ArticleCurrent biology : CB2017
Hof1 and Chs4 Interact via F-BAR Domain and Sel1-like Repeats to Control Extracellular Matrix Deposition during Cytokinesis.
Article in Current biology : CB, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed.
- Apical spectrin organizes cortical actin filament bundles to pattern C. elegans cuticle ridges.PLoS genetics · 2026Article
- Apical spectrin organizes cortical actin filament bundles to patternbioRxiv : the preprint server for biology · 2026Article
- 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
- The matrisome landscape controlling in vivo germ cell fates.Nature communications · 2024Article
- Transient septin sumoylation steers a Fir1-Skt5 protein complex between the split septin ring.The Journal of cell biology · 2024Article
- Live-cell imaging of septins and cell polarity proteins in the growing dikaryotic vegetative hypha of the model mushroom Coprinopsis cinerea.Scientific reports · 2023Article
- Identification of chitin synthase activator in Aspergillus niger and its application in citric acid fermentation.Applied microbiology and biotechnology · 2022Article
- Chitin Synthesis in Yeast: A Matter of Trafficking.International journal of molecular sciences · 2022Review
- Fission yeast paxillin contains two Cdc15 binding motifs for robust recruitment to the cytokinetic ring.Molecular biology of the cell · 2022Article
- The Role of the Cell Integrity Pathway in Septum Assembly in Yeast.Journal of fungi (Basel, Switzerland) · 2021Review
- The state of F-BAR domains as membrane-bound oligomeric platforms.Trends in cell biology · 2021Review
- Essential role of the endocytic site-associated protein Ecm25 in stress-induced cell elongation.Cell reports · 2021Article
- Article
- Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membrane Platform That Coordinates Cytoskeletal and Signaling Components for Cytokinesis.Cell reports · 2020Article
- A septin-Hof1 scaffold at the yeast bud neck binds and organizes actin cables.Molecular biology of the cell · 2020Article
- Implications of maintenance of mother-bud neck size in diverse vital processes of Saccharomyces cerevisiae.Current genetics · 2019Article
- A cell separation checkpoint that enforces the proper order of late cytokinetic events.The Journal of cell biology · 2019Article
- Molecular mechanisms of contractile-ring constriction and membrane trafficking in cytokinesis.Biophysical reviews · 2018Review
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8 authors.
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Abstract
Localized extracellular matrix (ECM) remodeling is thought to stabilize the cleavage furrow and maintain cell shape during cytokinesis [1-14]. This remodeling is spatiotemporally coordinated with a cytoskeletal structure pertaining to a kingdom of life, for example the FtsZ ring in bacteria [15], the phragmoplast in plants [16], and the actomyosin ring in fungi and animals [17, 18]. Although the cytoskeletal structures have been analyzed extensively, the mechanisms of ECM remodeling remain poorly understood. In the budding yeast Saccharomyces cerevisiae, ECM remodeling refers to sequential formations of the primary and secondary septa that are catalyzed by chitin synthase-II (Chs2) and chitin synthase-III (the catalytic subunit Chs3 and its activator Chs4), respectively [18, 19]. Surprisingly, both Chs2 and Chs3 are delivered to the division site at the onset of cytokinesis [6, 20]. What keeps Chs3 inactive until secondary septum formation remains unknown. Here, we show that Hof1 binds to the Sel1-like repeats (SLRs) of Chs4 via its F-BAR domain and inhibits Chs3-mediated chitin synthesis during cytokinesis. In addition, Hof1 is required for rapid accumulation as well as efficient removal of Chs4 at the division site. This study uncovers a mechanism by which Hof1 controls timely activation of Chs3 during cytokinesis and defines a novel interaction and function for the conserved F-BAR domain and SLR that are otherwise known for their abilities to bind membrane lipids [21, 22] and scaffold protein complex formation [23].
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