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Volumn 180, Issue , 2014, Pages 23-43

The response to inositol: Regulation of glycerolipid metabolism and stress response signaling in yeast

Author keywords

Glycerolipids; Inositol; Phosphatidic acid; Phosphatidylinositol; Sphingolipids; Stress response

Indexed keywords

CHOLINE; CYTIDINE DIPHOSPHATE; CYTIDINE DIPHOSPHATE DIACYLGLYCEROL INOSITOL 3 PHOSPHATIDYLTRANSFERASE; DIACYLGLYCEROL; FUNGAL ENZYME; GLYCEROLIPID; INOSITOL; MITOGEN ACTIVATED PROTEIN KINASE; MYOINOSITOL 1 PHOSPHATE SYNTHASE; PHOSPHATIDYLINOSITIDE; PROTEIN KINASE C; SPHINGOLIPID; TRANSCRIPTION FACTOR; TRIACYLGLYCEROL;

EID: 84897989500     PISSN: 00093084     EISSN: 18732941     Source Type: Journal    
DOI: 10.1016/j.chemphyslip.2013.12.013     Document Type: Review
Times cited : (76)

References (277)
  • 1
    • 0036923691 scopus 로고    scopus 로고
    • Regulation of subtelomeric silencing during stress response
    • W. Ai, P.G. Bertram, C.K. Tsang, T.F. Chan, and X.F. Zheng Regulation of subtelomeric silencing during stress response Mol. Cell 10 2002 1295 1305
    • (2002) Mol. Cell , vol.10 , pp. 1295-1305
    • Ai, W.1    Bertram, P.G.2    Tsang, C.K.3    Chan, T.F.4    Zheng, X.F.5
  • 2
    • 13444283465 scopus 로고    scopus 로고
    • Simulation and validation of modelled sphingolipid metabolism in Saccharomyces cerevisiae
    • F. Alvarez-Vasquez, K.J. Sims, L.A. Cowart, Y. Okamoto, E.O. Voit, and Y.A. Hannun Simulation and validation of modelled sphingolipid metabolism in Saccharomyces cerevisiae Nature 433 2005 425 430
    • (2005) Nature , vol.433 , pp. 425-430
    • Alvarez-Vasquez, F.1    Sims, K.J.2    Cowart, L.A.3    Okamoto, Y.4    Voit, E.O.5    Hannun, Y.A.6
  • 3
    • 0028084338 scopus 로고
    • Myc-Max-Mad: A transcription factor network controlling cell cycle progression, differentiation and death
    • B. Amati, and H. Land Myc-Max-Mad: a transcription factor network controlling cell cycle progression, differentiation and death Curr. Opin. Genet. Dev. 4 1994 102 108
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 102-108
    • Amati, B.1    Land, H.2
  • 4
    • 0028363566 scopus 로고
    • INO2 and INO4 gene products, positive regulators of phospholipid biosynthesis in Saccharomyces cerevisiae, form a complex that binds to the INO1 promoter
    • J. Ambroziak, and S.A. Henry INO2 and INO4 gene products, positive regulators of phospholipid biosynthesis in Saccharomyces cerevisiae, form a complex that binds to the INO1 promoter J. Biol. Chem. 269 1994 15344 15349
    • (1994) J. Biol. Chem. , vol.269 , pp. 15344-15349
    • Ambroziak, J.1    Henry, S.A.2
  • 5
    • 0029974122 scopus 로고    scopus 로고
    • Carbon source regulation of PIS1 gene expression in Saccharomyces cerevisiae involves the MCM1 gene and the two-component regulatory gene, SLN1
    • M.S. Anderson, and J.M. Lopes Carbon source regulation of PIS1 gene expression in Saccharomyces cerevisiae involves the MCM1 gene and the two-component regulatory gene, SLN1 J. Biol. Chem. 271 1996 26596 26601
    • (1996) J. Biol. Chem. , vol.271 , pp. 26596-26601
    • Anderson, M.S.1    Lopes, J.M.2
  • 6
    • 0028876869 scopus 로고
    • Autoregulated expression of the yeast INO2 and INO4 helix-loop-helix activator genes effects cooperative regulation on their target genes
    • B.P. Ashburner, and J.M. Lopes Autoregulated expression of the yeast INO2 and INO4 helix-loop-helix activator genes effects cooperative regulation on their target genes Mol. Cell. Biol. 15 1995 1709 1715
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1709-1715
    • Ashburner, B.P.1    Lopes, J.M.2
  • 7
    • 0028826137 scopus 로고
    • Regulation of yeast phospholipid biosynthetic gene expression in response to inositol involves two superimposed mechanisms
    • B.P. Ashburner, and J.M. Lopes Regulation of yeast phospholipid biosynthetic gene expression in response to inositol involves two superimposed mechanisms Proc. Natl. Acad. Sci. U.S.A. 92 1995 9722 9726
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9722-9726
    • Ashburner, B.P.1    Lopes, J.M.2
  • 8
    • 27844486104 scopus 로고    scopus 로고
    • Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces cerevisiae are localized to lipid particles
    • K. Athenstaedt, and G. Daum 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
  • 9
    • 0018940962 scopus 로고
    • Yeast mutant defective in phosphatidylserine synthesis
    • K. Atkinson, S. Fogel, and S.A. Henry Yeast mutant defective in phosphatidylserine synthesis J. Biol. Chem. 255 1980 6653 6661
    • (1980) J. Biol. Chem. , vol.255 , pp. 6653-6661
    • Atkinson, K.1    Fogel, S.2    Henry, S.A.3
  • 11
    • 0017763336 scopus 로고
    • Osmotic imbalance in inositol-starved spheroplasts of Saccharomyces cerevisiae
    • K.D. Atkinson, A.I. Kolat, and S.A. Henry Osmotic imbalance in inositol-starved spheroplasts of Saccharomyces cerevisiae J. Bacteriol. 132 1977 806 817
    • (1977) J. Bacteriol. , vol.132 , pp. 806-817
    • Atkinson, K.D.1    Kolat, A.I.2    Henry, S.A.3
  • 12
    • 0036001334 scopus 로고    scopus 로고
    • Stt4 PI 4-kinase localizes to the plasma membrane and functions in the Pkc1-mediated MAP kinase cascade
    • A. Audhya, and S.D. Emr Stt4 PI 4-kinase localizes to the plasma membrane and functions in the Pkc1-mediated MAP kinase cascade Dev. Cell 2 2002 593 605
    • (2002) Dev. Cell , vol.2 , pp. 593-605
    • Audhya, A.1    Emr, S.D.2
  • 13
    • 0028851909 scopus 로고
    • Functional characterization of an inositol-sensitive upstream activation sequence in yeast. A cis-regulatory element responsible for inositol-choline mediated regulation of phospholipid biosynthesis
    • N. Bachhawat, Q. Ouyang, and S.A. Henry Functional characterization of an inositol-sensitive upstream activation sequence in yeast. A cis-regulatory element responsible for inositol-choline mediated regulation of phospholipid biosynthesis J. Biol. Chem. 270 1995 25087 25095
    • (1995) J. Biol. Chem. , vol.270 , pp. 25087-25095
    • Bachhawat, N.1    Ouyang, Q.2    Henry, S.A.3
  • 14
    • 0026607356 scopus 로고
    • Cis and trans regulatory elements required for regulation of the CHO1 gene of Saccharomyces cerevisiae
    • A.M. Bailis, J.M. Lopes, S.D. Kohlwein, and S.A. Henry Cis and trans regulatory elements required for regulation of the CHO1 gene of Saccharomyces cerevisiae Nucleic Acids Res. 20 1992 1411 1418
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1411-1418
    • Bailis, A.M.1    Lopes, J.M.2    Kohlwein, S.D.3    Henry, S.A.4
  • 15
    • 0023073676 scopus 로고
    • The membrane-associated enzyme phosphatidylserine synthase is regulated at the level of mRNA abundance
    • A.M. Bailis, M.A. Poole, G.M. Carman, and S.A. Henry The membrane-associated enzyme phosphatidylserine synthase is regulated at the level of mRNA abundance Mol. Cell. Biol. 7 1987 167 176
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 167-176
    • Bailis, A.M.1    Poole, M.A.2    Carman, G.M.3    Henry, S.A.4
  • 16
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function
    • V.A. Bankaitis, J.R. Aitken, A.E. Cleves, and W. Dowhan An essential role for a phospholipid transfer protein in yeast Golgi function Nature 347 1990 561 562
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.A.1    Aitken, J.R.2    Cleves, A.E.3    Dowhan, W.4
  • 17
    • 0024518932 scopus 로고
    • The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex
    • V.A. Bankaitis, D.E. Malehorn, S.D. Emr, and R. Greene The Saccharomyces cerevisiae SEC14 gene encodes a cytosolic factor that is required for transport of secretory proteins from the yeast Golgi complex J. Cell Biol. 108 1989 1271 1281
    • (1989) J. Cell Biol. , vol.108 , pp. 1271-1281
    • Bankaitis, V.A.1    Malehorn, D.E.2    Emr, S.D.3    Greene, R.4
  • 18
    • 28444461398 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae
    • V.A. Bankaitis, S. Phillips, L. Yanagisawa, X. Li, S. Routt, and Z. Xie Phosphatidylinositol transfer protein function in the yeast Saccharomyces cerevisiae Adv. Enzyme Regul. 45 2005 155 170
