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Volumn 47, Issue 3, 2008, Pages 157-171

Synthesis and turnover of non-polar lipids in yeast

Author keywords

Acyltransferase; Lipase; Lipid particle droplet; Steryl ester; Triacylglycerol; Yeast

Indexed keywords

ESTER DERIVATIVE; GENE PRODUCT; HYDROLASE; MEMBRANE LIPID; STEROL ESTER; STERYL ESTER HYDROLASE; TRIACYLGLYCEROL; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 40849116174     PISSN: 01637827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plipres.2008.01.001     Document Type: Review
Times cited : (117)

References (141)
  • 1
    • 0022389171 scopus 로고
    • Cholesterol and cell membranes
    • Yeagle P.L. Cholesterol and cell membranes. Biochim Biophys Acta 882 (1985) 267-287
    • (1985) Biochim Biophys Acta , vol.882 , pp. 267-287
    • Yeagle, P.L.1
  • 2
    • 0028847265 scopus 로고
    • Physiological implications of sterol biosynthesis in yeast
    • Parks L.W., and Cassey W.M. Physiological implications of sterol biosynthesis in yeast. Annu Rev Microbiol 49 (1995) 95-116
    • (1995) Annu Rev Microbiol , vol.49 , pp. 95-116
    • Parks, L.W.1    Cassey, W.M.2
  • 3
    • 0032412784 scopus 로고    scopus 로고
    • Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae
    • Daum G., Lees N.D., Bard M., and Dickens R. Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae. Yeast 14 (1998) 1471-1501
    • (1998) Yeast , vol.14 , pp. 1471-1501
    • Daum, G.1    Lees, N.D.2    Bard, M.3    Dickens, R.4
  • 4
    • 0038491550 scopus 로고    scopus 로고
    • Ergosterol is required for targeting of tryptophan permease to yeast plasma membrane
    • Umebayashi K., and Nakano A. Ergosterol is required for targeting of tryptophan permease to yeast plasma membrane. J Cell Biol 161 (2003) 1117-1131
    • (2003) J Cell Biol , vol.161 , pp. 1117-1131
    • Umebayashi, K.1    Nakano, A.2
  • 5
    • 33749997544 scopus 로고    scopus 로고
    • Implications of sterol structure for membrane lipid composition, fluidity and phospholipid asymmetry in Saccharomyces cerevisiae
    • Sharma S.C. Implications of sterol structure for membrane lipid composition, fluidity and phospholipid asymmetry in Saccharomyces cerevisiae. FEMS Yeast Res 6 (2006) 1047-1051
    • (2006) FEMS Yeast Res , vol.6 , pp. 1047-1051
    • Sharma, S.C.1
  • 6
    • 27844526218 scopus 로고    scopus 로고
    • Homeostatic systems for sterols and other lipids
    • Garbarino J., and Sturley S.L. Homeostatic systems for sterols and other lipids. Biochem Soc Trans 33 (2005) 1182-1185
    • (2005) Biochem Soc Trans , vol.33 , pp. 1182-1185
    • Garbarino, J.1    Sturley, S.L.2
  • 7
    • 0032693609 scopus 로고    scopus 로고
    • Identification and characterization of major LP proteins of the yeast Saccharomyces cerevisiae
    • Athenstaedt K., Zweytick D., Jandrositz A., Kohlwein S.D., and Daum G. Identification and characterization of major LP proteins of the yeast Saccharomyces cerevisiae. J Bacteriol 181 (1999) 6441-6648
    • (1999) J Bacteriol , vol.181 , pp. 6441-6648
    • Athenstaedt, K.1    Zweytick, D.2    Jandrositz, A.3    Kohlwein, S.D.4    Daum, G.5
  • 8
    • 0029026637 scopus 로고
    • Eukaryotic phospholipid biosynthesis
    • Kent C. Eukaryotic phospholipid biosynthesis. Annu Rev Biochem 64 (1995) 315-343
    • (1995) Annu Rev Biochem , vol.64 , pp. 315-343
    • Kent, C.1
  • 9
    • 0029920267 scopus 로고    scopus 로고
    • Regulation of phospholipid biosynthesis in the yeast Saccharomyces cerevisiae
    • Carman G.M., and Zeimetz G.M. Regulation of phospholipid biosynthesis in the yeast Saccharomyces cerevisiae. J Biol Chem 271 (1996) 13293-13296
    • (1996) J Biol Chem , vol.271 , pp. 13293-13296
    • Carman, G.M.1    Zeimetz, G.M.2
  • 10
    • 0034684048 scopus 로고    scopus 로고
    • Intracellular lipid particles of eukaryotic cells
    • Zweytick D., Athenstaedt K., and Daum G. Intracellular lipid particles of eukaryotic cells. Biochim Biophys Acta 1469 (2000) 101-120
    • (2000) Biochim Biophys Acta , vol.1469 , pp. 101-120
    • Zweytick, D.1    Athenstaedt, K.2    Daum, G.3
  • 11
    • 0035810964 scopus 로고    scopus 로고
    • Lipid droplet: proteins floating on a pool of fat
    • Brown D.A. Lipid droplet: proteins floating on a pool of fat. Curr Biol 11 (2001) 446-449
    • (2001) Curr Biol , vol.11 , pp. 446-449
    • Brown, D.A.1
  • 12
    • 0032730257 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in the yeast Saccharomyces cerevisiae and interrelationship with other metabolic processes
    • Carman G.M., and Henry S.A. Phospholipid biosynthesis in the yeast Saccharomyces cerevisiae and interrelationship with other metabolic processes. Prog Lipid Res 38 (1999) 361-399
    • (1999) Prog Lipid Res , vol.38 , pp. 361-399
    • Carman, G.M.1    Henry, S.A.2
  • 13
    • 0034717835 scopus 로고    scopus 로고
    • Interorganelle transport of aminoglycerophospholipids
    • Voelker D.R. Interorganelle transport of aminoglycerophospholipids. Biochim Biophys Acta 1486 (2000) 97-107
    • (2000) Biochim Biophys Acta , vol.1486 , pp. 97-107
    • Voelker, D.R.1
  • 14
    • 21544470248 scopus 로고    scopus 로고
    • Protein kinase C and phospholipase D: intimate interactions in intracellular signaling
    • Becker K.P., and Hannun Y.A. Protein kinase C and phospholipase D: intimate interactions in intracellular signaling. Cell Mol Life Sci 62 (2005) 1448-1461
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1448-1461
    • Becker, K.P.1    Hannun, Y.A.2
  • 15
    • 34147158237 scopus 로고    scopus 로고
    • Regulation of triglyceride metabolism. I. Eukaryotic neutral lipid synthesis: many ways to skin ACAT or a DGAT
    • Turkish A., and Sturley S.L. Regulation of triglyceride metabolism. I. Eukaryotic neutral lipid synthesis: many ways to skin ACAT or a DGAT. Am J Physiol Gastrointest Liver Physiol 292 (2007) G953-G957
    • (2007) Am J Physiol Gastrointest Liver Physiol , vol.292
    • Turkish, A.1    Sturley, S.L.2
  • 16
    • 33749058310 scopus 로고    scopus 로고
    • A proposed model of fat packaging by exchangeable lipid droplet proteins
    • Wolins N.E., Brasaemle D.L., and Bickel P.E. A proposed model of fat packaging by exchangeable lipid droplet proteins. FEBS Lett 580 (2006) 5484-5491
    • (2006) FEBS Lett , vol.580 , pp. 5484-5491
    • Wolins, N.E.1    Brasaemle, D.L.2    Bickel, P.E.3
  • 17
    • 0033571069 scopus 로고    scopus 로고
    • Phosphatidic acid, a key intermediate in lipid metabolism
    • Athenstaedt K., and Daum G. Phosphatidic acid, a key intermediate in lipid metabolism. Eur J Biochem 266 (1999) 1-16
    • (1999) Eur J Biochem , vol.266 , pp. 1-16
    • Athenstaedt, K.1    Daum, G.2
  • 18
    • 0038182336 scopus 로고    scopus 로고
    • Triacylglycerol biosynthesis in yeast
    • Sorger D., and Daum G. Triacylglycerol biosynthesis in yeast. Appl Microbiol Biotechnol 61 (2003) 289-299
    • (2003) Appl Microbiol Biotechnol , vol.61 , pp. 289-299
    • Sorger, D.1    Daum, G.2
  • 20
    • 0038081050 scopus 로고    scopus 로고
    • Phosphorylation of the yeast phospholipid synthesis regulatory protein Opi1p by protein kinase A
