ArticleThe Journal of cell biology1998
Relocalization of phospholipase D activity mediates membrane formation during meiosis.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed, 137 citations in OpenAlex.
- Abscisic Acid, Microtubules and Phospholipase D-Solving a Cellular Bermuda Triangle.International journal of molecular sciences · 2024Article
- Membrane and organelle rearrangement during ascospore formation in budding yeast.Microbiology and molecular biology reviews : MMBR · 2024Review
- Recruitment of the lipid kinase Mss4 to the meiotic spindle pole promotes prospore membrane formation inMolecular biology of the cell · 2023Article
- Tubular ER Associates With Diacylglycerol-Rich Structures During Lipid Droplet Consumption.Frontiers in cell and developmental biology · 2020Article
- Regulation of Membrane Turnover by Phosphatidic Acid: Cellular Functions and Disease Implications.Frontiers in cell and developmental biology · 2019Review
- Gene Expression Pattern and Protein Localization of Arabidopsis Phospholipase D Alpha 1 Revealed by Advanced Light-Sheet and Super-Resolution Microscopy.Frontiers in plant science · 2018Article
- Lipid droplets are central organelles for meiosis II progression during yeast sporulation.Molecular biology of the cell · 2017Article
- SPO73 and SPO71 Function Cooperatively in Prospore Membrane Elongation During Sporulation in Saccharomyces cerevisiae.PloS one · 2015Article
- Positive feedback of NDT80 expression ensures irreversible meiotic commitment in budding yeast.PLoS genetics · 2014Article
- A visual screen of protein localization during sporulation identifies new components of prospore membrane-associated complexes in budding yeast.Eukaryotic cell · 2014Article
- A phosphatidylinositol transfer protein integrates phosphoinositide signaling with lipid droplet metabolism to regulate a developmental program of nutrient stress-induced membrane biogenesis.Molecular biology of the cell · 2014Article
- A neurotoxic glycerophosphocholine impacts PtdIns-4, 5-bisphosphate and TORC2 signaling by altering ceramide biosynthesis in yeast.PLoS genetics · 2014Article
- VPS13 regulates membrane morphogenesis during sporulation in Saccharomyces cerevisiae.Journal of cell science · 2012Article
- The conserved foot domain of RNA pol II associates with proteins involved in transcriptional initiation and/or early elongation.Genetics · 2011Article
- Sporulation in the budding yeast Saccharomyces cerevisiae.Genetics · 2011Review
- Phospholipase D: enzymology, functionality, and chemical modulation.Chemical reviews · 2011Review
- Srf1 is a novel regulator of phospholipase D activity and is essential to buffer the toxic effects of C16:0 platelet activating factor.PLoS genetics · 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
- Phospholipase D in the Golgi apparatus.Biochimica et biophysica acta · 2009Review
- Phosphatidylinositol-4,5-bisphosphate and phospholipase D-generated phosphatidic acid specify SNARE-mediated vesicle fusion for prospore membrane formation.Eukaryotic cell · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Phospholipase D (PLD) enzymes catalyze the hydrolysis of phosphatidylcholine and are involved in membrane trafficking and cytoskeletal reorganization. The Saccharomyces cerevisiae SPO14 gene encodes a PLD that is essential for meiosis. We have analyzed the role of PLD in meiosis by examining two mutant proteins, one with a point mutation in a conserved residue (Spo14pK--> H) and one with an amino-terminal deletion (Spo14pDeltaN), neither of which can restore meiosis in a spo14 deletion strain. Spo14pK--> H is enzymatically inactive, indicating that PLD activity is required, whereas Spo14pDeltaN retains PLD catalytic activity in vitro, indicating that PLD activity is not sufficient for meiosis. To explore other aspects of Spo14 function, we followed the localization of the enzyme during meiosis. Spo14p is initially distributed throughout the cell, becomes concentrated at the spindle pole bodies after the meiosis I division, and at meiosis II localizes to the new spore membrane as it surrounds the nuclei and then expands to encapsulate the associated cytoplasm during the formation of spores. The catalytically inactive protein also undergoes relocalization during meiosis; however, in the absence of PLD activity, no membrane is formed. In contrast, Spo14pDeltaN does not relocalize properly, indicating that the failure of this protein to complement a spo14 mutant is due to its inability to localize its PLD activity. Furthermore, we find that Spo14p movement is correlated with phosphorylation of the protein. These experiments indicate that PLD participates in regulated membrane formation during meiosis, and that both its catalytic activity and subcellular redistribution are essential for this function.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.