    • (2005) Adv. Enzyme Regul. , vol.45 , pp. 155-170
    • Bankaitis, V.A.1    Phillips, S.2    Yanagisawa, L.3    Li, X.4    Routt, S.5    Xie, Z.6
  • 19
    • 0017688609 scopus 로고
    • Changes in phospholipids of Saccharomyces cerevisiae associated with inositol-less death
    • G.W. Becker, and R.L. Lester Changes in phospholipids of Saccharomyces cerevisiae associated with inositol-less death J. Biol. Chem. 252 1977 8684 8691
    • (1977) J. Biol. Chem. , vol.252 , pp. 8684-8691
    • Becker, G.W.1    Lester, R.L.2
  • 20
    • 0028115840 scopus 로고
    • The sua8 suppressors of Saccharomyces cerevisiae encode replacements of conserved residues within the largest subunit of RNA polymerase II and affect transcription start site selection similarly to sua7 (TFIIB) mutations
    • R.W. Berroteran, D.E. Ware, and M. Hampsey The sua8 suppressors of Saccharomyces cerevisiae encode replacements of conserved residues within the largest subunit of RNA polymerase II and affect transcription start site selection similarly to sua7 (TFIIB) mutations Mol. Cell. Biol. 14 1994 226 237
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 226-237
    • Berroteran, R.W.1    Ware, D.E.2    Hampsey, M.3
  • 21
    • 0036460783 scopus 로고    scopus 로고
    • Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism
    • J.L. Betz, M. Chang, T.M. Washburn, S.E. Porter, C.L. Mueller, and J.A. Jaehning Phenotypic analysis of Paf1/RNA polymerase II complex mutations reveals connections to cell cycle regulation, protein synthesis, and lipid and nucleic acid metabolism Mol. Genet. Genomics 268 2002 272 285
    • (2002) Mol. Genet. Genomics , vol.268 , pp. 272-285
    • Betz, J.L.1    Chang, M.2    Washburn, T.M.3    Porter, S.E.4    Mueller, C.L.5    Jaehning, J.A.6
  • 22
    • 44349186331 scopus 로고    scopus 로고
    • Influence of genotype and nutrition on survival and metabolism of starving yeast
    • V.M. Boer, S. Amini, and D. Botstein Influence of genotype and nutrition on survival and metabolism of starving yeast Proc. Natl. Acad. Sci. U.S.A. 105 2008 6930 6935
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6930-6935
    • Boer, V.M.1    Amini, S.2    Botstein, D.3
  • 23
    • 31944436780 scopus 로고    scopus 로고
    • Depletion of phosphatidylcholine in yeast induces shortening and increased saturation of the lipid acyl chains: Evidence for regulation of intrinsic membrane curvature in a eukaryote
    • H.A. Boumann, J. Gubbens, M.C. Koorengevel, C.S. Oh, C.E. Martin, A.J. Heck, J. Patton-Vogt, S.A. Henry, B. de Kruijff, and A.I. de Kroon Depletion of phosphatidylcholine in yeast induces shortening and increased saturation of the lipid acyl chains: evidence for regulation of intrinsic membrane curvature in a eukaryote Mol. Biol. Cell 17 2006 1006 1017
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1006-1017
    • Boumann, H.A.1    Gubbens, J.2    Koorengevel, M.C.3    Oh, C.S.4    Martin, C.E.5    Heck, A.J.6    Patton-Vogt, J.7    Henry, S.A.8    De Kruijff, B.9    De Kroon, A.I.10
  • 24
    • 4243774348 scopus 로고
    • Mono- and dimethylethanolamine isolated from rat-liver phospholipids
    • J. Bremer, and D.M. Greenberg Mono- and dimethylethanolamine isolated from rat-liver phospholipids Biochim. Biophys. Acta 35 1959 287 288
    • (1959) Biochim. Biophys. Acta , vol.35 , pp. 287-288
    • Bremer, J.1    Greenberg, D.M.2
  • 26
    • 78649373124 scopus 로고    scopus 로고
    • Membranes in balance: Mechanisms of sphingolipid homeostasis
    • D.K. Breslow, and J.S. Weissman Membranes in balance: mechanisms of sphingolipid homeostasis Mol. Cell 40 2010 267 279
    • (2010) Mol. Cell , vol.40 , pp. 267-279
    • Breslow, D.K.1    Weissman, J.S.2
  • 27
    • 33751216445 scopus 로고    scopus 로고
    • Roles of phosphatidate phosphatase enzymes in lipid metabolism
    • G.M. Carman, and G.S. Han 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
  • 28
    • 33947267081 scopus 로고    scopus 로고
    • Regulation of phospholipid synthesis in Saccharomyces cerevisiae by zinc depletion
    • G.M. Carman, and G.S. Han Regulation of phospholipid synthesis in Saccharomyces cerevisiae by zinc depletion Biochim. Biophys. Acta 1771 2007 322 330
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 322-330
    • Carman, G.M.1    Han, G.S.2
  • 29
    • 59149106049 scopus 로고    scopus 로고
    • Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis
    • G.M. Carman, and G.S. Han Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis J. Biol. Chem. 284 2009 2593 2597
    • (2009) J. Biol. Chem. , vol.284 , pp. 2593-2597
    • Carman, G.M.1    Han, G.S.2
  • 30
    • 79959457450 scopus 로고    scopus 로고
    • Regulation of phospholipid synthesis in the yeast Saccharomyces cerevisiae
    • G.M. Carman, and G.S. Han Regulation of phospholipid synthesis in the yeast Saccharomyces cerevisiae Annu. Rev. Biochem. 80 2011 859 883
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 859-883
    • Carman, G.M.1    Han, G.S.2
  • 31
    • 0032730257 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in the yeast Saccharomyces cerevisiae and interrelationship with other metabolic processes
    • G.M. Carman, and S.A. Henry 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
  • 32
    • 38049110718 scopus 로고    scopus 로고
    • Phosphatidic acid plays a central role in the transcriptional regulation of glycerophospholipid synthesis in Saccharomyces cerevisiae
    • G.M. Carman, and S.A. Henry Phosphatidic acid plays a central role in the transcriptional regulation of glycerophospholipid synthesis in Saccharomyces cerevisiae J. Biol. Chem. 282 2007 37293 37297
    • (2007) J. Biol. Chem. , vol.282 , pp. 37293-37297
    • Carman, G.M.1    Henry, S.A.2
  • 33
    • 0020404410 scopus 로고
    • Properties of particulate and solubilized phosphatidylserine synthase activity from Saccharomyces cerevisiae. Inhibitory effect of choline in the growth medium
    • M.A. Carson, K.D. Atkinson, and C.J. Waechter Properties of particulate and solubilized phosphatidylserine synthase activity from Saccharomyces cerevisiae. Inhibitory effect of choline in the growth medium J. Biol. Chem. 257 1982 8115 8121
    • (1982) J. Biol. Chem. , vol.257 , pp. 8115-8121
    • Carson, M.A.1    Atkinson, K.D.2    Waechter, C.J.3
  • 34
    • 0021230103 scopus 로고
    • Coordinate regulation of phosphatidylserine decarboxylase activity and phospholipid N-methylation in yeast
    • M.A. Carson, M. Emala, P. Hogsten, and C.J. Waechter Coordinate regulation of phosphatidylserine decarboxylase activity and phospholipid N-methylation in yeast J. Biol. Chem. 259 1984 6267 6273
    • (1984) J. Biol. Chem. , vol.259 , pp. 6267-6273
    • Carson, M.A.1    Emala, M.2    Hogsten, P.3    Waechter, C.J.4
  • 36
    • 84870040165 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae actin patch protein App1p is a phosphatidate phosphatase enzyme
    • M. Chae, G.S. Han, and G.M. Carman The Saccharomyces cerevisiae actin patch protein App1p is a phosphatidate phosphatase enzyme J. Biol. Chem. 287 2012 40186 40196
    • (2012) J. Biol. Chem. , vol.287 , pp. 40186-40196
    • Chae, M.1    Han, G.S.2    Carman, G.M.3
  • 37
    • 11244299412 scopus 로고    scopus 로고
    • Role of the unfolded protein response pathway in secretory stress and regulation of INO1 expression in Saccharomyces cerevisiae
    • H.J. Chang, S.A. Jesch, M.L. Gaspar, and S.A. Henry Role of the unfolded protein response pathway in secretory stress and regulation of INO1 expression in Saccharomyces cerevisiae Genetics 168 2004 1899 1913
    • (2004) Genetics , vol.168 , pp. 1899-1913
    • Chang, H.J.1    Jesch, S.A.2    Gaspar, M.L.3    Henry, S.A.4
  • 38
    • 0036743487 scopus 로고    scopus 로고
    • Role of the unfolded protein response pathway in regulation of INO1 and in the sec14 bypass mechanism in Saccharomyces cerevisiae
    • H.J. Chang, E.W. Jones, and S.A. Henry Role of the unfolded protein response pathway in regulation of INO1 and in the sec14 bypass mechanism in Saccharomyces cerevisiae Genetics 162 2002 29 43
    • (2002) Genetics , vol.162 , pp. 29-43