    • Sreenivas A., and Carman G.M. Phosphorylation of the yeast phospholipid synthesis regulatory protein Opi1p by protein kinase A. J Biol Chem 278 (2003) 20673-20680
    • (2003) J Biol Chem , vol.278 , pp. 20673-20680
    • Sreenivas, A.1    Carman, G.M.2
  • 21
    • 0032812984 scopus 로고    scopus 로고
    • Overproduction of the Opi1 repressor inhibits transcriptional activation of structural genes required for phospholipid biosynthesis in the yeast Saccharomyces cerevisiae
    • Wagner C., Blank M., Strohmann B., and Schueller H.J. Overproduction of the Opi1 repressor inhibits transcriptional activation of structural genes required for phospholipid biosynthesis in the yeast Saccharomyces cerevisiae. Yeast 15 (1999) 843-854
    • (1999) Yeast , vol.15 , pp. 843-854
    • Wagner, C.1    Blank, M.2    Strohmann, B.3    Schueller, H.J.4
  • 22
    • 0029920267 scopus 로고    scopus 로고
    • Regulation of phospholipid biosynthesis in the yeast Saccharomyces cerevisiae
    • Carman G.M., and Zeimetz G.M. Regulation of phospholipid biosynthesis in the yeast Saccharomyces cerevisiae. J Biol Chem 71 (1996) 13293-13296
    • (1996) J Biol Chem , vol.71 , pp. 13293-13296
    • Carman, G.M.1    Zeimetz, G.M.2
  • 23
    • 0029963923 scopus 로고    scopus 로고
    • Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae
    • Greenberg M.L., and Lopes J.M. Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae. Microbiol Rev 60 (1996) 1-20
    • (1996) Microbiol Rev , vol.60 , pp. 1-20
    • Greenberg, M.L.1    Lopes, J.M.2
  • 24
    • 0000600344 scopus 로고
    • Regulation and compartmentalization of lipid synthesis in yeast
    • Broach J., Jones E., and Pringle J. (Eds), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Paltauf F., Kohlwein S.D., and Henry S.A. Regulation and compartmentalization of lipid synthesis in yeast. In: Broach J., Jones E., and Pringle J. (Eds). Molecular biology of the yeast Saccharomyces cerevisiae vol. II (1992), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 415-500
    • (1992) Molecular biology of the yeast Saccharomyces cerevisiae , vol.II , pp. 415-500
    • Paltauf, F.1    Kohlwein, S.D.2    Henry, S.A.3
  • 25
    • 0035834657 scopus 로고    scopus 로고
    • The initial step of the glycerolipid pathway: identification of glycerol 3-phosphate/dihydroxyacetone phosphate dual substrate acyltransferases in Saccharomyces cerevisiae
    • Zheng Z., and Zou J. The initial step of the glycerolipid pathway: identification of glycerol 3-phosphate/dihydroxyacetone phosphate dual substrate acyltransferases in Saccharomyces cerevisiae. J Biol Chem 276 (2001) 41710-41716
    • (2001) J Biol Chem , vol.276 , pp. 41710-41716
    • Zheng, Z.1    Zou, J.2
  • 26
    • 0033033118 scopus 로고    scopus 로고
    • Redundant systems of phosphatidic acid biosynthesis via acylation of glycerol-3-phosphate or dihydroxyacetone phosphate in the yeast Saccharomyces cerevisiae
    • Athenstaedt K., Weys S., Paltauf F., and Daum G. Redundant systems of phosphatidic acid biosynthesis via acylation of glycerol-3-phosphate or dihydroxyacetone phosphate in the yeast Saccharomyces cerevisiae. J Bacteriol 181 (1999) 1458-1463
    • (1999) J Bacteriol , vol.181 , pp. 1458-1463
    • Athenstaedt, K.1    Weys, S.2    Paltauf, F.3    Daum, G.4
  • 27
    • 0026796052 scopus 로고
    • The acyl dihydroxyacetone phosphate pathway enzymes for glycerolipid biosynthesis are present in the yeast Saccharomyces cerevisiae
    • Racenis P.V., Lai J.L., Das A.K., Mullick P.C., Hajra A.K., and Greenberg M.L. The acyl dihydroxyacetone phosphate pathway enzymes for glycerolipid biosynthesis are present in the yeast Saccharomyces cerevisiae. J Bacteriol 174 (1992) 5702-5710
    • (1992) J Bacteriol , vol.174 , pp. 5702-5710
    • Racenis, P.V.1    Lai, J.L.2    Das, A.K.3    Mullick, P.C.4    Hajra, A.K.5    Greenberg, M.L.6
  • 28
    • 0034614454 scopus 로고    scopus 로고
    • 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles
    • Athenstaedt K., and Daum G. 1-Acyldihydroxyacetone-phosphate reductase (Ayr1p) of the yeast Saccharomyces cerevisiae encoded by the open reading frame YIL124w is a major component of lipid particles. J Biol Chem 275 (2000) 235-240
    • (2000) J Biol Chem , vol.275 , pp. 235-240
    • Athenstaedt, K.1    Daum, G.2
  • 29
    • 0036310306 scopus 로고    scopus 로고
    • Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17β-hydroxysteroid dehydrogenase activity
    • Vico P., Cauet G., Rose K., Lathe R., and Degryse E. Dehydroepiandrosterone (DHEA) metabolism in Saccharomyces cerevisiae expressing mammalian steroid hydroxylase CYP7B: Ayr1p and Fox2p display 17β-hydroxysteroid dehydrogenase activity. Yeast 19 (2002) 873-886
    • (2002) Yeast , vol.19 , pp. 873-886
    • Vico, P.1    Cauet, G.2    Rose, K.3    Lathe, R.4    Degryse, E.5
  • 30
    • 0030867130 scopus 로고    scopus 로고
    • Biosynthesis of phosphatidic acid in lipid particles and endoplasmic reticulum of Saccharomyces cerevisiae
    • Athenstaedt K., and Daum G. Biosynthesis of phosphatidic acid in lipid particles and endoplasmic reticulum of Saccharomyces cerevisiae. J Bacteriol 179 (1997) 7611-7616
    • (1997) J Bacteriol , vol.179 , pp. 7611-7616
    • Athenstaedt, K.1    Daum, G.2
  • 31
    • 35648995880 scopus 로고    scopus 로고
    • SLC1 and SLC4 encode partially redundant acyl-coenzyme A 1-acylglycerol-3-phosphate O-acyltransferase of budding yeast
    • Benghezal M., Roubaty C., Veepuri V., Knudsen J., and Conzelmann A. SLC1 and SLC4 encode partially redundant acyl-coenzyme A 1-acylglycerol-3-phosphate O-acyltransferase of budding yeast. J Biol Chem 282 (2007) 30845-30855
    • (2007) J Biol Chem , vol.282 , pp. 30845-30855
    • Benghezal, M.1    Roubaty, C.2    Veepuri, V.3    Knudsen, J.4    Conzelmann, A.5
  • 32
    • 0027438892 scopus 로고
    • A suppressor gene that enables Saccharomyces cerevisiae to grow without making sphingolipids encodes a protein that resembles an Escherichia coli fatty acyltransferase
    • Nagiec M.M., Wells G.B., Lester R.L., and Dickson R.X. A suppressor gene that enables Saccharomyces cerevisiae to grow without making sphingolipids encodes a protein that resembles an Escherichia coli fatty acyltransferase. J Biol Chem 268 (1993) 22156-22163
    • (1993) J Biol Chem , vol.268 , pp. 22156-22163
    • Nagiec, M.M.1    Wells, G.B.2    Lester, R.L.3    Dickson, R.X.4
  • 33
    • 36348989203 scopus 로고    scopus 로고
    • LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation of lysophospholipids in the yeast Saccharomyces cerevisiae
    • Tamaki H., Shimada A., Ito Y., Ohya M., Takase J., Miyashita M., et al. LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation of lysophospholipids in the yeast Saccharomyces cerevisiae. J Biol Chem 282 (2007) 34288-34298
    • (2007) J Biol Chem , vol.282 , pp. 34288-34298
    • Tamaki, H.1    Shimada, A.2    Ito, Y.3    Ohya, M.4    Takase, J.5    Miyashita, M.6
  • 34
    • 35348954738 scopus 로고    scopus 로고
    • Identification and characterization of the major lysophosphatidylethanolamine acyltransferase in Saccharomyces cerevisiae
