ArticleEukaryotic cell2009
Protein phosphatase type 1-interacting protein Ysw1 is involved in proper septin organization and prospore membrane formation during sporulation.
Article in Eukaryotic cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Membrane and organelle rearrangement during ascospore formation in budding yeast.Microbiology and molecular biology reviews : MMBR · 2024Review
- Suppression of Vps13 adaptor protein mutants reveals a central role for PI4P in regulating prospore membrane extension.PLoS genetics · 2021Article
- Dynamic localization of a yeast development-specific PP1 complex during prospore membrane formation is dependent on multiple localization signals and complex formation.Molecular biology of the cell · 2017Article
- Effects of Rho1, a small GTPase on the production of recombinant glycoproteins in Saccharomyces cerevisiae.Microbial cell factories · 2016Article
- A visual screen of protein localization during sporulation identifies new components of prospore membrane-associated complexes in budding yeast.Eukaryotic cell · 2014Article
- VPS13 regulates membrane morphogenesis during sporulation in Saccharomyces cerevisiae.Journal of cell science · 2012Article
- Sporulation in the budding yeast Saccharomyces cerevisiae.Genetics · 2011Review
- Septins: molecular partitioning and the generation of cellular asymmetry.Cell division · 2009Article
- Article
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Sporulation of Saccharomyces cerevisiae is a developmental process in which four haploid spores are generated inside a diploid cell. Gip1, a sporulation-specific targeting subunit of protein phosphatase type 1, together with its catalytic subunit, Glc7, colocalizes with septins along the extending prospore membrane and is required for septin organization and spore wall formation. However, the mechanism by which Gip1-Glc7 phosphatase promotes these events is unclear. We show here that Ysw1, a sporulation-specific coiled-coil protein, has a functional relationship to Gip1-Glc7 phosphatase. Overexpression of YSW1 partially suppresses the sporulation defect of a temperature-sensitive allele of gip1. Ysw1 interacts with Gip1 in a two-hybrid assay, and this interaction is required for suppression. Ysw1 tagged with green fluorescent protein colocalizes with septins and Gip1 along the extending prospore membrane during spore formation. Sporulation is partially defective in ysw1Delta mutant, and cytological analysis revealed that septin structures are perturbed and prospore membrane extension is aberrant in ysw1Delta cells. These results suggest that Ysw1 functions with the Gip1-Glc7 phosphatase to promote proper septin organization and prospore membrane formation.
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