    • Chang, H.J.1    Jones, E.W.2    Henry, S.A.3
  • 39
    • 33947201241 scopus 로고    scopus 로고
    • Transcriptional regulation of yeast phospholipid biosynthetic genes
    • M. Chen, L.C. Hancock, and J.M. Lopes Transcriptional regulation of yeast phospholipid biosynthetic genes Biochim. Biophys. Acta 1771 2007 310 321
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 310-321
    • Chen, M.1    Hancock, L.C.2    Lopes, J.M.3
  • 40
    • 0026442388 scopus 로고
    • Coordinated regulation and inositol-mediated and fatty acid-mediated repression of fatty acid synthase genes in Saccharomyces cerevisiae
    • S.S. Chirala Coordinated regulation and inositol-mediated and fatty acid-mediated repression of fatty acid synthase genes in Saccharomyces cerevisiae Proc. Natl. Acad. Sci. U.S.A. 89 1992 10232 10236
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10232-10236
    • Chirala, S.S.1
  • 41
    • 0023664194 scopus 로고
    • Complementation of mutations and nucleotide sequence of FAS1 gene encoding beta subunit of yeast fatty acid synthase
    • S.S. Chirala, M.A. Kuziora, D.M. Spector, and S.J. Wakil Complementation of mutations and nucleotide sequence of FAS1 gene encoding beta subunit of yeast fatty acid synthase J. Biol. Chem. 262 1987 4231 4240
    • (1987) J. Biol. Chem. , vol.262 , pp. 4231-4240
    • Chirala, S.S.1    Kuziora, M.A.2    Spector, D.M.3    Wakil, S.J.4
  • 42
    • 0028216507 scopus 로고
    • Analysis of FAS3/ACC regulatory region of Saccharomyces cerevisiae: Identification of a functional UASINO and sequences responsible for fatty acid mediated repression
    • S.S. Chirala, Q. Zhong, W. Huang, and W. al-Feel Analysis of FAS3/ACC regulatory region of Saccharomyces cerevisiae: identification of a functional UASINO and sequences responsible for fatty acid mediated repression Nucleic Acids Res. 22 1994 412 418
    • (1994) Nucleic Acids Res. , vol.22 , pp. 412-418
    • Chirala, S.S.1    Zhong, Q.2    Huang, W.3    Al-Feel, W.4
  • 43
    • 84859488188 scopus 로고    scopus 로고
    • Pho85p-Pho80p phosphorylation of yeast Pah1p phosphatidate phosphatase regulates its activity, location, abundance, and function in lipid metabolism
    • H.S. Choi, W.M. Su, G.S. Han, D. Plote, Z. Xu, and G.M. Carman Pho85p-Pho80p phosphorylation of yeast Pah1p phosphatidate phosphatase regulates its activity, location, abundance, and function in lipid metabolism J. Biol. Chem. 287 2012 11290 11301
    • (2012) J. Biol. Chem. , vol.287 , pp. 11290-11301
    • Choi, H.S.1    Su, W.M.2    Han, G.S.3    Plote, D.4    Xu, Z.5    Carman, G.M.6
  • 44
    • 78651385378 scopus 로고    scopus 로고
    • Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae: Identification of SER(602), THR(723), and SER(744) as the sites phosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase
    • H.S. Choi, W.M. Su, J.M. Morgan, G.S. Han, Z. Xu, E. Karanasios, S. Siniossoglou, and G.M. Carman Phosphorylation of phosphatidate phosphatase regulates its membrane association and physiological functions in Saccharomyces cerevisiae: identification of SER(602), THR(723), AND SER(744) as the sites phosphorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase J. Biol. Chem. 286 2011 1486 1498
    • (2011) J. Biol. Chem. , vol.286 , pp. 1486-1498
    • Choi, H.S.1    Su, W.M.2    Morgan, J.M.3    Han, G.S.4    Xu, Z.5    Karanasios, E.6    Siniossoglou, S.7    Carman, G.M.8
  • 45
    • 4744368134 scopus 로고    scopus 로고
    • Phosphatidylcholine and N-methylated phospholipids are nonessential in Saccharomyces cerevisiae
    • J.Y. Choi, W.E. Martin, R.C. Murphy, and D.R. Voelker Phosphatidylcholine and N-methylated phospholipids are nonessential in Saccharomyces cerevisiae J. Biol. Chem. 279 2004 42321 42330
    • (2004) J. Biol. Chem. , vol.279 , pp. 42321-42330
    • Choi, J.Y.1    Martin, W.E.2    Murphy, R.C.3    Voelker, D.R.4
  • 46
    • 0027423244 scopus 로고
    • Cloning of a gene (PSD1) encoding phosphatidylserine decarboxylase from Saccharomyces cerevisiae by complementation of an Escherichia coli mutant
    • C.J. Clancey, S.C. Chang, and W. Dowhan Cloning of a gene (PSD1) encoding phosphatidylserine decarboxylase from Saccharomyces cerevisiae by complementation of an Escherichia coli mutant J. Biol. Chem. 268 1993 24580 24590
    • (1993) J. Biol. Chem. , vol.268 , pp. 24580-24590
    • Clancey, C.J.1    Chang, S.C.2    Dowhan, W.3
  • 47
    • 0026073075 scopus 로고
    • Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein
    • A.E. Cleves, T.P. McGee, E.A. Whitters, K.M. Champion, J.R. Aitken, W. Dowhan, M. Goebl, and V.A. Bankaitis Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein Cell 64 1991 789 800
    • (1991) Cell , vol.64 , pp. 789-800
    • Cleves, A.E.1    McGee, T.P.2    Whitters, E.A.3    Champion, K.M.4    Aitken, J.R.5    Dowhan, W.6    Goebl, M.7    Bankaitis, V.A.8
  • 48
    • 47049125352 scopus 로고    scopus 로고
    • Hos2p/Set3p deacetylase complex signals secretory stress through the Mpk1p cell integrity pathway
    • T.J. Cohen, M.J. Mallory, R. Strich, and T.P. Yao Hos2p/Set3p deacetylase complex signals secretory stress through the Mpk1p cell integrity pathway Eukaryot. Cell 7 2008 1191 1199
    • (2008) Eukaryot. Cell , vol.7 , pp. 1191-1199
    • Cohen, T.J.1    Mallory, M.J.2    Strich, R.3    Yao, T.P.4
  • 49
    • 0030879870 scopus 로고    scopus 로고
    • The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane
    • J.S. Cox, R.E. Chapman, and P. Walter The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane Mol. Biol. Cell 8 1997 1805 1814
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1805-1814
    • Cox, J.S.1    Chapman, R.E.2    Walter, P.3
  • 50
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • J.S. Cox, C.E. Shamu, and P. Walter Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase Cell 73 1993 1197 1206
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 51
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • J.S. Cox, and P. Walter A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response Cell 87 1996 391 404
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 53
    • 0017293280 scopus 로고
    • Control of inositol biosynthesis in Saccharomyces cerevisiae; Inositol-phosphate synthetase mutants
    • M.R. Culbertson, T.F. Donahue, and S.A. Henry Control of inositol biosynthesis in Saccharomyces cerevisiae; inositol-phosphate synthetase mutants J. Bacteriol. 126 1976 243 250
    • (1976) J. Bacteriol. , vol.126 , pp. 243-250
    • Culbertson, M.R.1    Donahue, T.F.2    Henry, S.A.3
  • 54
    • 0016739154 scopus 로고
    • Inositol-requiring mutants of Saccharomyces cerevisiae
    • M.R. Culbertson, and S.A. Henry Inositol-requiring mutants of Saccharomyces cerevisiae Genetics 80 1975 23 40
    • (1975) Genetics , vol.80 , pp. 23-40
    • Culbertson, M.R.1    Henry, S.A.2
  • 55
    • 0024494204 scopus 로고
    • Biosynthesis of inositol in yeast. Primary structure of myo-inositol-1-phosphate synthase (EC 5.5.1.4) and functional analysis of its structural gene, the INO1 locus
    • M. Dean-Johnson, and S.A. Henry Biosynthesis of inositol in yeast. Primary structure of myo-inositol-1-phosphate synthase (EC 5.5.1.4) and functional analysis of its structural gene, the INO1 locus J. Biol. Chem. 264 1989 1274 1283
    • (1989) J. Biol. Chem. , vol.264 , pp. 1274-1283
    • Dean-Johnson, M.1    Henry, S.A.2
  • 56
    • 70350169737 scopus 로고    scopus 로고
    • Cellular consequences of inositol depletion
    • R.M. Deranieh, and M.L. Greenberg Cellular consequences of inositol depletion Biochem. Soc. Trans. 37 2009 1099 1103
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 1099-1103
    • Deranieh, R.M.1    Greenberg, M.L.2
  • 57
    • 84884182719 scopus 로고    scopus 로고
    • Phosphorylation regulates myo-inositol-3-phosphate synthase: A novel regulatory mechanism of inositol biosynthesis
    • R.M. Deranieh, Q. He, J.A. Caruso, and M.L. Greenberg Phosphorylation regulates myo-inositol-3-phosphate synthase: a novel regulatory mechanism of inositol biosynthesis J. Biol. Chem. 2013
    • (2013) J. Biol. Chem.