    • Riekhof W.R., Wu J., Jones J.L., and Voelker D.R. Identification and characterization of the major lysophosphatidylethanolamine acyltransferase in Saccharomyces cerevisiae. J Biol Chem 282 (2007) 28344-28352
    • (2007) J Biol Chem , vol.282 , pp. 28344-28352
    • Riekhof, W.R.1    Wu, J.2    Jones, J.L.3    Voelker, D.R.4
  • 35
    • 35648981002 scopus 로고    scopus 로고
    • Identification of a novel lysophospholipid acyltransferase in Saccharomyces cerevisiae
    • Jain S., Stanford N., Bhagwat N., Seiler B., Costanzo M., Boone C., et al. Identification of a novel lysophospholipid acyltransferase in Saccharomyces cerevisiae. J Biol Chem 282 (2007) 30562-30569
    • (2007) J Biol Chem , vol.282 , pp. 30562-30569
    • Jain, S.1    Stanford, N.2    Bhagwat, N.3    Seiler, B.4    Costanzo, M.5    Boone, C.6
  • 37
    • 33846501577 scopus 로고    scopus 로고
    • Dynamics of neutral lipid storage and mobilization in yeast
    • Daum G., Wagner A., Czabany T., and Athenstaedt K. Dynamics of neutral lipid storage and mobilization in yeast. Biochimie 89 (2007) 243-248
    • (2007) Biochimie , vol.89 , pp. 243-248
    • Daum, G.1    Wagner, A.2    Czabany, T.3    Athenstaedt, K.4
  • 38
    • 33745307534 scopus 로고    scopus 로고
    • The life cycle of neutral lipids: synthesis, storage and degradation
    • Athenstaedt K., and Daum G. The life cycle of neutral lipids: synthesis, storage and degradation. Cell Mol Life Sci 63 (2006) 1355-1369
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1355-1369
    • Athenstaedt, K.1    Daum, G.2
  • 39
    • 33646920976 scopus 로고    scopus 로고
    • 2+-dependent phosphatidate phosphatase enzyme
    • 2+-dependent phosphatidate phosphatase enzyme. J Biol Chem 281 (2006) 9210-9218
    • (2006) J Biol Chem , vol.281 , pp. 9210-9218
    • Han, G.S.1    Wu, W.I.2    Carman, G.M.3
  • 40
    • 33947542353 scopus 로고    scopus 로고
    • Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns
    • Donkor J., Sariahmetoglu M., Dewald J., Brindley D.N., and Reue K. Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns. J Biol Chem 282 (2007) 3450-3457
    • (2007) J Biol Chem , vol.282 , pp. 3450-3457
    • Donkor, J.1    Sariahmetoglu, M.2    Dewald, J.3    Brindley, D.N.4    Reue, K.5
  • 41
    • 37549018969 scopus 로고    scopus 로고
    • The cellular functions of the yeast lipin homolog Pah1p are dependent on its phosphatidate phosphatase activity
    • Han G.S., Siniossoglou S., and Carman G.M. The cellular functions of the yeast lipin homolog Pah1p are dependent on its phosphatidate phosphatase activity. J Biol Chem 282 (2007) 37026-37035
    • (2007) J Biol Chem , vol.282 , pp. 37026-37035
    • Han, G.S.1    Siniossoglou, S.2    Carman, G.M.3
  • 42
    • 33751216445 scopus 로고    scopus 로고
    • Roles of phosphatidate phosphatase enzymes in lipid metabolism
    • Carman G.M., and Han G.S. Roles of phosphatidate phosphatase enzymes in lipid metabolism. Trends Biochem Sci 31 (2006) 694-699
    • (2006) Trends Biochem Sci , vol.31 , pp. 694-699
    • Carman, G.M.1    Han, G.S.2
  • 43
    • 21244480972 scopus 로고    scopus 로고
    • The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth
    • Santos-Rosa H., Leung J., Grimsey N., Peak-Chew S., and Siniossoglou S. The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth. EMBO J 24 (2005) 1931-1941
    • (2005) EMBO J , vol.24 , pp. 1931-1941
    • Santos-Rosa, H.1    Leung, J.2    Grimsey, N.3    Peak-Chew, S.4    Siniossoglou, S.5
  • 44
    • 40849147909 scopus 로고    scopus 로고
    • Kinetic analysis of sphingoid base inhibition of yeast phosphatidate phosphatase
    • Wu W.I., and Carman G.M. Kinetic analysis of sphingoid base inhibition of yeast phosphatidate phosphatase. Biochemistry 25 (1996) 2790-3796
    • (1996) Biochemistry , vol.25 , pp. 2790-3796
    • Wu, W.I.1    Carman, G.M.2
  • 45
    • 0027192315 scopus 로고
    • Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by sphingoid bases
    • Wu W.I., Lin Y.P., Wang E., Merrill Jr. A.H., and Carman G.M. Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by sphingoid bases. J Biol Chem 268 (1993) 13830-13837
    • (1993) J Biol Chem , vol.268 , pp. 13830-13837
    • Wu, W.I.1    Lin, Y.P.2    Wang, E.3    Merrill Jr., A.H.4    Carman, G.M.5
  • 46
    • 0028150667 scopus 로고
    • Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by nucleotides
    • Wu W.I., and Carman G.M. Regulation of phosphatidate phosphatase activity from the yeast Saccharomyces cerevisiae by nucleotides. J Biol Chem 269 (1994) 29496-29501
    • (1994) J Biol Chem , vol.269 , pp. 29496-29501
    • Wu, W.I.1    Carman, G.M.2
  • 47
    • 33751256342 scopus 로고    scopus 로고
    • Control of phospholipid synthesis by phosphorylation of the yeast lipin Pah1p/Smp2p Mg2+-dependent phosphatidate phosphatase
    • O'Hara L., Han G.S., Peak-Chew S., Grimsey N., Carman G.M., and Siniossoglou S. Control of phospholipid synthesis by phosphorylation of the yeast lipin Pah1p/Smp2p Mg2+-dependent phosphatidate phosphatase. J Biol Chem 281 (2006) 3450-3457
    • (2006) J Biol Chem , vol.281 , pp. 3450-3457
    • O'Hara, L.1    Han, G.S.2    Peak-Chew, S.3    Grimsey, N.4    Carman, G.M.5    Siniossoglou, S.6
  • 48
    • 0031552935 scopus 로고    scopus 로고
    • Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli
    • Carman G.M. Phosphatidate phosphatases and diacylglycerol pyrophosphate phosphatases in Saccharomyces cerevisiae and Escherichia coli. Biochim Biophys Acta 1348 (1997) 45-55
    • (1997) Biochim Biophys Acta , vol.1348 , pp. 45-55
    • Carman, G.M.1
  • 49
    • 0029920267 scopus 로고    scopus 로고
    • Regulation of phospholipid biosynthesis in the yeast Saccharomyces cerevisiae
    • Carman G.M., and Zeimetz G.M. Regulation of phospholipid biosynthesis in the yeast Saccharomyces cerevisiae. J Biol Chem 271 (1996) 13293-13296
    • (1996) J Biol Chem , vol.271 , pp. 13293-13296
    • Carman, G.M.1    Zeimetz, G.M.2
  • 50
    • 33751216445 scopus 로고    scopus 로고
    • Roles of phosphatidate phosphatase enzymes in lipid metabolism
    • Carman G.M., and Han G.S. Roles of phosphatidate phosphatase enzymes in lipid metabolism. Trends Biochem Sci 31 (2006) 694-699
    • (2006) Trends Biochem Sci , vol.31 , pp. 694-699
    • Carman, G.M.1    Han, G.S.2
  • 51
    • 15144354137 scopus 로고    scopus 로고
    • Isolation and characterization of the Saccharomyces cerevisiae DPP1 gene encoding diacylglycerol pyrophosphate phosphatase
    • Toke D.A., Bennett W.L., Dillon D.A., Wu W.I., Chen X., Ostrander D.B., et al. Isolation and characterization of the Saccharomyces cerevisiae DPP1 gene encoding diacylglycerol pyrophosphate phosphatase. J Biol Chem 273 (1998) 3278-3284
    • (1998) J Biol Chem , vol.273 , pp. 3278-3284
    • Toke, D.A.1    Bennett, W.L.2    Dillon, D.A.3    Wu, W.I.4    Chen, X.5    Ostrander, D.B.6
  • 53
    • 0030032698 scopus 로고    scopus 로고
    • Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae
    • Wu W.I., Liu Y., Riedel B., Wissing J.B., Fischl A.S., and Carman G.M. Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae. J Biol Chem 271 (1996) 1868-1876
    • (1996) J Biol Chem , vol.271 , pp. 1868-1876
