ArticleMolecular biology of the cell2002
Cell cycle-dependent assembly of a Gin4-septin complex.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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Who cites it
89 citing papers in PubMed, 151 citations in OpenAlex.
- Article
- A cyclin-polarity feedback network ensures healthy cell proliferation.Nature communications · 2026Article
- Bni5 regulates and coordinates septin architecture and myosin-II functions at the cell division site.The Journal of cell biology · 2025Article
- Mechanisms of growth-dependent regulation of the Gin4 kinase.Molecular biology of the cell · 2025Article
- Mechanisms of growth-dependent regulation of the Gin4 kinase.bioRxiv : the preprint server for biology · 2024Article
- Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024Review
- Cell growth and nutrient availability control the mitotic exit signaling network in budding yeast.The Journal of cell biology · 2024Article
- Reciprocal regulation by Elm1 and Gin4 controls septin hourglass assembly and remodeling.The Journal of cell biology · 2024Article
- The Roles of Septins in Regulating Fission Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024Review
- Insights of roles played by septins in pathogenic fungi.Virulence · 2021Review
- Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling.Molecular biology of the cell · 2021Article
- Lipid flippases in polarized growth.Current genetics · 2021Review
- Septin Assembly and Remodeling at the Cell Division Site During the Cell Cycle.Frontiers in cell and developmental biology · 2021Review
- TheInternational journal of molecular sciences · 2020Article
- Growth-Dependent Activation of Protein Kinases Suggests a Mechanism for Measuring Cell Growth.Genetics · 2020Article
- Effect of Nicotinamide AgainstFrontiers in microbiology · 2019Article
- Architecture, remodeling, and functions of the septin cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2019Review
- Prolonged cyclin-dependent kinase inhibition results in septin perturbations during return to growth and mitosis.The Journal of cell biology · 2018Article
- Phosphorylation of Pnut in the Early Stages ofG3 (Bethesda, Md.) · 2018Article
- The septin-associated kinase Gin4 recruits Gps1 to the site of cell division.Molecular biology of the cell · 2017Article
29 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gin4, a Nim1-related kinase, is required in budding yeast for localization of the septins and for proper control of daughter cell growth during G2/M. Gin4 becomes hyperphosphorylated when cells enter mitosis, leading to activation of Gin4 kinase activity. In this study, we have used immunoaffinity chromatography to identify proteins that associate with Gin4 during mitosis, with the goal of finding targets of Gin4 kinase activity and proteins that play a role in Gin4 activation. We show that during mitosis Gin4 is assembled into a multiprotein complex that includes Nap1, Bni5, the septins, and at least two molecules of Gin4. The associated Gin4 molecules present in this complex phosphorylate each other, leading to Gin4 hyperphosphorylation. Furthermore, the Shs1 septin present in the complex undergoes Gin4-dependent phosphorylation during mitosis and appears to be a substrate of Gin4 in vitro, suggesting that it is a target of Gin4 kinase activity in vivo. Genetic data support the idea that Shs1 is an important target of Gin4 kinase activity. Association of Gin4 with the septins during mitosis requires Shs1, Nap1, Cla4, Elm1, and the kinase activities of Gin4 and Cdc28. Self-association of Gin4 molecules requires Shs1 but not Cla4 or Nap1. Previous work has suggested that the septins function together as a tight complex, and we found that the majority of the Shs1 in the cell is tightly bound to the other septins Cdc3, Cdc10, Cdc11, and Cdc12. Interestingly, however, Shs1 can bind to Gin4 and induce Gin4 oligomerization under conditions in which the Cdc11 septin does not bind to Gin4, suggesting that Shs1 can function independently of the other septins. Taken together, these findings suggest that highly regulated protein-binding events ensure that the Gin4 kinase is activated only during mitosis and only in association with Shs1, a likely in vivo substrate of Gin4. In addition, these results provide clues to how Gin4 may regulate the localization or function of the septins.
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