    • Deranieh, R.M.1    He, Q.2    Caruso, J.A.3    Greenberg, M.L.4
  • 58
    • 50049119791 scopus 로고    scopus 로고
    • Thematic review series: Sphingolipids. New insights into sphingolipid metabolism and function in budding yeast
    • R.C. Dickson Thematic review series: sphingolipids. New insights into sphingolipid metabolism and function in budding yeast J. Lipid Res. 49 2008 909 921
    • (2008) J. Lipid Res. , vol.49 , pp. 909-921
    • Dickson, R.C.1
  • 59
    • 0030069907 scopus 로고    scopus 로고
    • GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COP II vesicles
    • T.L. Doering, and R. Schekman GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COP II vesicles EMBO J. 15 1996 182 191
    • (1996) EMBO J. , vol.15 , pp. 182-191
    • Doering, T.L.1    Schekman, R.2
  • 60
    • 0000050123 scopus 로고
    • Inositol mutants of Saccharomyces cerevisiae: Mapping the ino1 locus and characterizing alleles of the ino1, ino2 and ino4 loci
    • T.F. Donahue, and S.A. Henry Inositol mutants of Saccharomyces cerevisiae: mapping the ino1 locus and characterizing alleles of the ino1, ino2 and ino4 loci Genetics 98 1981 491 503
    • (1981) Genetics , vol.98 , pp. 491-503
    • Donahue, T.F.1    Henry, S.A.2
  • 61
    • 0019877154 scopus 로고
    • Myo-Inositol-1-phosphate synthase. Characteristics of the enzyme and identification of its structural gene in yeast
    • T.F. Donahue, and S.A. Henry myo-Inositol-1-phosphate synthase. Characteristics of the enzyme and identification of its structural gene in yeast J. Biol. Chem. 256 1981 7077 7085
    • (1981) J. Biol. Chem. , vol.256 , pp. 7077-7085
    • Donahue, T.F.1    Henry, S.A.2
  • 62
    • 0035830886 scopus 로고    scopus 로고
    • Turnover of phosphatidylcholine in Saccharomyces cerevisiae. The role of the CDP-choline pathway
    • S.R. Dowd, M.E. Bier, and J.L. Patton-Vogt Turnover of phosphatidylcholine in Saccharomyces cerevisiae. The role of the CDP-choline pathway J. Biol. Chem. 276 2001 3756 3763
    • (2001) J. Biol. Chem. , vol.276 , pp. 3756-3763
    • Dowd, S.R.1    Bier, M.E.2    Patton-Vogt, J.L.3
  • 63
    • 0033010289 scopus 로고    scopus 로고
    • The product of the SNF2/SWI2 paralogue INO80 of Saccharomyces cerevisiae required for efficient expression of various yeast structural genes is part of a high-molecular-weight protein complex
    • R. Ebbert, A. Birkmann, and H.J. Schuller The product of the SNF2/SWI2 paralogue INO80 of Saccharomyces cerevisiae required for efficient expression of various yeast structural genes is part of a high-molecular-weight protein complex Mol. Microbiol. 32 1999 741 751
    • (1999) Mol. Microbiol. , vol.32 , pp. 741-751
    • Ebbert, R.1    Birkmann, A.2    Schuller, H.J.3
  • 64
    • 0034663636 scopus 로고    scopus 로고
    • Combinatorial regulation of phospholipid biosynthetic gene expression by the UME6, SIN3 and RPD3 genes
    • M. Elkhaimi, M.R. Kaadige, D. Kamath, J.C. Jackson, H. Biliran Jr., and J.M. Lopes Combinatorial regulation of phospholipid biosynthetic gene expression by the UME6, SIN3 and RPD3 genes Nucleic Acids Res. 28 2000 3160 3167
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3160-3167
    • Elkhaimi, M.1    Kaadige, M.R.2    Kamath, D.3    Jackson, J.C.4    Biliran, Jr.H.5    Lopes, J.M.6
  • 65
    • 78651385047 scopus 로고    scopus 로고
    • DGK1-encoded diacylglycerol kinase activity is required for phospholipid synthesis during growth resumption from stationary phase in Saccharomyces cerevisiae
    • S. Fakas, C. Konstantinou, and G.M. Carman DGK1-encoded diacylglycerol kinase activity is required for phospholipid synthesis during growth resumption from stationary phase in Saccharomyces cerevisiae J. Biol. Chem. 286 2011 1464 1474
    • (2011) J. Biol. Chem. , vol.286 , pp. 1464-1474
    • Fakas, S.1    Konstantinou, C.2    Carman, G.M.3
  • 66
    • 0033591216 scopus 로고    scopus 로고
    • The LPP1 and DPP1 gene products account for most of the isoprenoid phosphate phosphatase activities in Saccharomyces cerevisiae
    • A. Faulkner, X. Chen, J. Rush, B. Horazdovsky, C.J. Waechter, G.M. Carman, and P.C. Sternweis 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    Sternweis, P.C.7
  • 67
    • 73649107925 scopus 로고    scopus 로고
    • NTE1-encoded phosphatidylcholine phospholipase b regulates transcription of phospholipid biosynthetic genes
    • J.P. Fernandez-Murray, G.J. Gaspard, S.A. Jesch, and C.R. McMaster NTE1-encoded phosphatidylcholine phospholipase b regulates transcription of phospholipid biosynthetic genes J. Biol. Chem. 284 2009 36034 36046
    • (2009) J. Biol. Chem. , vol.284 , pp. 36034-36046
    • Fernandez-Murray, J.P.1    Gaspard, G.J.2    Jesch, S.A.3    McMaster, C.R.4
  • 68
    • 31944439123 scopus 로고    scopus 로고
    • Glycerophosphocholine catabolism as a new route for choline formation for phosphatidylcholine synthesis by the Kennedy pathway
    • J.P. Fernandez-Murray, and C.R. McMaster Glycerophosphocholine catabolism as a new route for choline formation for phosphatidylcholine synthesis by the Kennedy pathway J. Biol. Chem. 280 2005 38290 38296
    • (2005) J. Biol. Chem. , vol.280 , pp. 38290-38296
    • Fernandez-Murray, J.P.1    McMaster, C.R.2
  • 69
    • 84862189303 scopus 로고    scopus 로고
    • GPI-anchor remodeling: Potential functions of GPI-anchors in intracellular trafficking and membrane dynamics
    • M. Fujita, and T. Kinoshita GPI-anchor remodeling: potential functions of GPI-anchors in intracellular trafficking and membrane dynamics Biochim. Biophys. Acta 1821 2012 1050 1058
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 1050-1058
    • Fujita, M.1    Kinoshita, T.2
  • 70
    • 84863613036 scopus 로고    scopus 로고
    • Acetyl-CoA carboxylase regulates global histone acetylation
    • L. Galdieri, and A. Vancura Acetyl-CoA carboxylase regulates global histone acetylation J. Biol. Chem. 287 2012 23865 23876
    • (2012) J. Biol. Chem. , vol.287 , pp. 23865-23876
    • Galdieri, L.1    Vancura, A.2
  • 71
    • 0028796702 scopus 로고
    • The Saccharomyces cerevisiae SPT7 gene encodes a very acidic protein important for transcription in vivo
    • L.J. Gansheroff, C. Dollard, P. Tan, and F. Winston The Saccharomyces cerevisiae SPT7 gene encodes a very acidic protein important for transcription in vivo Genetics 139 1995 523 536
    • (1995) Genetics , vol.139 , pp. 523-536
    • Gansheroff, L.J.1    Dollard, C.2    Tan, P.3    Winston, F.4
  • 73
    • 21844441146 scopus 로고    scopus 로고
    • Phosphatidylinositol biosynthesis: Biochemistry and regulation
    • M.E. Gardocki, N. Jani, and J.M. Lopes Phosphatidylinositol biosynthesis: biochemistry and regulation Biochim. Biophys. Acta 1735 2005 89 100
    • (2005) Biochim. Biophys. Acta , vol.1735 , pp. 89-100
    • Gardocki, M.E.1    Jani, N.2    Lopes, J.M.3
  • 74
    • 0141755264 scopus 로고    scopus 로고
    • Expression of the yeast PIS1 gene requires multiple regulatory elements including a Rox1p binding site
    • M.E. Gardocki, and J.M. Lopes Expression of the yeast PIS1 gene requires multiple regulatory elements including a Rox1p binding site J. Biol. Chem. 278 2003 38646 38652
    • (2003) J. Biol. Chem. , vol.278 , pp. 38646-38652
    • Gardocki, M.E.1    Lopes, J.M.2
  • 75
    • 33747375103 scopus 로고    scopus 로고
    • Inositol induces a profound alteration in the pattern and rate of synthesis and turnover of membrane lipids in Saccharomyces cerevisiae
    • M.L. Gaspar, M.A. Aregullin, S.A. Jesch, and S.A. Henry Inositol induces a profound alteration in the pattern and rate of synthesis and turnover of membrane lipids in Saccharomyces cerevisiae J. Biol. Chem. 281 2006 22773 22785
    • (2006) J. Biol. Chem. , vol.281 , pp. 22773-22785
    • Gaspar, M.L.1    Aregullin, M.A.2    Jesch, S.A.3    Henry, S.A.4
  • 77
    • 78751547969 scopus 로고    scopus 로고