    • Wu, W.I.1    Liu, Y.2    Riedel, B.3    Wissing, J.B.4    Fischl, A.S.5    Carman, G.M.6
  • 54
    • 0033951478 scopus 로고    scopus 로고
    • Enzymological properties of the LPP1-encoded lipid phosphatase from Saccharomyces cerevisiae
    • Furneisen J.M., and Carman G.M. Enzymological properties of the LPP1-encoded lipid phosphatase from Saccharomyces cerevisiae. Biochim Biophys Acta 1484 (2000) 71-82
    • (2000) Biochim Biophys Acta , vol.1484 , pp. 71-82
    • Furneisen, J.M.1    Carman, G.M.2
  • 55
    • 0033591216 scopus 로고    scopus 로고
    • The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae
    • Faulkner A., Chen X., Rush J., Horazdovsky B., Waechter C.J., Carman G.M., et al. The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae. J Biol Chem 274 (1999) 14831-14837
    • (1999) J Biol Chem , vol.274 , pp. 14831-14837
    • Faulkner, A.1    Chen, X.2    Rush, J.3    Horazdovsky, B.4    Waechter, C.J.5    Carman, G.M.6
  • 56
    • 0031048876 scopus 로고    scopus 로고
    • Identification of a novel phosphatase sequence motif
    • Stukey J., and Carman G.M. Identification of a novel phosphatase sequence motif. Protein Sci 6 (1997) 469-472
    • (1997) Protein Sci , vol.6 , pp. 469-472
    • Stukey, J.1    Carman, G.M.2
  • 57
    • 40849100973 scopus 로고    scopus 로고
    • Vacuole membrane topography of the DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc
    • Han G.S., Johnston C.N., and Carman G.M. Vacuole membrane topography of the DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc. J Biol Chem 276 (2001) 14331-14338
    • (2001) J Biol Chem , vol.276 , pp. 14331-14338
    • Han, G.S.1    Johnston, C.N.2    Carman, G.M.3
  • 59
    • 0030027564 scopus 로고    scopus 로고
    • Identification and characterization of a gene encoding phospholipase D activity in yeast
    • Waksman M., Eli Y., Liscovitch M., and Gerst J.E. Identification and characterization of a gene encoding phospholipase D activity in yeast. J Biol Chem 271 (1996) 2361-2364
    • (1996) J Biol Chem , vol.271 , pp. 2361-2364
    • Waksman, M.1    Eli, Y.2    Liscovitch, M.3    Gerst, J.E.4
  • 60
    • 0030614455 scopus 로고    scopus 로고
    • 2+-dependent, phosphatidylethanolamine-hydrolyzing phospholipase D in yeast bearing a disruption in PLD1
    • 2+-dependent, phosphatidylethanolamine-hydrolyzing phospholipase D in yeast bearing a disruption in PLD1. J Biol Chem 272 (1997) 36-39
    • (1997) J Biol Chem , vol.272 , pp. 36-39
    • Waksman, M.1    Tang, X.2    Eli, Y.3    Gerst, J.E.4    Liscovitch, M.5
  • 61
    • 0030062093 scopus 로고    scopus 로고
    • Characterization of Saccharomyces cerevisiae deficient in expression of phospholipase D
    • Ella K.M., Dolan J.W., Qi C., and Meier K.E. Characterization of Saccharomyces cerevisiae deficient in expression of phospholipase D. Biochem J 314 (1996) 15-19
    • (1996) Biochem J , vol.314 , pp. 15-19
    • Ella, K.M.1    Dolan, J.W.2    Qi, C.3    Meier, K.E.4
  • 63
    • 0027304451 scopus 로고
    • Genetic and biochemical characterization of a phosphatidylinositol-specific phospholipase C in Saccharomyces cerevisiae
    • Flick J.S., and Thorner J. Genetic and biochemical characterization of a phosphatidylinositol-specific phospholipase C in Saccharomyces cerevisiae. Mol Cell Biol 13 (1993) 5861-5876
    • (1993) Mol Cell Biol , vol.13 , pp. 5861-5876
    • Flick, J.S.1    Thorner, J.2
  • 64
    • 0030175841 scopus 로고    scopus 로고
    • Biosynthesis of triacylglycerols
    • Lehner R., and Kuksis A. Biosynthesis of triacylglycerols. Prog Lipid Res 35 (1996) 169-201
    • (1996) Prog Lipid Res , vol.35 , pp. 169-201
    • Lehner, R.1    Kuksis, A.2
  • 65
    • 0036135597 scopus 로고    scopus 로고
    • Synthesis of triacylglycerols by the acyl-coenzyme A:diacylglycerol acyltransferase Dga1p in lipid particles of the yeast Saccharomyces cerevisiae
    • Sorger D., and Daum G. Synthesis of triacylglycerols by the acyl-coenzyme A:diacylglycerol acyltransferase Dga1p in lipid particles of the yeast Saccharomyces cerevisiae. J Bacteriol 184 (2002) 519-524
    • (2002) J Bacteriol , vol.184 , pp. 519-524
    • Sorger, D.1    Daum, G.2
  • 66
    • 0033522379 scopus 로고    scopus 로고
    • Analysis of amino acid motifs diagnostic for the sn-glycerol-3-phosphate acyltransferase reaction
    • Lewin T.M., Wang P., and Coleman R.A. Analysis of amino acid motifs diagnostic for the sn-glycerol-3-phosphate acyltransferase reaction. Biochemistry 38 (1999) 5764-5771
    • (1999) Biochemistry , vol.38 , pp. 5764-5771
    • Lewin, T.M.1    Wang, P.2    Coleman, R.A.3
  • 67
    • 0037088637 scopus 로고    scopus 로고
    • The DGA1 gene determines a second triglyceride synthetic pathway in yeast
    • Oelkers P., Cromley D., Padamsee M., Billheimer J.T., and Sturley S.L. The DGA1 gene determines a second triglyceride synthetic pathway in yeast. J Biol Chem 277 (2002) 8877-8881
    • (2002) J Biol Chem , vol.277 , pp. 8877-8881
    • Oelkers, P.1    Cromley, D.2    Padamsee, M.3    Billheimer, J.T.4    Sturley, S.L.5
  • 68
    • 0034612345 scopus 로고    scopus 로고
    • Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants
    • Dahlqvist A., Stahl U., Lenman M., Banas A., Lee M., Sandager L., et al. Phospholipid:diacylglycerol acyltransferase: an enzyme that catalyzes the acyl-CoA-independent formation of triacylglycerol in yeast and plants. Proc Natl Acad Sci USA 97 (2000) 6487-6492
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6487-6492
    • Dahlqvist, A.1    Stahl, U.2    Lenman, M.3    Banas, A.4    Lee, M.5    Sandager, L.6
  • 69
    • 0034717265 scopus 로고    scopus 로고
    • A lecithin cholesterol acyltransferase-like gene mediates diacylglycerol esterification in yeast
    • Oelkers P., Tinkelenberg A., Erdeniz N., Cromley D., Billheimer I.T., and Sturley S.L. A lecithin cholesterol acyltransferase-like gene mediates diacylglycerol esterification in yeast. J Biol Chem 275 (2000) 15609-15612
    • (2000) J Biol Chem , vol.275 , pp. 15609-15612
    • Oelkers, P.1    Tinkelenberg, A.2    Erdeniz, N.3    Cromley, D.4    Billheimer, I.T.5    Sturley, S.L.6
  • 70
    • 3843131947 scopus 로고    scopus 로고
    • A yeast strain lacking lipid particles bears a defect in ergosterol formation
    • Sorger D., Athenstaedt K., Hrastnik C., and Daum G. A yeast strain lacking lipid particles bears a defect in ergosterol formation. J Biol Chem 279 (2004) 31190-31196
    • (2004) J Biol Chem , vol.279 , pp. 31190-31196
    • Sorger, D.1    Athenstaedt, K.2    Hrastnik, C.3    Daum, G.4
  • 71
    • 0035914412 scopus 로고    scopus 로고
    • DGAT2 is a new diacylglycerol acyltransferase gene family: purification, cloning, and expression in insect cells of two polypeptides from Mortierella ramanniana with diacylglycerol acyltransferase activity
    • Lardizabal K.D., Mai J.T., Wagner N.W., Wyrick A., Voelker T., and Hawkins D.J. DGAT2 is a new diacylglycerol acyltransferase gene family: purification, cloning, and expression in insect cells of two polypeptides from Mortierella ramanniana with diacylglycerol acyltransferase activity. J Biol Chem 276 (2001) 38862-38869
    • (2001) J Biol Chem , vol.276 , pp. 38862-38869
