ArticleEukaryotic cell2003
Ady4p and Spo74p are components of the meiotic spindle pole body that promote growth of the prospore membrane in Saccharomyces cerevisiae.
Article in Eukaryotic cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 51 citations in OpenAlex.
- Membrane and organelle rearrangement during ascospore formation in budding yeast.Microbiology and molecular biology reviews : MMBR · 2024Review
- Rewiring of the phosphoproteome executes two meiotic divisions in budding yeast.The EMBO journal · 2024Article
- Meiotic Cytokinesis inJournal of fungi (Basel, Switzerland) · 2024Review
- Recruitment of the lipid kinase Mss4 to the meiotic spindle pole promotes prospore membrane formation inMolecular biology of the cell · 2023Article
- The Spo13/Meikin pathway confines the onset of gamete differentiation to meiosis II in yeast.The EMBO journal · 2022Article
- Autophagy of an Amyloid-like Translational Repressor Regulates Meiotic Exit.Developmental cell · 2020Article
- Analysis of the protein composition of the spindle pole body during sporulation in Ashbya gossypii.PloS one · 2019Article
- 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
- Article
- Compromised RNA polymerase III complex assembly leads to local alterations of intergenic RNA polymerase II transcription in Saccharomyces cerevisiae.BMC biology · 2014Article
- Sporulation genes associated with sporulation efficiency in natural isolates of yeast.PloS one · 2013Article
- Acetate regulation of spore formation is under the control of the Ras/cyclic AMP/protein kinase A pathway and carbon dioxide in Saccharomyces cerevisiae.Eukaryotic cell · 2012Article
- Sporulation in the budding yeast Saccharomyces cerevisiae.Genetics · 2011Review
- The fission yeast pleckstrin homology domain protein Spo7 is essential for initiation of forespore membrane assembly and spore morphogenesis.Molecular biology of the cell · 2011Article
- Vesicle docking to the spindle pole body is necessary to recruit the exocyst during membrane formation in Saccharomyces cerevisiae.Molecular biology of the cell · 2010Article
- Membrane assembly modulates the stability of the meiotic spindle-pole body.Journal of cell science · 2010Article
- A guaninine nucleotide exchange factor is a component of the meiotic spindle pole body in Schizosaccharomyces pombe.Molecular biology of the cell · 2010Article
- Protein phosphatase type 1-interacting protein Ysw1 is involved in proper septin organization and prospore membrane formation during sporulation.Eukaryotic cell · 2009Article
- Cdc7-Dbf4 regulates NDT80 transcription as well as reductional segregation during budding yeast meiosis.Molecular biology of the cell · 2008Article
- Sorting signals within the Saccharomyces cerevisiae sporulation-specific dityrosine transporter, Dtr1p, C terminus promote Golgi-to-prospore membrane transport.Eukaryotic cell · 2008Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Spore formation in Saccharomyces cerevisiae occurs via the de novo synthesis of the prospore membrane during the second meiotic division. Prospore membrane formation is triggered by assembly of a membrane-organizing center, the meiotic outer plaque (MOP), on the cytoplasmic face of the spindle pole body (SPB) during meiosis. We report here the identification of two new components of the MOP, Ady4p and Spo74p. Ady4p and Spo74p interact with known proteins of the MOP and are localized to the outer plaque of the SPB during meiosis II. MOP assembly and prospore membrane formation are abolished in spo74Delta/spo74Delta cells and occur aberrantly in ady4Delta/ady4Delta cells. Spo74p and the MOP component Mpc70p are mutually dependent for recruitment to SPBs during meiosis. In contrast, both Ady4p and Spo74p are present at SPBs, albeit at reduced levels, in cells that lack the MOP component Mpc54p. Our findings suggest a model for the assembled MOP in which Mpc54p, Mpc70p, and Spo74p make up a core structural unit of the scaffold that initiates synthesis of the prospore membrane, and Ady4p is an auxiliary component that stabilizes the plaque.
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