    • Coordination of storage lipid synthesis and membrane biogenesis: Evidence for cross-talk between triacylglycerol metabolism and phosphatidylinositol synthesis
    • M.L. Gaspar, H.F. Hofbauer, S.D. Kohlwein, and S.A. Henry Coordination of storage lipid synthesis and membrane biogenesis: evidence for cross-talk between triacylglycerol metabolism and phosphatidylinositol synthesis J. Biol. Chem. 286 2011 1696 1708
    • (2011) J. Biol. Chem. , vol.286 , pp. 1696-1708
    • Gaspar, M.L.1    Hofbauer, H.F.2    Kohlwein, S.D.3    Henry, S.A.4
  • 78
    • 54449092523 scopus 로고    scopus 로고
    • A block in endoplasmic reticulum-to-Golgi trafficking inhibits phospholipid synthesis and induces neutral lipid accumulation
    • M.L. Gaspar, S.A. Jesch, R. Viswanatha, A.L. Antosh, W.J. Brown, S.D. Kohlwein, and S.A. Henry A block in endoplasmic reticulum-to-Golgi trafficking inhibits phospholipid synthesis and induces neutral lipid accumulation J. Biol. Chem. 283 2008 25735 25751
    • (2008) J. Biol. Chem. , vol.283 , pp. 25735-25751
    • Gaspar, M.L.1    Jesch, S.A.2    Viswanatha, R.3    Antosh, A.L.4    Brown, W.J.5    Kohlwein, S.D.6    Henry, S.A.7
  • 79
    • 0025944585 scopus 로고
    • Regulation of phosphatidylethanolamine methyltransferase and phospholipid methyltransferase by phospholipid precursors in Saccharomyces cerevisiae
    • P.M. Gaynor, T. Gill, S. Toutenhoofd, E.F. Summers, P. McGraw, M.J. Homann, S.A. Henry, and G.M. Carman Regulation of phosphatidylethanolamine methyltransferase and phospholipid methyltransferase by phospholipid precursors in Saccharomyces cerevisiae Biochim. Biophys. Acta 1090 1991 326 332
    • (1991) Biochim. Biophys. Acta , vol.1090 , pp. 326-332
    • Gaynor, P.M.1    Gill, T.2    Toutenhoofd, S.3    Summers, E.F.4    McGraw, P.5    Homann, M.J.6    Henry, S.A.7    Carman, G.M.8
  • 80
    • 39049184513 scopus 로고    scopus 로고
    • The structure and mechanism of myo-inositol-1-phosphate synthase
    • J.H. Geiger, and X. Jin The structure and mechanism of myo-inositol-1-phosphate synthase Subcell. Biochem. 39 2006 157 180
    • (2006) Subcell. Biochem. , vol.39 , pp. 157-180
    • Geiger, J.H.1    Jin, X.2
  • 81
    • 80051975542 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer proteins: Negotiating the regulatory interface between lipid metabolism and lipid signaling in diverse cellular processes
    • R. Ghosh, and V.A. Bankaitis Phosphatidylinositol transfer proteins: negotiating the regulatory interface between lipid metabolism and lipid signaling in diverse cellular processes Biofactors 37 2011 290 308
    • (2011) Biofactors , vol.37 , pp. 290-308
    • Ghosh, R.1    Bankaitis, V.A.2
  • 82
    • 0011060849 scopus 로고
    • The enzymatic conversion of phospholipid ethanolamine to phospholipid choline in rat liver
    • K.D. Gibson, J.D. Wilson, and S. Udenfriend The enzymatic conversion of phospholipid ethanolamine to phospholipid choline in rat liver J. Biol. Chem. 236 1961 673 679
    • (1961) J. Biol. Chem. , vol.236 , pp. 673-679
    • Gibson, K.D.1    Wilson, J.D.2    Udenfriend, S.3
  • 83
    • 0032743154 scopus 로고    scopus 로고
    • Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles
    • C.F. Gilstring, M. Melin-Larsson, and P.O. Ljungdahl Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesicles Mol. Biol. Cell 10 1999 3549 3565
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3549-3565
    • Gilstring, C.F.1    Melin-Larsson, M.2    Ljungdahl, P.O.3
  • 84
    • 0034075621 scopus 로고    scopus 로고
    • Regulation of the yeast INO1 gene. The products of the INO2, INO4 and OPI1 regulatory genes are not required for repression in response to inositol
    • J.A. Graves, and S.A. Henry Regulation of the yeast INO1 gene. The products of the INO2, INO4 and OPI1 regulatory genes are not required for repression in response to inositol Genetics 154 2000 1485 1495
    • (2000) Genetics , vol.154 , pp. 1485-1495
    • Graves, J.A.1    Henry, S.A.2
  • 86
    • 0019988791 scopus 로고
    • Characterization of a yeast regulatory mutant constitutive for synthesis of inositol-1-phosphate synthase
    • M.L. Greenberg, P. Goldwasser, and S.A. Henry Characterization of a yeast regulatory mutant constitutive for synthesis of inositol-1-phosphate synthase Mol. Gen. Genet. 186 1982 157 163
    • (1982) Mol. Gen. Genet. , vol.186 , pp. 157-163
    • Greenberg, M.L.1    Goldwasser, P.2    Henry, S.A.3
  • 88
    • 0029963923 scopus 로고    scopus 로고
    • Genetic regulation of phospholipid biosynthesis in Saccharomyces cerevisiae
    • M.L. Greenberg, and J.M. Lopes 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
  • 89
    • 0020287589 scopus 로고
    • Regulatory mutations of inositol biosynthesis in yeast: Isolation of inositol-excreting mutants
    • M.L. Greenberg, B. Reiner, and S.A. Henry Regulatory mutations of inositol biosynthesis in yeast: isolation of inositol-excreting mutants Genetics 100 1982 19 33
    • (1982) Genetics , vol.100 , pp. 19-33
    • Greenberg, M.L.1    Reiner, B.2    Henry, S.A.3
  • 90
    • 0030884077 scopus 로고    scopus 로고
    • Regulation of yeast phospholipid biosynthetic genes in phosphatidylserine decarboxylase mutants
    • P. Griac Regulation of yeast phospholipid biosynthetic genes in phosphatidylserine decarboxylase mutants J. Bacteriol. 179 1997 5843 5848
    • (1997) J. Bacteriol. , vol.179 , pp. 5843-5848
    • Griac, P.1
  • 91
    • 34249818772 scopus 로고    scopus 로고
    • Sec14 related proteins in yeast
    • P. Griac Sec14 related proteins in yeast Biochim. Biophys. Acta 1771 2007 737 745
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 737-745
    • Griac, P.1
  • 92
    • 0033135198 scopus 로고    scopus 로고
    • The yeast inositol-sensitive upstream activating sequence, UASINO, responds to nitrogen availability
    • P. Griac, and S.A. Henry The yeast inositol-sensitive upstream activating sequence, UASINO, responds to nitrogen availability Nucleic Acids Res. 27 1999 2043 2050
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2043-2050
    • Griac, P.1    Henry, S.A.2
  • 93
    • 0029818842 scopus 로고    scopus 로고
    • The role of phosphatidylcholine biosynthesis in the regulation of the INO1 gene of yeast
    • P. Griac, M.J. Swede, and S.A. Henry The role of phosphatidylcholine biosynthesis in the regulation of the INO1 gene of yeast J. Biol. Chem. 271 1996 25692 25698
    • (1996) J. Biol. Chem. , vol.271 , pp. 25692-25698
    • Griac, P.1    Swede, M.J.2    Henry, S.A.3
  • 94
    • 84864301007 scopus 로고    scopus 로고
    • Multiple histone deacetylases are recruited by corepressor Sin3 and contribute to gene repression mediated by Opi1 regulator of phospholipid biosynthesis in the yeast Saccharomyces cerevisiae
    • M. Grigat, Y. Jaschke, F. Kliewe, M. Pfeifer, S. Walz, and H.J. Schuller Multiple histone deacetylases are recruited by corepressor Sin3 and contribute to gene repression mediated by Opi1 regulator of phospholipid biosynthesis in the yeast Saccharomyces cerevisiae Mol. Genet. Genomics 287 2012 461 472
    • (2012) Mol. Genet. Genomics , vol.287 , pp. 461-472
    • Grigat, M.1    Jaschke, Y.2    Kliewe, F.3    Pfeifer, M.4    Walz, S.5    Schuller, H.J.6
  • 95
    • 84880075508 scopus 로고    scopus 로고
    • Orm proteins integrate multiple signals to maintain sphingolipid homeostasis
    • C. Gururaj, R. Federman, and A. Chang Orm proteins integrate multiple signals to maintain sphingolipid homeostasis J. Biol. Chem. 288 2013 20453 20463
    • (2013) J. Biol. Chem. , vol.288 , pp. 20453-20463
    • Gururaj, C.1    Federman, R.2    Chang, A.3
  • 96
    • 0030966330 scopus 로고    scopus 로고
    • A review of phenotypes in Saccharomyces cerevisiae
    • M. Hampsey A review of phenotypes in Saccharomyces cerevisiae Yeast 13 1997 1099 1133
    • (1997) Yeast , vol.13 , pp. 1099-1133