    • Lardizabal, K.D.1    Mai, J.T.2    Wagner, N.W.3    Wyrick, A.4    Voelker, T.5    Hawkins, D.J.6
  • 72
    • 0035914356 scopus 로고    scopus 로고
    • Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members
    • Cases S., Stone S.J., Zhou P., Yen E., Tow B., Lardizabal K.D., et al. Cloning of DGAT2, a second mammalian diacylglycerol acyltransferase, and related family members. J Biol Chem 276 (2001) 38870-38876
    • (2001) J Biol Chem , vol.276 , pp. 38870-38876
    • Cases, S.1    Stone, S.J.2    Zhou, P.3    Yen, E.4    Tow, B.5    Lardizabal, K.D.6
  • 73
    • 0031041071 scopus 로고    scopus 로고
    • Functional expression of a cDNA to human acyl-coenzyme A:cholesterol acyltransferase in yeast. Species-dependent substrate specificity and inhibitor sensitivity
    • Yang H., Cromley D., Wang H., Billheimer J.T., and Sturley S.L. Functional expression of a cDNA to human acyl-coenzyme A:cholesterol acyltransferase in yeast. Species-dependent substrate specificity and inhibitor sensitivity. J Biol Chem 272 (1997) 3980-3985
    • (1997) J Biol Chem , vol.272 , pp. 3980-3985
    • Yang, H.1    Cromley, D.2    Wang, H.3    Billheimer, J.T.4    Sturley, S.L.5
  • 74
    • 36348956692 scopus 로고    scopus 로고
    • DGA1 (diacylglycerol acyltransferase gene) overexpression and leucine biosynthesis significantly increase lipid accumulation in the Δsnf2 disruptant of Saccharomyces cerevisiae
    • Kamisaka Y., Tomita N., Kimura K., Kainou K., and Uemura H. DGA1 (diacylglycerol acyltransferase gene) overexpression and leucine biosynthesis significantly increase lipid accumulation in the Δsnf2 disruptant of Saccharomyces cerevisiae. Biochem J 408 (2007) 61-68
    • (2007) Biochem J , vol.408 , pp. 61-68
    • Kamisaka, Y.1    Tomita, N.2    Kimura, K.3    Kainou, K.4    Uemura, H.5
  • 75
    • 0028987639 scopus 로고
    • The SNF2/SWI2/GAM1/TYE3/RIC1 gene is involved in the coordinate regulation of phospholipid synthesis in Saccharomyces cerevisiae
    • Kodaki T., Hosaka K., Nikawa J., and Yamashita S. The SNF2/SWI2/GAM1/TYE3/RIC1 gene is involved in the coordinate regulation of phospholipid synthesis in Saccharomyces cerevisiae. J Biochem (Tokyo) 117 (1995) 362-368
    • (1995) J Biochem (Tokyo) , vol.117 , pp. 362-368
    • Kodaki, T.1    Hosaka, K.2    Nikawa, J.3    Yamashita, S.4
  • 76
    • 33645232394 scopus 로고    scopus 로고
    • Identification of genes affecting lipid content using transposon mutagenesis in Saccharomyces cerevisiae
    • Kamisaka Y., Noda N., Tomita N., Kimura K., Kodaki T., and Hosaka K. Identification of genes affecting lipid content using transposon mutagenesis in Saccharomyces cerevisiae. Biosci Biotechnol Biochem 70 (2006) 646-653
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 646-653
    • Kamisaka, Y.1    Noda, N.2    Tomita, N.3    Kimura, K.4    Kodaki, T.5    Hosaka, K.6
  • 77
    • 0345171460 scopus 로고    scopus 로고
    • Enzymes of triacylglycerol synthesis and their regulation
    • Coleman R.A., and Lee D.P. Enzymes of triacylglycerol synthesis and their regulation. Prog Lipid Res 43 (2004) 134-176
    • (2004) Prog Lipid Res , vol.43 , pp. 134-176
    • Coleman, R.A.1    Lee, D.P.2
  • 78
    • 33846211895 scopus 로고    scopus 로고
    • Diacylglycerol acyltransferase: a key mediator of plant triacylglycerol synthesis
    • Lung S.C., and Weselake R.J. Diacylglycerol acyltransferase: a key mediator of plant triacylglycerol synthesis. Lipids 41 (2006) 1073-1088
    • (2006) Lipids , vol.41 , pp. 1073-1088
    • Lung, S.C.1    Weselake, R.J.2
  • 79
    • 15944416374 scopus 로고    scopus 로고
    • Mechanisms and mediators of neutral lipid biosynthesis in eukaryotic cells
    • Daum G. (Ed), Springer, Berlin/Heidelberg/New York
    • Oelkers P.M., and Sturley S.L. Mechanisms and mediators of neutral lipid biosynthesis in eukaryotic cells. In: Daum G. (Ed). Lipid metabolism and membrane biogenesis (2004), Springer, Berlin/Heidelberg/New York 289-311
    • (2004) Lipid metabolism and membrane biogenesis , pp. 289-311
    • Oelkers, P.M.1    Sturley, S.L.2
  • 80
    • 0029835340 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two isoforms of Saccharomyces cerevisiae acyl-CoA:sterol acyltransferase
    • Yu C., Kennedy N.J., Chang C.C., and Rothblatt J.A. Molecular cloning and characterization of two isoforms of Saccharomyces cerevisiae acyl-CoA:sterol acyltransferase. J Biol Chem 271 (1996) 24157-24163
    • (1996) J Biol Chem , vol.271 , pp. 24157-24163
    • Yu, C.1    Kennedy, N.J.2    Chang, C.C.3    Rothblatt, J.A.4
  • 81
    • 3242790123 scopus 로고    scopus 로고
    • Dynamics of neutral lipid storage in yeast
    • Müllner H., and Daum G. Dynamics of neutral lipid storage in yeast. Acta Biochim Pol 51 (2004) 323-347
    • (2004) Acta Biochim Pol , vol.51 , pp. 323-347
    • Müllner, H.1    Daum, G.2
  • 83
    • 0034879653 scopus 로고    scopus 로고
    • Transcriptional regulation of the two sterol esterification genes in the yeast Saccharomyces cerevisiae
    • Jensen-Pergakes K., Guo Z., Giattina M., Sturley S.L., and Bard M. Transcriptional regulation of the two sterol esterification genes in the yeast Saccharomyces cerevisiae. J Bacteriol 183 (2001) 4950-4957
    • (2001) J Bacteriol , vol.183 , pp. 4950-4957
    • Jensen-Pergakes, K.1    Guo, Z.2    Giattina, M.3    Sturley, S.L.4    Bard, M.5
  • 84
    • 0033974053 scopus 로고    scopus 로고
    • Contribution of Are1p and Are2p to steryl ester synthesis in the yeast Saccharomyces cerevisiae
    • Zweytick D., Leitner E., Kohlwein S.D., Yu C., Rothblatt J., and Daum G. Contribution of Are1p and Are2p to steryl ester synthesis in the yeast Saccharomyces cerevisiae. Eur J Biochem 267 (2000) 1075-1082
    • (2000) Eur J Biochem , vol.267 , pp. 1075-1082
    • Zweytick, D.1    Leitner, E.2    Kohlwein, S.D.3    Yu, C.4    Rothblatt, J.5    Daum, G.6
  • 85
    • 0033489962 scopus 로고    scopus 로고
    • Enhanced sterol-acyl transferase activity promotes sterol accumulation in Saccharomyces cerevisiae
    • Polakowski T., Bastl R., Stahl U., and Lang C. Enhanced sterol-acyl transferase activity promotes sterol accumulation in Saccharomyces cerevisiae. Appl Microbiol Biotechnol 53 (1999) 30-35
    • (1999) Appl Microbiol Biotechnol , vol.53 , pp. 30-35
    • Polakowski, T.1    Bastl, R.2    Stahl, U.3    Lang, C.4
  • 86
    • 0027205567 scopus 로고
    • The structural requirements of sterols for membrane function in Saccharomyces cerevisiae
    • Nes W.D., Janssen G.G., Crumley F.G., Kalinowska M., and Akihisa T. The structural requirements of sterols for membrane function in Saccharomyces cerevisiae. Arch Biochem Biophys 300 (1993) 724-733
    • (1993) Arch Biochem Biophys , vol.300 , pp. 724-733
    • Nes, W.D.1    Janssen, G.G.2    Crumley, F.G.3    Kalinowska, M.4    Akihisa, T.5
  • 87
    • 0037005998 scopus 로고    scopus 로고
    • Heme-regulated expression of two yeast acyl-CoA:sterol acyltransferases is involved in the specific response of sterol esterification to anaerobiosis
    • Valachovic M., Klobucnikova V., Griac P., and Hapala I. Heme-regulated expression of two yeast acyl-CoA:sterol acyltransferases is involved in the specific response of sterol esterification to anaerobiosis. FEMS Microbiol Lett 206 (2002) 121-125
