ArticleThe Biochemical journal1995
Characterization of a regulated form of phospholipase D in the yeast Saccharomyces cerevisiae.
Article in The Biochemical journal, 1995. 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, 50 citations in OpenAlex.
- 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
- Phosphohydrolase and transphosphatidylation reactions of two Streptomyces phospholipase D enzymes: covalent versus noncovalent catalysis.Protein science : a publication of the Protein Society · 2003Article
- Cloning, overexpression, and characterization of a bacterial Ca2+-dependent phospholipase D.Protein science : a publication of the Protein Society · 2002Article
- Propranolol inhibits hyphal development in Candida albicans.Antimicrobial agents and chemotherapy · 2002Article
- Phospholipase D: molecular and cell biology of a novel gene family.The Biochemical journal · 2000Review
- Activation of phospholipase D by growth factors and oncogenes in murine fibroblasts follow alternative but cross-talking pathways.The Biochemical journal · 1997Article
- Characterization of Saccharomyces cerevisiae deficient in expression of phospholipase D.The Biochemical journal · 1996Article
- Phospholipase D signaling is essential for meiosis.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Phospholipase D (PLD), which is present in bacterial, plant and animal cells, can serve as an important element of signal-transduction pathways. This study examined the potential role of this enzyme in the regulation of Saccharomyces cerevisiae. An assay in vitro using a fluorescent 1-acyl-2-alkyl glycerophosphocholine as substrate was used to assess PLD activity in yeast cell extracts. A neutral PLD activity is present in membranes prepared from both haploid and diploid yeast cells, as evidenced by the production of phosphatidic acid and phosphatidylbutanol in the presence of butanol. Alcohols, in addition to serving as substrates for transphosphatidylation, stimulate PLD activity. Increased PLD activity is detected in membranes when either haploid or diploid cells are incubated in the presence of a non-fermentable carbon source. Membrane PLD activity increases within 10 min after diploid cells are placed in a sporulation-inducing medium lacking nitrogen and containing a non-fermentable carbon source. The increased activity persists for 2-3 h, and then declines to control values. This response occurs in the presence of cycloheximide, an inhibitor of protein synthesis. These data indicate that PLD activity is present in yeast, and that activation of PLD is an early event in sporulation in this organism.
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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 OpenQuestion graph.