    • Hampsey, M.1
  • 97
    • 77951979740 scopus 로고    scopus 로고
    • Characterization of the human LPIN1-encoded phosphatidate phosphatase isoforms
    • G.S. Han, and G.M. Carman Characterization of the human LPIN1-encoded phosphatidate phosphatase isoforms J. Biol. Chem. 285 2010 14628 14638
    • (2010) J. Biol. Chem. , vol.285 , pp. 14628-14638
    • Han, G.S.1    Carman, G.M.2
  • 98
    • 0035971250 scopus 로고    scopus 로고
    • Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc
    • G.S. Han, C.N. Johnston, X. Chen, K. Athenstaedt, G. Daum, and G.M. Carman Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase by zinc J. Biol. Chem. 276 2001 10126 10133
    • (2001) J. Biol. Chem. , vol.276 , pp. 10126-10133
    • Han, G.S.1    Johnston, C.N.2    Chen, X.3    Athenstaedt, K.4    Daum, G.5    Carman, G.M.6
  • 99
    • 50649090967 scopus 로고    scopus 로고
    • An unconventional diacylglycerol kinase that regulates phospholipid synthesis and nuclear membrane growth
    • G.S. Han, L. O'Hara, G.M. Carman, and S. Siniossoglou An unconventional diacylglycerol kinase that regulates phospholipid synthesis and nuclear membrane growth J. Biol. Chem. 283 2008 20433 20442
    • (2008) J. Biol. Chem. , vol.283 , pp. 20433-20442
    • Han, G.S.1    O'Hara, L.2    Carman, G.M.3    Siniossoglou, S.4
  • 100
    • 50649106881 scopus 로고    scopus 로고
    • Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase
    • G.S. Han, L. O'Hara, S. Siniossoglou, and G.M. Carman Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase J. Biol. Chem. 283 2008 20443 20453
    • (2008) J. Biol. Chem. , vol.283 , pp. 20443-20453
    • Han, G.S.1    O'Hara, L.2    Siniossoglou, S.3    Carman, G.M.4
  • 101
    • 37549018969 scopus 로고    scopus 로고
    • The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity
    • G.S. Han, S. Siniossoglou, and G.M. Carman 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
  • 102
  • 103
    • 77950541324 scopus 로고    scopus 로고
    • Orm1 and Orm2 are conserved endoplasmic reticulum membrane proteins regulating lipid homeostasis and protein quality control
    • S. Han, M.A. Lone, R. Schneiter, and A. Chang Orm1 and Orm2 are conserved endoplasmic reticulum membrane proteins regulating lipid homeostasis and protein quality control Proc. Natl. Acad. Sci. U.S.A. 107 2010 5851 5856
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5851-5856
    • Han, S.1    Lone, M.A.2    Schneiter, R.3    Chang, A.4
  • 104
    • 23844541658 scopus 로고    scopus 로고
    • Regulation of the PIS1-encoded phosphatidylinositol synthase in Saccharomyces cerevisiae by zinc
    • S.H. Han, G.S. Han, W.M. Iwanyshyn, and G.M. Carman Regulation of the PIS1-encoded phosphatidylinositol synthase in Saccharomyces cerevisiae by zinc J. Biol. Chem. 280 2005 29017 29024
    • (2005) J. Biol. Chem. , vol.280 , pp. 29017-29024
    • Han, S.H.1    Han, G.S.2    Iwanyshyn, W.M.3    Carman, G.M.4
  • 106
    • 0018965678 scopus 로고
    • Effects of inositol starvation on phospholipid and glycan syntheses in Saccharomyces cerevisiae
    • B.A. Hanson, and R.L. Lester Effects of inositol starvation on phospholipid and glycan syntheses in Saccharomyces cerevisiae J. Bacteriol. 142 1980 79 89
    • (1980) J. Bacteriol. , vol.142 , pp. 79-89
    • Hanson, B.A.1    Lester, R.L.2
  • 107
    • 0027289677 scopus 로고
    • Acetyl-CoA carboxylase from yeast is an essential enzyme and is regulated by factors that control phospholipid metabolism
    • M. Hasslacher, A.S. Ivessa, F. Paltauf, and S.D. Kohlwein Acetyl-CoA carboxylase from yeast is an essential enzyme and is regulated by factors that control phospholipid metabolism J. Biol. Chem. 268 1993 10946 10952
    • (1993) J. Biol. Chem. , vol.268 , pp. 10946-10952
    • Hasslacher, M.1    Ivessa, A.S.2    Paltauf, F.3    Kohlwein, S.D.4
  • 108
    • 0029817763 scopus 로고    scopus 로고
    • Spreading of transcriptional repressor SIR3 from telomeric heterochromatin
    • A. Hecht, S. Strahl-Bolsinger, and M. Grunstein Spreading of transcriptional repressor SIR3 from telomeric heterochromatin Nature 383 1996 92 96
    • (1996) Nature , vol.383 , pp. 92-96
    • Hecht, A.1    Strahl-Bolsinger, S.2    Grunstein, M.3
  • 109
    • 15944391363 scopus 로고    scopus 로고
    • Sterol homeostasis in the budding yeast, Saccharomyces cerevisiae
    • A.L. Henneberry, and S.L. Sturley Sterol homeostasis in the budding yeast, Saccharomyces cerevisiae Semin. Cell Dev. Biol. 16 2005 155 161
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 155-161
    • Henneberry, A.L.1    Sturley, S.L.2
  • 110
    • 0015765975 scopus 로고
    • Death resulting from fatty acid starvation in yeast
    • S.A. Henry Death resulting from fatty acid starvation in yeast J. Bacteriol. 116 1973 1293 1303
    • (1973) J. Bacteriol. , vol.116 , pp. 1293-1303
    • Henry, S.A.1
  • 111
    • 0017579105 scopus 로고
    • Growth and metabolism of inositol-starved Saccharomyces cerevisiae
    • S.A. Henry, K.D. Atkinson, A.I. Kolat, and M.R. Culbertson Growth and metabolism of inositol-starved Saccharomyces cerevisiae J. Bacteriol. 130 1977 472 484
    • (1977) J. Bacteriol. , vol.130 , pp. 472-484
    • Henry, S.A.1    Atkinson, K.D.2    Kolat, A.I.3    Culbertson, M.R.4
  • 112
    • 0016790829 scopus 로고
    • Selection of spontaneous mutants by inositol starvation in yeast
    • S.A. Henry, T.F. Donahue, and M.R. Culbertson Selection of spontaneous mutants by inositol starvation in yeast Mol. Gen. Genet. 143 1975 5 11
    • (1975) Mol. Gen. Genet. , vol.143 , pp. 5-11
    • Henry, S.A.1    Donahue, T.F.2    Culbertson, M.R.3
  • 113
    • 0016711106 scopus 로고
    • A new method for mutant selection in Saccharomyces cerevisiae
    • S.A. Henry, and B. Horowitz A new method for mutant selection in Saccharomyces cerevisiae Genetics 79 1975 175 186
    • (1975) Genetics , vol.79 , pp. 175-186
    • Henry, S.A.1    Horowitz, B.2
  • 114
    • 84857424979 scopus 로고    scopus 로고
    • Metabolism and regulation of glycerolipids in the yeast Saccharomyces cerevisiae
    • S.A. Henry, S.D. Kohlwein, and G.M. Carman Metabolism and regulation of glycerolipids in the yeast Saccharomyces cerevisiae Genetics 190 2012 317 349
    • (2012) Genetics , vol.190 , pp. 317-349
    • Henry, S.A.1    Kohlwein, S.D.2    Carman, G.M.3
  • 115
    • 0031610424 scopus 로고    scopus 로고
    • Genetic regulation of phospholipid metabolism: Yeast as a model eukaryote
    • S.A. Henry, and J.L. Patton-Vogt Genetic regulation of phospholipid metabolism: yeast as a model eukaryote Prog. Nucleic Acid Res. Mol. Biol. 61 1998 133 179
    • (1998) Prog. Nucleic Acid Res. Mol. Biol. , vol.61 , pp. 133-179
    • Henry, S.A.1    Patton-Vogt, J.L.2
  • 116
    • 80655144718 scopus 로고    scopus 로고
    • Coordinated regulation of sulfur and phospholipid metabolism reflects the importance of methylation in the growth of yeast
    • M.J. Hickman, A.A. Petti, O. Ho-Shing, S.J. Silverman, R.S. McIsaac, T.A. Lee, and D. Botstein Coordinated regulation of sulfur and phospholipid metabolism reflects the importance of methylation in the growth of yeast Mol. Biol. Cell 22 2011 4192 4204
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4192-4204
    • Hickman, M.J.1    Petti, A.A.2    Ho-Shing, O.3    Silverman, S.J.4    McIsaac, R.S.5    Lee, T.A.6    Botstein, D.7
  • 117
    • 0022799260 scopus 로고
    • Expression of the Saccharomyces cerevisiae inositol-1-phosphate synthase (INO1) gene is regulated by factors that affect phospholipid synthesis
    • J.P. Hirsch, and S.A. Henry Expression of the Saccharomyces cerevisiae inositol-1-phosphate synthase (INO1) gene is regulated by factors that affect phospholipid synthesis Mol. Cell. Biol. 6 1986 3320 3328
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3320-3328
    • Hirsch, J.P.1    Henry, S.A.2
  • 118
