Phosphatidate phosphatase from Saccharomyces cerevisiae. Isolation of 45- and 104-kDa forms of the enzyme that are differentially regulated by inositol

Morlock, Kelly R.; McLaughlin, Jennifer; Lin, Yi; Carman, George M.

doi:10.1016/s0021-9258(19)67835-x

Cited by 63 publications

(9 citation statements)

References 48 publications

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“…The model for the recycling of Dol-P-(P) in Figure 2 clearly requires lipid phosphatases that can convert Dol-P-P to Dol-P and dephosphorylate Dol-P. These activities have been documented in microsomal fractions from yeast (Hosaka and Yamashita, 1984;Morlock et al, 1991;Carman, 1997) and many mammalian tissues (Idoyaga-Vargas et al, 1980;Wedgwood and Strominger, 1980;Appelkvist et al, 1981;Burton et al, 1981;Rip et al, 1981;Belocopitow and Boscoboinik, 1982;Scher and Waechter, 1984;Frank and Waechter, 1998), but their structures, specificity, subcellular locations, and Table III. Lipid-mediated reactions releasing Dol-P or Dol-P-P on the lumenal surface of the ER in yeasts and mammals Lipid-mediated reactions Number of lumenally oriented Dol-P(P)s formed for each reaction sequence M 5 N 2 -P-P-Dol → G 3 M 9 N 2 -P-P-Dol 7…”

Section: Proposed Roles For Dol-p-p/dol-p Phosphatase In the Recycling Modelmentioning

confidence: 97%

The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum

Schenk¹,

Fernández²,

Waechter³

2001

Glycobiology

175

190

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The precursor oligosaccharide donor for protein N-glycosylation in eukaryotes, Glc3Man9GlcNAc(2)-P-P-dolichol, is synthesized in two stages on both leaflets of the rough endoplasmic reticulum (ER). There is good evidence that the level of dolichyl monophosphate (Dol-P) is one rate-controlling factor in the first stage of the assembly process. In the current topological model it is proposed that ER proteins (flippases) then mediate the transbilayer movement of Man-P-Dol, Glc-P-Dol, and Man5GlcNAc(2)-P-P-Dol from the cytoplasmic leaflet to the lumenal leaflet. The rate of flipping of the three intermediates could plausibly influence the conversion of Man5GlcNAc(2)-P-P-Dol to Glc3Man(9)GlcNAc(2)-P-P-Dol in the second stage on the lumenal side of the rough ER. This article reviews the current understanding of the enzymes involved in the de novo biosynthesis of Dol-P and other polyisoprenoid glycosyl carrier lipids and speculates about the role of membrane proteins and enzymes that could be involved in the transbilayer movement of the lipid intermediates and the recycling of Dol-P and Dol-P-P discharged during glycosylphosphatidylinositol anchor biosynthesis, N-glycosylation, and O- and C-mannosylation reactions on the lumenal surface of the rough ER.

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Section: Proposed Roles For Dol-p-p/dol-p Phosphatase In the Recycling Modelmentioning

confidence: 97%

The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum

Schenk¹,

Fernández²,

Waechter³

2001

Glycobiology

175

190

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“…The biochemical properties of these PA phosphatases are similar except that the 104-kDa enzyme has a higher turnover number (Lin & Carman, 1989Morlock et al, 1991). Both PA phosphatase isoforms are regulated similarly by growth phase (Morlock et al, 1991), sphingoid bases (Wu et al, 1993), and nucleotides (Wu & Carman, 1994). On the other hand, the 104-and 45-kDa forms of PA phosphatase are regulated differentially by inositol supplementation (Morlock et al, 1988(Morlock et al, , 1991 and phosphorylation (Quinlan et al, 1992).…”

mentioning

confidence: 98%

“…Both PA phosphatase isoforms are regulated similarly by growth phase (Morlock et al, 1991), sphingoid bases (Wu et al, 1993), and nucleotides (Wu & Carman, 1994). On the other hand, the 104-and 45-kDa forms of PA phosphatase are regulated differentially by inositol supplementation (Morlock et al, 1988(Morlock et al, , 1991 and phosphorylation (Quinlan et al, 1992). Inositol supplementation induces the expression of 45-kDa PA phosphatase but has no effect on the expression of the 104-kDa enzyme (Morlock et al, 1991).…”