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 121-125
    • Valachovic, M.1    Klobucnikova, V.2    Griac, P.3    Hapala, I.4
  • 88
    • 0030603150 scopus 로고    scopus 로고
    • Positive and negative regulation of a sterol biosynthetic gene (ERG3) in the post-squalene portion of the yeast ergosterol pathway
    • Arthington-Skaggs B.A., Crowell D.N., Yang H., Sturley S.L., and Bard M. Positive and negative regulation of a sterol biosynthetic gene (ERG3) in the post-squalene portion of the yeast ergosterol pathway. FEBS Lett 392 (1996) 155-161
    • (1996) FEBS Lett , vol.392 , pp. 155-161
    • Arthington-Skaggs, B.A.1    Crowell, D.N.2    Yang, H.3    Sturley, S.L.4    Bard, M.5
  • 89
    • 23344435534 scopus 로고    scopus 로고
    • Dual activators of the sterol biosynthetic pathway of Saccharomyces cerevisiae: similar activation/regulatory domains but different response mechanisms
    • Davies B.S.J., Wang H.S., and Rine J. Dual activators of the sterol biosynthetic pathway of Saccharomyces cerevisiae: similar activation/regulatory domains but different response mechanisms. Mol Cell Biol 25 (2005) 7375-7385
    • (2005) Mol Cell Biol , vol.25 , pp. 7375-7385
    • Davies, B.S.J.1    Wang, H.S.2    Rine, J.3
  • 90
    • 0031931498 scopus 로고    scopus 로고
    • Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles
    • Leber R., Landl K., Zinser E., Ahorn H., Spök A., Kohlwein S.D., et al. Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles. Mol Biol Cell 9 (1998) 375-386
    • (1998) Mol Biol Cell , vol.9 , pp. 375-386
    • Leber, R.1    Landl, K.2    Zinser, E.3    Ahorn, H.4    Spök, A.5    Kohlwein, S.D.6
  • 91
    • 0024803720 scopus 로고
    • Regulation of squalene synthetase and squalene epoxidase activities in Saccharomyces cerevisiae
    • M'Baya B., Fegueur M., Servouse M., and Karst F. Regulation of squalene synthetase and squalene epoxidase activities in Saccharomyces cerevisiae. Lipids 24 (1989) 1020-1023
    • (1989) Lipids , vol.24 , pp. 1020-1023
    • M'Baya, B.1    Fegueur, M.2    Servouse, M.3    Karst, F.4
  • 92
    • 0035956912 scopus 로고    scopus 로고
    • Supernatant protein factor, which stimulates the conversion of squalene to lanosterol, is a cytosolic squalene transfer protein and enhances cholesterol biosynthesis
    • Shibata N., Arita M., Misaki Y., Dohmae N., Takio K., Ono T., et al. Supernatant protein factor, which stimulates the conversion of squalene to lanosterol, is a cytosolic squalene transfer protein and enhances cholesterol biosynthesis. Proc Natl Acad Sci USA 98 (2001) 2244-2249
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2244-2249
    • Shibata, N.1    Arita, M.2    Misaki, Y.3    Dohmae, N.4    Takio, K.5    Ono, T.6
  • 93
    • 0034731399 scopus 로고    scopus 로고
    • Mutations in yeast ARV1 alter intracellular sterol distribution and are complemented by human ARV1
    • Tinkelenberg A.H., Liu Y., Alcantara F., Khan S., Guo Z., Bard M., et al. Mutations in yeast ARV1 alter intracellular sterol distribution and are complemented by human ARV1. J Biol Chem 275 (2000) 40667-40670
    • (2000) J Biol Chem , vol.275 , pp. 40667-40670
    • Tinkelenberg, A.H.1    Liu, Y.2    Alcantara, F.3    Khan, S.4    Guo, Z.5    Bard, M.6
  • 94
    • 0037183971 scopus 로고    scopus 로고
    • Yeast cells lacking the ARV1 gene harbor defects in sphingolipid metabolism. Complementation by human ARV1
    • Swain E., Stukey J., McDonough V., Germann M., Liu Y., Sturley S.L., et al. Yeast cells lacking the ARV1 gene harbor defects in sphingolipid metabolism. Complementation by human ARV1. J Biol Chem 277 (2002) 36152-36160
    • (2002) J Biol Chem , vol.277 , pp. 36152-36160
    • Swain, E.1    Stukey, J.2    McDonough, V.3    Germann, M.4    Liu, Y.5    Sturley, S.L.6
  • 95
    • 33947206157 scopus 로고    scopus 로고
    • Synthesis, storage and degradation of neutral lipids in yeast
    • Czabany T., Athenstaedt K., and Daum G. Synthesis, storage and degradation of neutral lipids in yeast. Biochim Biophys Acta 1771 (2007) 299-309
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 299-309
    • Czabany, T.1    Athenstaedt, K.2    Daum, G.3
  • 96
    • 33745307534 scopus 로고    scopus 로고
    • The life cycle of neutral lipids: synthesis, storage and degradation
    • Athenstaedt K., and Daum G. The life cycle of neutral lipids: synthesis, storage and degradation. Cell Mol Life Sci 63 (2006) 1355-1369
    • (2006) Cell Mol Life Sci , vol.63 , pp. 1355-1369
    • Athenstaedt, K.1    Daum, G.2
  • 97
    • 33846501577 scopus 로고    scopus 로고
    • Dynamics of neutral lipid storage and mobilization in yeast
    • Daum G., Wagner A., Czabany T., and Athenstaedt K. Dynamics of neutral lipid storage and mobilization in yeast. Biochimie 89 (2007) 243-248
    • (2007) Biochimie , vol.89 , pp. 243-248
    • Daum, G.1    Wagner, A.2    Czabany, T.3    Athenstaedt, K.4
  • 98
    • 84989092697 scopus 로고
    • Oleosomes (lipid bodies) in nitrogen-fixing peanut nodules
    • Jayaram S., and Bal A.K. Oleosomes (lipid bodies) in nitrogen-fixing peanut nodules. Plant Cell Environ 14 (1991) 195-203
    • (1991) Plant Cell Environ , vol.14 , pp. 195-203
    • Jayaram, S.1    Bal, A.K.2
  • 99
    • 0029871347 scopus 로고    scopus 로고
    • PCR-synthesis of marker cassettes with long flanking homology regions for gene disruption in S. cerevisiae
    • Wach A. PCR-synthesis of marker cassettes with long flanking homology regions for gene disruption in S. cerevisiae. Yeast 12 (1996) 259-265
    • (1996) Yeast , vol.12 , pp. 259-265
    • Wach, A.1
  • 100
    • 0025772167 scopus 로고
    • Perilipin, a major hormonally regulated adipocyte-specific phosphoprotein associated with the periphery of lipid storage droplets
    • Greenberg A.S., Egan J.J., Wek S.A., Garty N.B., Blanchette-Mackie E.J., and Londos C. Perilipin, a major hormonally regulated adipocyte-specific phosphoprotein associated with the periphery of lipid storage droplets. J Biol Chem 266 (1991) 11341-11346
    • (1991) J Biol Chem , vol.266 , pp. 11341-11346
    • Greenberg, A.S.1    Egan, J.J.2    Wek, S.A.3    Garty, N.B.4    Blanchette-Mackie, E.J.5    Londos, C.6
  • 101
    • 1642565185 scopus 로고    scopus 로고
    • Identification of major proteins in the lipid droplet-enriched fraction isolated from the human hepatocyte cell line HuH7
    • Fujimoto Y., Itabe H., Sakai J., Makita M., Noda J., Mori M., et al. Identification of major proteins in the lipid droplet-enriched fraction isolated from the human hepatocyte cell line HuH7. Biochim Biophys Acta 1644 (2004) 47-59
    • (2004) Biochim Biophys Acta , vol.1644 , pp. 47-59
    • Fujimoto, Y.1    Itabe, H.2    Sakai, J.3    Makita, M.4    Noda, J.5    Mori, M.6
  • 102
    • 0024987957 scopus 로고
    • Oleosin KD 18 on the surface of oil bodies in maize. Genomic and cDNA sequences and the deduced protein structure
    • Qu R.D., and Huang A.H. Oleosin KD 18 on the surface of oil bodies in maize. Genomic and cDNA sequences and the deduced protein structure. J Biol Chem 265 (1990) 2238-2243
