ArticleJournal of cell science2013
Coupling of septins to the axial landmark by Bud4 in budding yeast.
Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024Review
- A dynamic network model predicts the phenotypes of multicellular clusters from cellular properties.Current biology : CB · 2024Article
- Cdc42 couples septin recruitment to the axial landmark assembly via Axl2 in budding yeast.Journal of cell science · 2024Article
- Quantitative analysis of septin Cdc10 & Cdc3-associated proteome during stress response in the fungal pathogen Cryptococcus neoformans.PloS one · 2024Article
- Multicellular growth as a dynamic network of cells.bioRxiv : the preprint server for biology · 2023Article
- Article
- Role of the anillin-like protein in growth of Cryptococcus neoformans at human host temperature.Fungal genetics and biology : FG & B · 2022Article
- Characterization of Bud3 domains sufficient for bud neck targeting inAccess microbiology · 2022Article
- 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
- Review
- Regulation of Cdc42 for polarized growth in budding yeast.Microbial cell (Graz, Austria) · 2020Review
- Anillin facilitates septin assembly to prevent pathological outfoldings of central nervous system myelin.eLife · 2019Article
- Architecture, remodeling, and functions of the septin cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2019Review
- The anillin-related Int1 protein and the Sep7 septin collaborate to maintain cellular ploidy in Candida albicans.Scientific reports · 2018Article
- Resistance to the Plant Defensin NaD1 Features Modifications to the Cell Wall and Osmo-Regulation Pathways of Yeast.Frontiers in microbiology · 2018Article
- Mechanics and regulation of cytokinesis in budding yeast.Seminars in cell & developmental biology · 2017Review
- Cell Biology of Hyphal Growth.Microbiology spectrum · 2017Review
- Analysis of Septin Reorganization at Cytokinesis Using Polarized Fluorescence Microscopy.Frontiers in cell and developmental biology · 2017Article
- Detection of protein-protein interactions at the septin collar in Saccharomyces cerevisiae using a tripartite split-GFP system.Molecular biology of the cell · 2016Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Cells of the budding yeast Saccharomyces cerevisiae select a site for polarized growth in a specific pattern that depends on their cell type. Haploid a and α cells bud in the axial budding pattern, which requires assembly of a landmark that includes the Bud4 protein. To understand how an axial bud site is established, we performed a structure-function analysis of Bud4. Bud4 contains DUF1709 (domain of unknown function), which is similar to a part of the anillin-homology domain, and a putative Pleckstrin homology (PH) domain near to its C terminus. Although its localization depends on septins, a conserved family of GTP-binding proteins, Bud4 is necessary for the stable inheritance of septin rings during cell division. Although some anillins interact directly with septins, we find that neither DUF1709 nor the PH domain is necessary for targeting Bud4 to the mother-bud neck. Instead, this C-terminal region is crucial for association of Bud4 with Bud3 and other components of the axial landmark. Remarkably, septins colocalize with Bud4 mutant proteins that lack these C-terminal domains, forming an arc or a single ring instead of a double ring during and after cytokinesis. Interestingly, overexpression of Bud4 also induces formation of extra Bud4 rings and arcs that are associated with septins. Analyses of a series of bud4 truncation mutants suggest that at least two domains in the central region play a redundant role in targeting Bud4 to the mother-bud neck and are thus likely to interact with septins. Taken together, these results indicate that Bud4 functions as a platform that links septins to the axial landmark.
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