    • 0023191358 scopus 로고
    • Coordinate regulation of phospholipid biosynthesis by serine in Saccharomyces cerevisiae
    • M.J. Homann, A.M. Bailis, S.A. Henry, and G.M. Carman Coordinate regulation of phospholipid biosynthesis by serine in Saccharomyces cerevisiae J. Bacteriol. 169 1987 3276 3280
    • (1987) J. Bacteriol. , vol.169 , pp. 3276-3280
    • Homann, M.J.1    Bailis, A.M.2    Henry, S.A.3    Carman, G.M.4
  • 119
    • 0021961327 scopus 로고
    • Regulation of CDP-diacylglycerol synthase activity in Saccharomyces cerevisiae
    • M.J. Homann, S.A. Henry, and G.M. Carman Regulation of CDP-diacylglycerol synthase activity in Saccharomyces cerevisiae J. Bacteriol. 163 1985 1265 1266
    • (1985) J. Bacteriol. , vol.163 , pp. 1265-1266
    • Homann, M.J.1    Henry, S.A.2    Carman, G.M.3
  • 120
    • 0030977168 scopus 로고    scopus 로고
    • ADA1, a novel component of the ADA/GCN5 complex, has broader effects than GCN5, ADA2, or ADA3
    • J. Horiuchi, N. Silverman, B. Pina, G.A. Marcus, and L. Guarente ADA1, a novel component of the ADA/GCN5 complex, has broader effects than GCN5, ADA2, or ADA3 Mol. Cell. Biol. 17 1997 3220 3228
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3220-3228
    • Horiuchi, J.1    Silverman, N.2    Pina, B.3    Marcus, G.A.4    Guarente, L.5
  • 121
    • 0025440498 scopus 로고
    • Regulation of expression of phospholipid-biosynthetic genes in yeast: Coordinate repression by inositol and choline
    • K. Hosaka, and T. Kodaki Regulation of expression of phospholipid- biosynthetic genes in yeast: coordinate repression by inositol and choline Seikagaku 62 1990 451 456
    • (1990) Seikagaku , vol.62 , pp. 451-456
    • Hosaka, K.1    Kodaki, T.2
  • 122
    • 0025308303 scopus 로고
    • Repression of choline kinase by inositol and choline in Saccharomyces cerevisiae
    • K. Hosaka, T. Murakami, T. Kodaki, J. Nikawa, and S. Yamashita Repression of choline kinase by inositol and choline in Saccharomyces cerevisiae J. Bacteriol. 172 1990 2005 2012
    • (1990) J. Bacteriol. , vol.172 , pp. 2005-2012
    • Hosaka, K.1    Murakami, T.2    Kodaki, T.3    Nikawa, J.4    Yamashita, S.5
  • 123
    • 0025249935 scopus 로고
    • The Saccharomyces cerevisiae INO4 gene encodes a small, highly basic protein required for derepression of phospholipid biosynthetic enzymes
    • D.K. Hoshizaki, J.E. Hill, and S.A. Henry The Saccharomyces cerevisiae INO4 gene encodes a small, highly basic protein required for derepression of phospholipid biosynthetic enzymes J. Biol. Chem. 265 1990 4736 4745
    • (1990) J. Biol. Chem. , vol.265 , pp. 4736-4745
    • Hoshizaki, D.K.1    Hill, J.E.2    Henry, S.A.3
  • 124
    • 33745751071 scopus 로고    scopus 로고
    • Regulation of phosphatidylcholine homeostasis by Sec14
    • A.G. Howe, and C.R. McMaster Regulation of phosphatidylcholine homeostasis by Sec14 Can. J. Physiol. Pharmacol. 84 2006 29 38
    • (2006) Can. J. Physiol. Pharmacol. , vol.84 , pp. 29-38
    • Howe, A.G.1    McMaster, C.R.2
  • 125
    • 0028040191 scopus 로고
    • A pleiotropic phospholipid biosynthetic regulatory mutation in Saccharomyces cerevisiae is allelic to sin3 (sdi1, ume4, rpd1)
    • K.A. Hudak, J.M. Lopes, and S.A. Henry A pleiotropic phospholipid biosynthetic regulatory mutation in Saccharomyces cerevisiae is allelic to sin3 (sdi1, ume4, rpd1) Genetics 136 1994 475 483
    • (1994) Genetics , vol.136 , pp. 475-483
    • Hudak, K.A.1    Lopes, J.M.2    Henry, S.A.3
  • 126
    • 0029968853 scopus 로고    scopus 로고
    • The yeast UME6 gene is required for both negative and positive transcriptional regulation of phospholipid biosynthetic gene expression
    • J.C. Jackson, and J.M. Lopes The yeast UME6 gene is required for both negative and positive transcriptional regulation of phospholipid biosynthetic gene expression Nucleic Acids Res. 24 1996 1322 1329
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1322-1329
    • Jackson, J.C.1    Lopes, J.M.2
  • 127
    • 56749182210 scopus 로고    scopus 로고
    • Transcription regulation of the Saccharomyces cerevisiae PIS1 gene by inositol and the pleiotropic regulator, Ume6p
    • N.M. Jani, and J.M. Lopes Transcription regulation of the Saccharomyces cerevisiae PIS1 gene by inositol and the pleiotropic regulator, Ume6p Mol. Microbiol. 70 2008 1529 1539
    • (2008) Mol. Microbiol. , vol.70 , pp. 1529-1539
    • Jani, N.M.1    Lopes, J.M.2
  • 128
    • 65549124929 scopus 로고    scopus 로고
    • Regulated transcription of the Saccharomyces cerevisiae phosphatidylinositol biosynthetic gene, PIS1, yields pleiotropic effects on phospholipid synthesis
    • N.M. Jani, and J.M. Lopes Regulated transcription of the Saccharomyces cerevisiae phosphatidylinositol biosynthetic gene, PIS1, yields pleiotropic effects on phospholipid synthesis FEMS Yeast Res. 9 2009 552 564
    • (2009) FEMS Yeast Res. , vol.9 , pp. 552-564
    • Jani, N.M.1    Lopes, J.M.2
  • 129
    • 79551592413 scopus 로고    scopus 로고
    • Pleiotropic corepressors Sin3 and Ssn6 interact with repressor Opi1 and negatively regulate transcription of genes required for phospholipid biosynthesis in the yeast Saccharomyces cerevisiae
    • Y. Jaschke, J. Schwarz, D. Clausnitzer, C. Muller, and H.J. Schuller Pleiotropic corepressors Sin3 and Ssn6 interact with repressor Opi1 and negatively regulate transcription of genes required for phospholipid biosynthesis in the yeast Saccharomyces cerevisiae Mol. Genet. Genomics 285 2011 91 100
    • (2011) Mol. Genet. Genomics , vol.285 , pp. 91-100
    • Jaschke, Y.1    Schwarz, J.2    Clausnitzer, D.3    Muller, C.4    Schuller, H.J.5
  • 130
    • 0034879653 scopus 로고    scopus 로고
    • Transcriptional regulation of the two sterol esterification genes in the yeast Saccharomyces cerevisiae
    • K. Jensen-Pergakes, Z. Guo, M. Giattina, S.L. Sturley, and M. Bard 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
  • 131
    • 78650658177 scopus 로고    scopus 로고
    • Interruption of inositol sphingolipid synthesis triggers Stt4p-dependent protein kinase C signaling
    • S.A. Jesch, M.L. Gaspar, C.J. Stefan, M.A. Aregullin, and S.A. Henry Interruption of inositol sphingolipid synthesis triggers Stt4p-dependent protein kinase C signaling J. Biol. Chem. 285 2010 41947 41960
    • (2010) J. Biol. Chem. , vol.285 , pp. 41947-41960
    • Jesch, S.A.1    Gaspar, M.L.2    Stefan, C.J.3    Aregullin, M.A.4    Henry, S.A.5
  • 132
    • 33747735581 scopus 로고    scopus 로고
    • Multiple endoplasmic reticulum-to-nucleus signaling pathways coordinate phospholipid metabolism with gene expression by distinct mechanisms
    • S.A. Jesch, P. Liu, X. Zhao, M.T. Wells, and S.A. Henry Multiple endoplasmic reticulum-to-nucleus signaling pathways coordinate phospholipid metabolism with gene expression by distinct mechanisms J. Biol. Chem. 281 2006 24070 24083
    • (2006) J. Biol. Chem. , vol.281 , pp. 24070-24083
    • Jesch, S.A.1    Liu, P.2    Zhao, X.3    Wells, M.T.4    Henry, S.A.5
  • 133
    • 15744368614 scopus 로고    scopus 로고
    • Genome-wide analysis reveals inositol, not choline, as the major effector of Ino2p-Ino4p and unfolded protein response target gene expression in yeast
    • S.A. Jesch, X. Zhao, M.T. Wells, and S.A. Henry Genome-wide analysis reveals inositol, not choline, as the major effector of Ino2p-Ino4p and unfolded protein response target gene expression in yeast J. Biol. Chem. 280 2005 9106 9118
    • (2005) J. Biol. Chem. , vol.280 , pp. 9106-9118
    • Jesch, S.A.1    Zhao, X.2    Wells, M.T.3    Henry, S.A.4
  • 134
    • 33747720764 scopus 로고    scopus 로고
    • Yeast inositol phospholipids: Synthesis, regulation and involvement in membrane trafficking and lipid signalling
    • G. Daum, Research Signpost Kerala, India
