Phospholipase D signaling is essential for meiosis.

Rose, Kristine L.; Rudge, Simon A.; Frohman, Michael A.; Morris, Andrew J.; Engebrecht, JoAnne

doi:10.1073/pnas.92.26.12151

Cited by 201 publications

(219 citation statements)

References 33 publications

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“…3), demonstrating that yeast contains at least two independent phospholipases D. With yeast PtdCho or POPC as the substrate, PLD activity was low in membrane fractions from the wild type cells incubated in the presence of EDTA and disappeared in membranes from pldl mutants. Cleavage of NBD-PtdCho by Pldlp is strongly stimulated by PIP2 (4 mol%), which is in accordance with previous reports [9,11]. Ca-PLD is not affected by PIP2 (Fig.…”

Section: Phospholipase D Activity In Pldl Mutantssupporting

confidence: 93%

“…Colocalization of both phospholipases D in the plasma membrane suggests that these enzymes may be involved in signal transduction pathways signalling external stimuli. However, for Pldlp/ Spol4p this appears unlikely [9], since cells lacking Spol4p undergo the first steps of meiosis [14]. Since wild type cells are insensitive to external stimuli after having decided for meiosis, it was suggested that Pldlp is activated rather by an, as yet unidentified, internal event.…”

Section: Discussionmentioning

confidence: 99%

“…The yeast PLD1 gene when expressed in a heterologous system, Ci5 cells, gives rise to a membrane associated enzyme, which has substrate specificity for phosphatidylcholine (PtdCho) and is stimulated by phosphatidylinositol-4,5-bisphosphate (PIP2). Activity is reduced in the presence of Mg 2+ and oleate, but is unaffected in the presence of the chelators EDTA and EGTA and is not significantly stimulated by Ca 2+ [9].…”

Section: Introductionmentioning

confidence: 89%

“…Recently, the PLD1 gene encoding a PLD was cloned and sequenced [9][10][11]. Pldlp, as derived from the sequence, has a predicted molecular weight of 195 kDa.…”

Section: Phospholipase D Activity In Pldl Mutantsmentioning

confidence: 99%

“…Recently a PLD that is induced during sporulation was identified in yeast [8][9][10][11]. This yeast PLD is able to perform transphosphatidylation and accepts primary alcohols with chain lengths ranging from one to seven carbon atoms.…”

Section: Introductionmentioning

confidence: 99%

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Identification of a novel, Ca²⁺‐dependent phospholipase D with preference for phosphatidylserine and phosphatidylethanolamine in Saccharomyces cerevisiae

1996

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A membrane-bound phospholipase D (PLD) fromSaccharomyces cerevisiae was solubilized from mitochondrial and plasma membranes and partially purified. The enzyme has an apparent molecular weight of approximately 60 kDa, is strictly Ca2+-dependent and preferentially hydrolyses phosphatidylserine and phosphatidylethanolamine. Enzyme activity is significantly increased in membranes from cells grown on a nonfermentable carbon source. The CaZ+-dependent PLD is distinct from PLD encoded by the SPO141PLDI gene. The 195 kDa SPO141PLDI gene product is specific for PtdCho, Ca 2+-independent and is activated by PIP2. Furthermore, Pldlp has transphosphatidylation activity in the presence of ethanol and thus resembles the prototypic PLD activity found in mammalian cells and plants. In contrast, the Ca2+-dependent PLD described here is not affected by PIP2 and does not catalyze transphosphatidylation. Thus, the Ca2+-dependent PLD characterized in this study appears to be a member of a novel family of phospholipases D.

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Section: Phospholipase D Activity In Pldl Mutantssupporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 89%

“…Recently, the PLD1 gene encoding a PLD was cloned and sequenced [9][10][11]. Pldlp, as derived from the sequence, has a predicted molecular weight of 195 kDa.…”

Section: Phospholipase D Activity In Pldl Mutantsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Identification of a novel, Ca²⁺‐dependent phospholipase D with preference for phosphatidylserine and phosphatidylethanolamine in Saccharomyces cerevisiae

1996

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Expression and regulation of phospholipase D isoforms in mammalian cell lines

