ArticleMolecular and cellular biology2002
Bni5p, a septin-interacting protein, is required for normal septin function and cytokinesis in Saccharomyces cerevisiae.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 79 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
- Article
- Bni5 regulates and coordinates septin architecture and myosin-II functions at the cell division site.The Journal of cell biology · 2025Article
- Article
- 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
- Article
- Septin Assembly and Remodeling at the Cell Division Site During the Cell Cycle.Frontiers in cell and developmental biology · 2021Review
- Connecting cell polarity signals to the cytokinetic machinery in yeast and metazoan cells.Cell cycle (Georgetown, Tex.) · 2021Review
- The LKB1-like Kinase Elm1 Controls Septin Hourglass Assembly and Stability by Regulating Filament Pairing.Current biology : CB · 2020Article
- Cell size sets the diameter of the budding yeast contractile ring.Nature communications · 2020Article
- Comparative Analysis of the Roles of Non-muscle Myosin-IIs in Cytokinesis in Budding Yeast, Fission Yeast, and Mammalian Cells.Frontiers in cell and developmental biology · 2020Review
- Temporal regulation of morphogenetic events in Saccharomyces cerevisiae.Molecular biology of the cell · 2018Article
- Mechanics and regulation of cytokinesis in budding yeast.Seminars in cell & developmental biology · 2017Review
- 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
- The final cut: cell polarity meets cytokinesis at the bud neck in S. cerevisiae.Cellular and molecular life sciences : CMLS · 2016Review
- The Nim1 kinase Gin4 has distinct domains crucial for septin assembly, phospholipid binding and mitotic exit.Journal of cell science · 2016Article
- Novel Interactome of Saccharomyces cerevisiae Myosin Type II Identified by a Modified Integrated Membrane Yeast Two-Hybrid (iMYTH) Screen.G3 (Bethesda, Md.) · 2016Article
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
Abstract
In the budding yeast Saccharomyces cerevisiae, the Cdc3p, Cdc10p, Cdc11p, Cdc12p, and Sep7p/Shs1p septins assemble early in the cell cycle in a ring that marks the future cytokinetic site. The septins appear to be major structural components of a set of filaments at the mother-bud neck and function as a scaffold for recruiting proteins involved in cytokinesis and other processes. We isolated a novel gene, BNI5, as a dosage suppressor of the cdc12-6 growth defect. Overexpression of BNI5 also suppressed the growth defects of cdc10-1, cdc11-6, and sep7Delta strains. Loss of BNI5 resulted in a cytokinesis defect, as evidenced by the formation of connected cells with shared cytoplasms, and deletion of BNI5 in a cdc3-6, cdc10-1, cdc11-6, cdc12-6, or sep7Delta mutant strain resulted in enhanced defects in septin localization and cytokinesis. Bni5p localizes to the mother-bud neck in a septin-dependent manner shortly after bud emergence and disappears from the neck approximately 2 to 3 min before spindle disassembly. Two-hybrid, in vitro binding, and protein-localization studies suggest that Bni5p interacts with the N-terminal domain of Cdc11p, which also appears to be sufficient for the localization of Cdc11p, its interaction with other septins, and other critical aspects of its function. Our data suggest that the Bni5p-septin interaction is important for septin ring stability and function, which is in turn critical for normal cytokinesis.
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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.