ArticleMolecular and cellular biology1996
Protein phosphatase type 1 interacts with proteins required for meiosis and other cellular processes in Saccharomyces cerevisiae.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 96 citations in OpenAlex.
- Protein phosphatases of Saccharomyces cerevisiae.Current genetics · 2019Review
- Article
- 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
- Metabolic differentiation of surface and invasive cells of yeast colony biofilms revealed by gene expression profiling.BMC genomics · 2017Article
- Glucose-induced posttranslational activation of protein phosphatases PP2A and PP1 in yeast.Cell research · 2012Article
- Article
- Dephosphorylation of gamma H2A by Glc7/protein phosphatase 1 promotes recovery from inhibition of DNA replication.Molecular and cellular biology · 2010Article
- Protein phosphatase type 1-interacting protein Ysw1 is involved in proper septin organization and prospore membrane formation during sporulation.Eukaryotic cell · 2009Article
- Lessons from fungal F-box proteins.Eukaryotic cell · 2009Review
- Protein phosphatase-1 inhibitor-3 is an in vivo target of caspase-3 and participates in the apoptotic response.The Journal of biological chemistry · 2008Article
- Scd5p mediates phosphoregulation of actin and endocytosis by the type 1 phosphatase Glc7p in yeast.Molecular biology of the cell · 2007Article
- Alternative modes of organellar segregation during sporulation in Saccharomyces cerevisiae.Eukaryotic cell · 2007Article
- Nucleocytoplasmic trafficking is required for functioning of the adaptor protein Sla1p in endocytosis.Traffic (Copenhagen, Denmark) · 2007Article
- Glc7/protein phosphatase 1 regulatory subunits can oppose the Ipl1/aurora protein kinase by redistributing Glc7.Molecular and cellular biology · 2006Article
- Glucose signaling in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2006Review
- Histone H3 Ser10 phosphorylation-independent function of Snf1 and Reg1 proteins rescues a gcn5- mutant in HIS3 expression.Molecular and cellular biology · 2005Article
- Ascospore formation in the yeast Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2005Review
- Review
- Ady4p and Spo74p are components of the meiotic spindle pole body that promote growth of the prospore membrane in Saccharomyces cerevisiae.Eukaryotic cell · 2003Article
- The Ark1/Prk1 family of protein kinases. Regulators of endocytosis and the actin skeleton.EMBO reports · 2003Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein phosphatase type I (PP1) is involved in diverse cellular processes, and its activity toward specific substrates is thought to be controlled by different regulatory or targeting subunits. To identify regulatory subunits and substrates of the Saccharomyces cerevisiae PP1, encoded by GLC7, we used the two-hybrid system to detect interacting proteins. Among the many proteins identified were Gac1, a known glycogen regulatory subunit, and a protein with homology to Gac1. We also characterized a new gene designated GIP1, for Glc7-interacting protein. We show that a Gip1 fusion protein coimmunoprecipitates with PP1 from cell extracts. Molecular and genetic analyses indicate that GIP1 is expressed specifically during meiosis, affects transcription of late meiotic genes, and is essential for sporulation. Thus, the Gip1 protein is a candidate for a meiosis-specific substrate or regulator of PP1. Finally, we recovered two genes, RED1 and SCD5, with roles in meiosis and the vesicular secretory pathway, respectively. These results provide strong evidence implicating PP1 function in meiosis. In addition, this study indicates that the two-hybrid system offers a promising approach to understanding the multiple roles and interactions of PP1 in cellular regulation.
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