Gibbs

Meier

2000

J. Cell. Phys.

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Phospholipase D (PLD) is activated in mammalian cells in response to diverse stimuli that include growth factors, activators of protein kinase C, and agonists binding to G-protein-coupled receptors. Two forms of mammalian PLD, PLD1 and PLD2, have been identified. Expression of mRNA and protein for PLD1 and PLD2 was analyzed in the following cell lines: A7r5 (rat vascular smooth muscle); EL4 (mouse thymoma); HL-60 (human myeloid leukemia); Jurkat (human leukemia); PC-3 (human prostate adenocarcinoma); PC-12K (rat phaeochromocytoma); and Rat-1 HIR (rat fibroblast). All, with the exception of EL4, express agonist-activated PLD activity. PLD1 is expressed in A7r5, HL-60, PC-3, and Rat-1, while PLD2 is expressed in A7r5, Jurkat, PC12K, PC-3, and Rat-1. Neither isoform is expressed in EL4. Guanine nucleotide-independent PLD activity is present in membranes from all cells expressing PLD2. In PC12K cells, which express only PLD2, treatment with nerve growth factor causes neurite outgrowth and increases expression of PLD2 mRNA and protein within 6-12 h. A corresponding increase is observed in membrane PLD activity and in phorbol-12-myristate-13-acetate (PMA)-stimulated PLD activity in intact cells. These results show that PLD2 can be regulated both pretranslationally and posttranslationally by agonists.

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Genomic structure, cloning and expression of two phospholipase D isoenzymes from white cabbage

Schäffner

Rücknagel

Mansfeld

et al. 2002

Eur. J. Lipid Sci. Technol.

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Phospholipase D (PLD) from cabbage is interesting as biocatalyst in phospholipid transformation. To provide the basis for genetic engineering of the enzyme, gene cloning and sequencing were carried out. We have recently identified two isoenzymes, PLD1 and PLD2, on the basis of their cDNAs, here we describe their genomic structure consisting of 3404 and 3614 bp, respectively. Based on their sequence, PLD1 and PLD2 can be assigned to the α-type of plant PLDs, they contain two HKD motifs and the C2 domain with a phosphatidylinositol 4,5-bisphosphate (PIP 2 ) binding motif. Starting from pld1 cDNA, expression studies were carried out. Whereas expression using constructs with StrepTactin or Glutathion S-transferase tags was not successful, soluble active enzyme was produced from constructs without tag. pld2 was expressed accordingly. Both enzymes were purified by Ca 2+ -mediated hydrophobic interaction chromatography to high purity. N-terminal sequencing of PLD1 and PLD2 revealed that the Met-free N-termini of both enzymes correspond to sequences derived from the coding region of the pld1 and pld2 genes, respectively. Both recombinant enzymes showed highest hydrolytic activities at pH 5.5 to 5.6, independent of Ca 2+ concentration (10-100 mM). The optimum Ca 2+ concentration was 45 mM for PLD1 and PLD2. Both enzymes showed comparable activities in hydrolysis and transphosphatidylation of phospholipids.

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Phospholipase D signaling is essential for meiosis.

Abstract: Phospholipid metabolism plays an important role in cellular regulation by

Cited by 201 publications

References 33 publications

Identification of a novel, Ca²⁺‐dependent phospholipase D with preference for phosphatidylserine and phosphatidylethanolamine in Saccharomyces cerevisiae

Identification of a novel, Ca²⁺‐dependent phospholipase D with preference for phosphatidylserine and phosphatidylethanolamine in Saccharomyces cerevisiae

Expression and regulation of phospholipase D isoforms in mammalian cell lines

Genomic structure, cloning and expression of two phospholipase D isoenzymes from white cabbage

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Phospholipase D signaling is essential for meiosis.

Abstract: Phospholipid metabolism plays an important role in cellular regulation by

Cited by 201 publications

References 33 publications

Identification of a novel, Ca2+‐dependent phospholipase D with preference for phosphatidylserine and phosphatidylethanolamine in Saccharomyces cerevisiae

Identification of a novel, Ca2+‐dependent phospholipase D with preference for phosphatidylserine and phosphatidylethanolamine in Saccharomyces cerevisiae

Expression and regulation of phospholipase D isoforms in mammalian cell lines

Genomic structure, cloning and expression of two phospholipase D isoenzymes from white cabbage

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Product

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Identification of a novel, Ca²⁺‐dependent phospholipase D with preference for phosphatidylserine and phosphatidylethanolamine in Saccharomyces cerevisiae

Identification of a novel, Ca²⁺‐dependent phospholipase D with preference for phosphatidylserine and phosphatidylethanolamine in Saccharomyces cerevisiae