ArticleEukaryotic cell2012
Roles of Hsl1p and Hsl7p in Swe1p degradation: beyond septin tethering.
Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Article
- Integrating Rio1 activities discloses its nutrient-activated network in Saccharomyces cerevisiae.Nucleic acids research · 2018Article
- 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
- Sensing a bud in the yeast morphogenesis checkpoint: a role for Elm1.Molecular biology of the cell · 2016Article
- Septin-Associated Protein Kinases in the YeastFrontiers in cell and developmental biology · 2016Review
- Molecular mechanism of flocculation self-recognition in yeast and its role in mating and survival.mBio · 2015Article
- Septins and Generation of Asymmetries in Fungal Cells.Annual review of microbiology · 2015Review
- Fungal pathogens are platforms for discovering novel and conserved septin properties.Current opinion in microbiology · 2014Review
- Feedback control of Swe1p degradation in the yeast morphogenesis checkpoint.Molecular biology of the cell · 2013Article
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Authors and funding
3 authors.
Funding
Abstract
The morphogenesis checkpoint in Saccharomyces cerevisiae couples bud formation to the cell division cycle by delaying nuclear division until cells have successfully constructed a bud. The cell cycle delay is due to the mitosis-inhibitory kinase Swe1p, which phosphorylates the cyclin-dependent kinase Cdc28p. In unperturbed cells, Swe1p is degraded via a mechanism thought to involve its tethering to a cortical scaffold of septin proteins at the mother-bud neck. In cells that experience stresses that delay bud formation, Swe1p is stabilized, accumulates, and promotes a G(2) delay. The tethering of Swe1p to the neck requires two regulators, called Hsl1p and Hsl7p. Hsl1p interacts with septins, and Hsl7p interacts with Swe1p; tethering occurs when Hsl1p interacts with Hsl7p. Here we created a version of Swe1p that is artificially tethered to the neck by fusion to a septin so that Swe1p no longer requires Hsl1p or Hsl7p for its localization to the neck. We show that the interaction between Hsl1p and Hsl7p, required for normal Swe1p degradation, is no longer needed for septin-Swe1p degradation, supporting the idea that the Hsl1p-Hsl7p interaction serves mainly to tether Swe1p to the neck. However, both Hsl1p and Hsl7p are still required for Swe1p degradation, implying that these proteins play additional roles beyond localizing Swe1p to the neck.
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