologyOpen · 2022Review
- Article
- Tell the Difference Between Mitosis and Meiosis: Interplay Between Chromosomes, Cytoskeleton, and Cell Cycle Regulation.Frontiers in cell and developmental biology · 2021Review
- Masters of asymmetry - lessons and perspectives from 50 years of septins.Molecular biology of the cell · 2020Review
- Reversible solidification of fission yeast cytoplasm after prolonged nutrient starvation.Journal of cell science · 2019Article
- Glucose starvation triggers filamentous septin assemblies in anBiology open · 2019Article
- The Unsolved Problem of How Cells Sense Micron-Scale Curvature.Trends in biochemical sciences · 2017Review
- Assembly, molecular organization, and membrane-binding properties of development-specific septins.The Journal of cell biology · 2016Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
Abstract
During yeast sporulation, a forespore membrane (FSM) initiates at each spindle-pole body and extends to form the spore envelope. We used Schizosaccharomyces pombe to investigate the role of septins during this process. During the prior conjugation of haploid cells, the four vegetatively expressed septins (Spn1, Spn2, Spn3, and Spn4) coassemble at the fusion site and are necessary for its normal morphogenesis. Sporulation involves a different set of four septins (Spn2, Spn5, Spn6, and the atypical Spn7) that does not include the core subunits of the vegetative septin complex. The four sporulation septins form a complex in vitro and colocalize interdependently to a ring-shaped structure along each FSM, and septin mutations result in disoriented FSM extension. The septins and the leading-edge proteins appear to function in parallel to orient FSM extension. Spn2 and Spn7 bind to phosphatidylinositol 4-phosphate [PtdIns(4)P] in vitro, and PtdIns(4)P is enriched in the FSMs, suggesting that septins bind to the FSMs via this lipid. Cells expressing a mutant Spn2 protein unable to bind PtdIns(4)P still form extended septin structures, but these structures fail to associate with the FSMs, which are frequently disoriented. Thus, septins appear to form a scaffold that helps to guide the oriented extension of the FSM.
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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.