    • (1990) J Biol Chem , vol.265 , pp. 2238-2243
    • Qu, R.D.1    Huang, A.H.2
  • 103
    • 34248189053 scopus 로고    scopus 로고
    • CGI-58 facilitates lipolysis on lipid droplets but is not involved in the vesiculation of lipid droplets caused by hormonal stimulation
    • Yamaguchi T., Omatsu N., Morimoto E., Nakashima H., Ueno K., Tanaka T., et al. CGI-58 facilitates lipolysis on lipid droplets but is not involved in the vesiculation of lipid droplets caused by hormonal stimulation. J Lipid Res 48 (2007) 1078-1089
    • (2007) J Lipid Res , vol.48 , pp. 1078-1089
    • Yamaguchi, T.1    Omatsu, N.2    Morimoto, E.3    Nakashima, H.4    Ueno, K.5    Tanaka, T.6
  • 104
    • 4744341229 scopus 로고    scopus 로고
    • Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in 3T3-L1 adipocytes
    • Subramanian V., Rothenberg A., Gomez C., Cohen A.W., Garcia A., Bhattacharyya S., et al. Perilipin A mediates the reversible binding of CGI-58 to lipid droplets in 3T3-L1 adipocytes. J Biol Chem 279 (2004) 42062-42071
    • (2004) J Biol Chem , vol.279 , pp. 42062-42071
    • Subramanian, V.1    Rothenberg, A.2    Gomez, C.3    Cohen, A.W.4    Garcia, A.5    Bhattacharyya, S.6
  • 105
    • 3142738035 scopus 로고    scopus 로고
    • CGI-58 interacts with perilipin and is localized to lipid droplets: possible involvement of CGI-58 mislocalization in chanarin-dorfman syndrome
    • Yamaguchi T., Omatsu N., Matsushita S., and Osumi T. CGI-58 interacts with perilipin and is localized to lipid droplets: possible involvement of CGI-58 mislocalization in chanarin-dorfman syndrome. J Biol Chem 279 (2004) 30490-30497
    • (2004) J Biol Chem , vol.279 , pp. 30490-30497
    • Yamaguchi, T.1    Omatsu, N.2    Matsushita, S.3    Osumi, T.4
  • 106
    • 0034764272 scopus 로고    scopus 로고
    • Mutations in CGI-58, the gene encoding a new protein of the esterase/lipase/thioesterase subfamily, in chanarin-dorfman syndrome
    • Lefevre C., Jobard F., Caux F., Bouadjar B., Karaduman A., Heilig R., et al. Mutations in CGI-58, the gene encoding a new protein of the esterase/lipase/thioesterase subfamily, in chanarin-dorfman syndrome. Am J Hum Genet 69 (2001) 1002-1012
    • (2001) Am J Hum Genet , vol.69 , pp. 1002-1012
    • Lefevre, C.1    Jobard, F.2    Caux, F.3    Bouadjar, B.4    Karaduman, A.5    Heilig, R.6
  • 107
    • 0017239547 scopus 로고
    • Receptor-mediated control of cholesterol metabolism
    • Brown M.S., and Goldstein J.L. Receptor-mediated control of cholesterol metabolism. Science 191 (1976) 150-154
    • (1976) Science , vol.191 , pp. 150-154
    • Brown, M.S.1    Goldstein, J.L.2
  • 108
    • 0016612281 scopus 로고
    • Role of the low density lipoprotein receptor in regulating the content of free and esterified cholesterol in human fibroblasts
    • Brown M.S., Faust J.R., and Goldstein J.L. Role of the low density lipoprotein receptor in regulating the content of free and esterified cholesterol in human fibroblasts. J Clin Invest 55 (1975) 783-793
    • (1975) J Clin Invest , vol.55 , pp. 783-793
    • Brown, M.S.1    Faust, J.R.2    Goldstein, J.L.3
  • 110
    • 0028081336 scopus 로고
    • Characterization of lipid particles of the yeast Saccharomyces cerevisiae
    • Leber R., Zinser E., Zellnig G., Paltauf F., and Daum G. Characterization of lipid particles of the yeast Saccharomyces cerevisiae. Yeast 10 (1994) 1421-1428
    • (1994) Yeast , vol.10 , pp. 1421-1428
    • Leber, R.1    Zinser, E.2    Zellnig, G.3    Paltauf, F.4    Daum, G.5
  • 112
    • 33751161853 scopus 로고    scopus 로고
    • Adipophilin-enriched domains in the endoplasmic reticulum membrane are sites of lipid droplet biogenesis
    • Robenek H., Hofnagel O., Buers I., Robenek M.J., Troyer D., and Severs N.J. Adipophilin-enriched domains in the endoplasmic reticulum membrane are sites of lipid droplet biogenesis. J Cell Sci 119 (2006) 4215-4224
    • (2006) J Cell Sci , vol.119 , pp. 4215-4224
    • Robenek, H.1    Hofnagel, O.2    Buers, I.3    Robenek, M.J.4    Troyer, D.5    Severs, N.J.6
  • 113
    • 0019303464 scopus 로고
    • Transport of lipid across capillary endothelium
    • Scow R.O., Blanchette-Mackie E.J., and Smith L.C. Transport of lipid across capillary endothelium. Fed Proc 39 (1980) 2610-2617
    • (1980) Fed Proc , vol.39 , pp. 2610-2617
    • Scow, R.O.1    Blanchette-Mackie, E.J.2    Smith, L.C.3
  • 114
    • 2342510295 scopus 로고    scopus 로고
    • Role of Caveolin-1 in the modulation of lipolysis and lipid droplet formation
    • Cohen A.W., Razani B., Schubert W., Williams T.M., Wang X.B., Iyengar P., et al. Role of Caveolin-1 in the modulation of lipolysis and lipid droplet formation. Diabetes 53 (2004) 1261-1270
    • (2004) Diabetes , vol.53 , pp. 1261-1270
    • Cohen, A.W.1    Razani, B.2    Schubert, W.3    Williams, T.M.4    Wang, X.B.5    Iyengar, P.6
  • 116
    • 34547216748 scopus 로고    scopus 로고
    • A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum
    • Ploegh H.L. A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum. Nature 448 (2007) 435-437
    • (2007) Nature , vol.448 , pp. 435-437
    • Ploegh, H.L.1
  • 117
    • 34548514866 scopus 로고    scopus 로고
    • Proteins under new management: lipid droplets deliver
    • Welte M.A. Proteins under new management: lipid droplets deliver. Trends Cell Biol 17 (2007) 363-369
    • (2007) Trends Cell Biol , vol.17 , pp. 363-369
    • Welte, M.A.1
  • 118
    • 2442601576 scopus 로고    scopus 로고
    • Targeting of proteins involved in sterol biosynthesis to lipid particles of the yeast Saccharomyces cerevisiae
    • Müllner H., Zweytick D., Leber R., Turnowsky F., and Daum G. Targeting of proteins involved in sterol biosynthesis to lipid particles of the yeast Saccharomyces cerevisiae. Biochim Biophys Acta 1663 (2004) 9-13
    • (2004) Biochim Biophys Acta , vol.1663 , pp. 9-13
    • Müllner, H.1    Zweytick, D.2    Leber, R.3    Turnowsky, F.4    Daum, G.5
  • 120
    • 0027984281 scopus 로고
    • Saccharomyces cerevisiae contains four fatty acid activation (FAA) genes: an assessment of their role in regulating protein N-myristoylation and cellular lipid metabolism
    • Johnson D.R., Knoll L.J., Levin D.E., and Gordon J.I. Saccharomyces cerevisiae contains four fatty acid activation (FAA) genes: an assessment of their role in regulating protein N-myristoylation and cellular lipid metabolism. J Cell Biol 127 (1994) 751-762
    • (1994) J Cell Biol , vol.127 , pp. 751-762
    • Johnson, D.R.1    Knoll, L.J.2    Levin, D.E.3    Gordon, J.I.4
  • 121
    • 0037931415 scopus 로고    scopus 로고
    • YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid particles of Saccharomyces cerevisiae
    • Athenstaedt K., and Daum G. YMR313c/TGL3 encodes a novel triacylglycerol lipase located in lipid particles of Saccharomyces cerevisiae. J Biol Chem 278 (2003) 23317-23323
    • (2003) J Biol Chem , vol.278 , pp. 23317-23323
    • Athenstaedt, K.1    Daum, G.2
  • 122
    • 33644853354 scopus 로고    scopus 로고
    • Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast
    • Kurat C.F., Natter K., Petschnigg J., Wolinski H., Scheuringer K., Scholz H., et al. Obese yeast: triglyceride lipolysis is functionally conserved from mammals to yeast. J Biol Chem 281 (2005) 491-500