mentioning

confidence: 99%

“…Abbreviations: PA, phosphatidate; DG, diacylglycerol; TG, triacylglycerol; PE, phosphatidylethanolamine; PC, phosphatidylcholine; CDP-DG, CDP-diacylglycerol; PS, phosphatidylserine; PGP, phosphatidylglycerophosphate; PG, phosphatidylglycerol; CL, cardiolipin; PI, phosphatidylinositol; PIPs, polyphosphoinositides; SL, sphingolipids; Cer, ceramide; PAP, PA phosphatase; PSS, PS synthase. Two membrane-associated forms (104 and 45 kDa) of PA phosphatase have been purified and characterized from S. cereVisiae (Lin & Carman, 1989;Morlock et al, 1991). The biochemical properties of these PA phosphatases are similar except that the 104-kDa enzyme has a higher turnover number (Lin & Carman, 1989Morlock et al, 1991).…”

mentioning

confidence: 99%

“…Two membrane-associated forms (104 and 45 kDa) of PA phosphatase have been purified and characterized from S. cereVisiae (Lin & Carman, 1989;Morlock et al, 1991). The biochemical properties of these PA phosphatases are similar except that the 104-kDa enzyme has a higher turnover number (Lin & Carman, 1989Morlock et al, 1991). Both PA phosphatase isoforms are regulated similarly by growth phase (Morlock et al, 1991), sphingoid bases (Wu et al, 1993), and nucleotides (Wu & Carman, 1994).…”

mentioning

confidence: 99%

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Regulation of Phosphatidate Phosphatase Activity from the YeastSaccharomyces cerevisiaeby Phospholipids

Carman

1996

Biochemistry

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Regulation of Saccharomyces cerevisiae membrane-associated phosphatidate phosphatase (3-sn-phosphatidate phosphohydrolase, EC 3.1.3.4) activity by phospholipids was examined using purified enzyme and Triton X-100/phospholipid-mixed micelles. Anionic phospholipids activated phosphatidate phosphatase activity whereas zwitterionic phospholipids had a slight inhibitory effect on activity. Cardiolipin (A0.5 = 1.9 mol %), CDP-diacylglycerol (A0.5 = 2.6 mol %), and phosphatidylinositol (A0.5 = 5.5 mol %) were the most potent anionic phospholipid activators. Enzyme activation by cardiolipin (n=2.8), CDP-diacylglycerol (n=2.1), and phosphatidylinositol (n=3.3) followed positive cooperative kinetics. A kinetic analysis was performed to determine the mechanism of phosphatidate phosphatase activation by anionic phospholipids. The dependence of phosphatidate phosphatase on phosphatidate was cooperative (n approximately 2.2) in the absence and presence of phospholipid activators. Cardiolipin, CDP-diacylglycerol, and phosphatidylinositol were mixed competitive activators of phosphatidate phosphatase activity. The major effect of the activators was to cause a decrease in the Km for phosphatidate. Sphinganine, a positively charged sphingoid base, inhibited phosphatidate phosphatase activity and antagonized the activation of the enzyme by cardiolipin and phosphatidylinositol. Sphinganine caused an increase in the cooperativity of cardiolipin activation, but had little effect on the A0.5 value for cardiolipin. On the other hand, sphinganine had little effect on the cooperativity of phosphatidylinositol activation, but caused an increase in the A0.5 value for phosphatidylinositol. The activation constants for cardiolipin, CDP-diacylglycerol, and phosphatidylinositol were within the range of their cellular concentrations. These results suggested that the activation of phosphatidate phosphatase activity by anionic phospholipids may be physiologically relevant.

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Disruption of a Gene Encoding Phosphatidic Acid Phosphatase Causes Abnormal Phenotypes in Cell Growth and Abnormal Cytokinesis inSaccharomyces cerevisiae

Katagiri

Shinozaki

1998

Biochemical and Biophysical Research Communications

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Phosphatidate phosphatase from Saccharomyces cerevisiae. Isolation of 45- and 104-kDa forms of the enzyme that are differentially regulated by inositol

Cited by 63 publications

References 48 publications

The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum

The ins(ide) and outs(ide) of dolichyl phosphate biosynthesis and recycling in the endoplasmic reticulum

Regulation of Phosphatidate Phosphatase Activity from the YeastSaccharomyces cerevisiaeby Phospholipids

Disruption of a Gene Encoding Phosphatidic Acid Phosphatase Causes Abnormal Phenotypes in Cell Growth and Abnormal Cytokinesis inSaccharomyces cerevisiae

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