    • (2005) J Biol Chem , vol.281 , pp. 491-500
    • Kurat, C.F.1    Natter, K.2    Petschnigg, J.3    Wolinski, H.4    Scheuringer, K.5    Scholz, H.6
  • 124
    • 27844486104 scopus 로고    scopus 로고
    • Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles
    • Athenstaedt K., and Daum G. Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles. J Biol Chem 280 (2005) 37301-37309
    • (2005) J Biol Chem , vol.280 , pp. 37301-37309
    • Athenstaedt, K.1    Daum, G.2
  • 125
    • 0027231368 scopus 로고
    • Sterol composition of yeast organelle membranes and subcellular distribution of enzymes involved in sterol metabolism
    • Zinser E., Paltauf F., and Daum G. Sterol composition of yeast organelle membranes and subcellular distribution of enzymes involved in sterol metabolism. J Bacteriol 175 (1993) 2853-2858
    • (1993) J Bacteriol , vol.175 , pp. 2853-2858
    • Zinser, E.1    Paltauf, F.2    Daum, G.3
  • 126
    • 0025057072 scopus 로고    scopus 로고
    • A serine protease triad forms the catalytic centre of a triacylglycerol lipase
    • Brady L., Brzozowski A.M., Derewenda Z.S., Dodson E., Dodson G., Tolley S., et al. A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 343 (1999) 767-770
    • (1999) Nature , vol.343 , pp. 767-770
    • Brady, L.1    Brzozowski, A.M.2    Derewenda, Z.S.3    Dodson, E.4    Dodson, G.5    Tolley, S.6
  • 128
    • 0030874881 scopus 로고    scopus 로고
    • Lipases and alpha/beta hydrolase fold
    • Schrag J.D., and Cygler M. Lipases and alpha/beta hydrolase fold. Method Enzymol 284 (1997) 85-107
    • (1997) Method Enzymol , vol.284 , pp. 85-107
    • Schrag, J.D.1    Cygler, M.2
  • 130
    • 33646842826 scopus 로고    scopus 로고
    • SUGAR-DEPENDENT1 encodes a patatin domain triacylglycerol lipase that initiates storage oil breakdown in germinating Arabidopsis seeds
    • Eastmond P.J. SUGAR-DEPENDENT1 encodes a patatin domain triacylglycerol lipase that initiates storage oil breakdown in germinating Arabidopsis seeds. Plant Cell 18 (2006) 665-675
    • (2006) Plant Cell , vol.18 , pp. 665-675
    • Eastmond, P.J.1
  • 132
    • 85047685160 scopus 로고    scopus 로고
    • Identification, purification, and characterization of a thermally stable lipase from rice bran. A new member of the (phospho)lipase family
    • Bhardwaj K., Raju A., and Rajasekharan R. Identification, purification, and characterization of a thermally stable lipase from rice bran. A new member of the (phospho)lipase family. Plant Physiol 127 (2001) 1728-1738
    • (2001) Plant Physiol , vol.127 , pp. 1728-1738
    • Bhardwaj, K.1    Raju, A.2    Rajasekharan, R.3
  • 133
    • 0016221254 scopus 로고
    • Inositol phosphorylceramide, a novel substance and the chief member of a major group of yeast sphingolipids containing a single inositol phosphate
    • Smith S.W., and Lester R.L. Inositol phosphorylceramide, a novel substance and the chief member of a major group of yeast sphingolipids containing a single inositol phosphate. J Biol Chem 249 (1974) 3395-3405
    • (1974) J Biol Chem , vol.249 , pp. 3395-3405
    • Smith, S.W.1    Lester, R.L.2
  • 134
    • 0030878240 scopus 로고    scopus 로고
    • ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation
    • Oh C.S., Toke D.A., Mandala S., and Martin C.E. ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J Biol Chem 272 (1997) 17376-17384
    • (1997) J Biol Chem , vol.272 , pp. 17376-17384
    • Oh, C.S.1    Toke, D.A.2    Mandala, S.3    Martin, C.E.4
  • 135
    • 2642589009 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae TGL2 gene encodes a protein with lipolytic activity and can complement an Escherichia coli diacylglycerol kinase disruptant
    • Van Heusden G.P., Nebohâcovâ M., Overbeeke T.L., and Steensma H.Y. The Saccharomyces cerevisiae TGL2 gene encodes a protein with lipolytic activity and can complement an Escherichia coli diacylglycerol kinase disruptant. Yeast 14 (1998) 225-232
    • (1998) Yeast , vol.14 , pp. 225-232
    • Van Heusden, G.P.1    Nebohâcovâ, M.2    Overbeeke, T.L.3    Steensma, H.Y.4
  • 136
    • 0019162068 scopus 로고
    • The cholesteryl ester cycle in macrophage foam cells. Continual hydrolysis and re-esterification of cytoplasmic cholesteryl esters
    • Brown M.S., Ho Y.K., and Goldstein J.L. The cholesteryl ester cycle in macrophage foam cells. Continual hydrolysis and re-esterification of cytoplasmic cholesteryl esters. J Biol Chem 255 (1980) 9344-9352
    • (1980) J Biol Chem , vol.255 , pp. 9344-9352
    • Brown, M.S.1    Ho, Y.K.2    Goldstein, J.L.3
  • 137
    • 0017822390 scopus 로고
    • Characterization of sterol-ester hydrolase in Saccharomyces cerevisiae
    • Taketani S., Osumi T., and Katsuki H. Characterization of sterol-ester hydrolase in Saccharomyces cerevisiae. Biochim Biophys Acta 525 (1978) 87-92
    • (1978) Biochim Biophys Acta , vol.525 , pp. 87-92
    • Taketani, S.1    Osumi, T.2    Katsuki, H.3
  • 138
    • 17144404154 scopus 로고    scopus 로고
    • YEH2/YLR020c encodes a novel steryl ester hydrolase of the yeast Saccharomyces cerevisiae
    • Müllner H., Deutsch G., Leitner E., Ingolic E., and Daum G. YEH2/YLR020c encodes a novel steryl ester hydrolase of the yeast Saccharomyces cerevisiae. J Biol Chem 280 (2005) 13321-13328
    • (2005) J Biol Chem , vol.280 , pp. 13321-13328
    • Müllner, H.1    Deutsch, G.2    Leitner, E.3    Ingolic, E.4    Daum, G.5
  • 139
    • 14044272811 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae YLL012/YEH1, YLR020/YEH2, and TGL1 genes encode a novel family of membrane-anchored lipases that are required for steryl ester hydrolysis
    • Köffel R., Tiwari R., Falquet L., and Schneiter R. The Saccharomyces cerevisiae YLL012/YEH1, YLR020/YEH2, and TGL1 genes encode a novel family of membrane-anchored lipases that are required for steryl ester hydrolysis. Mol Cell Biol 25 (2005) 1655-1668
    • (2005) Mol Cell Biol , vol.25 , pp. 1655-1668
    • Köffel, R.1    Tiwari, R.2    Falquet, L.3    Schneiter, R.4
  • 140
    • 20444465269 scopus 로고    scopus 로고
    • The lipid droplet enzyme Tgl1p hydrolyzes both steryl esters and triglycerides in the yeast, Saccharomyces cerevisiae
    • Jandrositz A., Petschnigg J., Zimmermann R., Natter K., Scholze H., Hermetter A., et al. The lipid droplet enzyme Tgl1p hydrolyzes both steryl esters and triglycerides in the yeast, Saccharomyces cerevisiae. Biochim Biophys Acta 1735 (2005) 50-58
    • (2005) Biochim Biophys Acta , vol.1735 , pp. 50-58
    • Jandrositz, A.1    Petschnigg, J.2    Zimmermann, R.3    Natter, K.4    Scholze, H.5    Hermetter, A.6
  • 141
    • 33746268567 scopus 로고    scopus 로고
    • Yeh1 constitutes the major steryl ester hydrolase under heme-deficient conditions in Saccharomyces cerevisiae
    • Köffel R., and Schneiter R. Yeh1 constitutes the major steryl ester hydrolase under heme-deficient conditions in Saccharomyces cerevisiae. Eukaryot Cell 5 (2006) 1018-1025
    • (2006) Eukaryot Cell , vol.5 , pp. 1018-1025
    • Köffel, R.1    Schneiter, R.2


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