    • S.A. Jesch, and S.A. Henry Yeast inositol phospholipids: synthesis, regulation and involvement in membrane trafficking and lipid signalling G. Daum, Cell Biology and Dynamics of Yeast Lipids 2005 Research Signpost Kerala, India 105 131
    • (2005) Cell Biology and Dynamics of Yeast Lipids , pp. 105-131
    • Jesch, S.A.1    Henry, S.A.2
  • 135
    • 0038793610 scopus 로고    scopus 로고
    • Structures of NAD(+)- and NADH-bound 1-l-myo-inositol 1-phosphate synthase
    • X. Jin, and J.H. Geiger Structures of NAD(+)- and NADH-bound 1-l-myo-inositol 1-phosphate synthase Acta Crystallogr. D: Biol. Crystallogr. 59 2003 1154 1164
    • (2003) Acta Crystallogr. D: Biol. Crystallogr. , vol.59 , pp. 1154-1164
    • Jin, X.1    Geiger, J.H.2
  • 136
    • 0031733350 scopus 로고    scopus 로고
    • Pleiotropic effects of the opi1 regulatory mutation of yeast: Its effects on growth and on phospholipid and inositol metabolism
    • V. Jiranek, J.A. Graves, and S.A. Henry Pleiotropic effects of the opi1 regulatory mutation of yeast: its effects on growth and on phospholipid and inositol metabolism Microbiology 144 Pt 10 1998 2739 2748
    • (1998) Microbiology , vol.144 , Issue.PART 10 , pp. 2739-2748
    • Jiranek, V.1    Graves, J.A.2    Henry, S.A.3
  • 138
    • 2542422679 scopus 로고    scopus 로고
    • Human 1-d-myo-inositol-3-phosphate synthase is functional in yeast
    • S. Ju, G. Shaltiel, A. Shamir, G. Agam, and M.L. Greenberg Human 1-d-myo-inositol-3-phosphate synthase is functional in yeast J. Biol. Chem. 279 2004 21759 21765
    • (2004) J. Biol. Chem. , vol.279 , pp. 21759-21765
    • Ju, S.1    Shaltiel, G.2    Shamir, A.3    Agam, G.4    Greenberg, M.L.5
  • 139
    • 0343924289 scopus 로고    scopus 로고
    • Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters
    • D. Kadosh, and K. Struhl Repression by Ume6 involves recruitment of a complex containing Sin3 corepressor and Rpd3 histone deacetylase to target promoters Cell 89 1997 365 371
    • (1997) Cell , vol.89 , pp. 365-371
    • Kadosh, D.1    Struhl, K.2
  • 140
    • 0031865050 scopus 로고    scopus 로고
    • Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo
    • D. Kadosh, and K. Struhl Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo Mol. Cell. Biol. 18 1998 5121 5127
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5121-5127
    • Kadosh, D.1    Struhl, K.2
  • 141
    • 0031552996 scopus 로고    scopus 로고
    • The phospholipid methyltransferases in yeast
    • M.I. Kanipes, and S.A. Henry The phospholipid methyltransferases in yeast Biochim. Biophys. Acta 1348 1997 134 141
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 134-141
    • Kanipes, M.I.1    Henry, S.A.2
  • 143
    • 78049319504 scopus 로고    scopus 로고
    • A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase
    • E. Karanasios, G.S. Han, Z. Xu, G.M. Carman, and S. Siniossoglou A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase Proc. Natl. Acad. Sci. U.S.A. 107 2010 17539 17544
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17539-17544
    • Karanasios, E.1    Han, G.S.2    Xu, Z.3    Carman, G.M.4    Siniossoglou, S.5
  • 145
    • 0024279590 scopus 로고
    • Regulation of phospholipid biosynthesis in Saccharomyces cerevisiae by inositol. Inositol is an inhibitor of phosphatidylserine synthase activity
    • M.J. Kelley, A.M. Bailis, S.A. Henry, and G.M. Carman Regulation of phospholipid biosynthesis in Saccharomyces cerevisiae by inositol. Inositol is an inhibitor of phosphatidylserine synthase activity J. Biol. Chem. 263 1988 18078 18085
    • (1988) J. Biol. Chem. , vol.263 , pp. 18078-18085
    • Kelley, M.J.1    Bailis, A.M.2    Henry, S.A.3    Carman, G.M.4
  • 146
    • 0038349948 scopus 로고    scopus 로고
    • Sequencing and comparison of yeast species to identify genes and regulatory elements
    • M. Kellis, N. Patterson, M. Endrizzi, B. Birren, and E.S. Lander Sequencing and comparison of yeast species to identify genes and regulatory elements Nature 423 2003 241 254
    • (2003) Nature , vol.423 , pp. 241-254
    • Kellis, M.1    Patterson, N.2    Endrizzi, M.3    Birren, B.4    Lander, E.S.5
  • 147
    • 0033591224 scopus 로고    scopus 로고
    • Isolation and characterization of the Saccharomyces cerevisiae EKI1 gene encoding ethanolamine kinase
    • K. Kim, K.H. Kim, M.K. Storey, D.R. Voelker, and G.M. Carman Isolation and characterization of the Saccharomyces cerevisiae EKI1 gene encoding ethanolamine kinase J. Biol. Chem. 274 1999 14857 14866
    • (1999) J. Biol. Chem. , vol.274 , pp. 14857-14866
    • Kim, K.1    Kim, K.H.2    Storey, M.K.3    Voelker, D.R.4    Carman, G.M.5
  • 148
    • 0011330351 scopus 로고
    • Isolation of the yeast INO1 gene: Located on an autonomously replicating plasmid, the gene is fully regulated
    • L.S. Klig, and S.A. Henry Isolation of the yeast INO1 gene: located on an autonomously replicating plasmid, the gene is fully regulated Proc. Natl. Acad. Sci. U.S.A. 81 1984 3816 3820
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 3816-3820
    • Klig, L.S.1    Henry, S.A.2
  • 149
    • 0021848614 scopus 로고
    • Coordinate regulation of phospholipid biosynthesis in Saccharomyces cerevisiae: Pleiotropically constitutive opi1 mutant
    • L.S. Klig, M.J. Homann, G.M. Carman, and S.A. Henry Coordinate regulation of phospholipid biosynthesis in Saccharomyces cerevisiae: pleiotropically constitutive opi1 mutant J. Bacteriol. 162 1985 1135 1141
    • (1985) J. Bacteriol. , vol.162 , pp. 1135-1141
    • Klig, L.S.1    Homann, M.J.2    Carman, G.M.3    Henry, S.A.4
  • 150
    • 0023992943 scopus 로고
    • Saccharomyces cerevisiae mutant with a partial defect in the synthesis of CDP-diacylglycerol and altered regulation of phospholipid biosynthesis
    • L.S. Klig, M.J. Homann, S.D. Kohlwein, M.J. Kelley, S.A. Henry, and G.M. Carman Saccharomyces cerevisiae mutant with a partial defect in the synthesis of CDP-diacylglycerol and altered regulation of phospholipid biosynthesis J. Bacteriol. 170 1988 1878 1886
    • (1988) J. Bacteriol. , vol.170 , pp. 1878-1886
    • Klig, L.S.1    Homann, M.J.2    Kohlwein, S.D.3    Kelley, M.J.4    Henry, S.A.5    Carman, G.M.6
  • 151
    • 0023850946 scopus 로고
    • Isolation of the yeast INO4 gene, a positive regulator of phospholipid biosynthesis
    • L.S. Klig, D.K. Hoshizaki, and S.A. Henry Isolation of the yeast INO4 gene, a positive regulator of phospholipid biosynthesis Curr. Genet. 13 1988 7 14
    • (1988) Curr. Genet. , vol.13 , pp. 7-14
    • Klig, L.S.1    Hoshizaki, D.K.2    Henry, S.A.3
  • 152
    • 0026027643 scopus 로고
    • Identification of the upstream activation sequences responsible for the expression and regulation of the PEM1 and PEM2 genes encoding the enzymes of the phosphatidylethanolamine methylation pathway in Saccharomyces cerevisiae
    • T. Kodaki, K. Hosaka, J. Nikawa, and S. Yamashita Identification of the upstream activation sequences responsible for the expression and regulation of the PEM1 and PEM2 genes encoding the enzymes of the phosphatidylethanolamine methylation pathway in Saccharomyces cerevisiae J. Biochem. 109 1991 276 287
    • (1991) J. Biochem. , vol.109 , pp. 276-287
    • Kodaki, T.1    Hosaka, K.2    Nikawa, J.3    Yamashita, S.4
  • 153
    • 0026333918 scopus 로고
    • Functional analysis of the regulatory region of the yeast phosphatidylserine synthase gene, PSS
    • T. Kodaki, J. Nikawa, K. Hosaka, and S. Yamashita Functional analysis of the regulatory region of the yeast phosphatidylserine synthase gene, PSS J. Bacteriol. 173 1991 7992 7995
    • (1991) J. Bacteriol. , vol.173 , pp. 7992-7995
    • Kodaki, T.1    Nikawa, J.2    Hosaka, K.3    Yamashita, S.4
  • 154
    • 0142150117 scopus 로고    scopus 로고
    • Differential transcriptional regulation of two distinct S-adenosylmethionine synthetase genes (SAM1 and SAM2) of Saccharomyces cerevisiae
    • T. Kodaki, S. Tsuji, N. Otani, D. Yamamoto, K.S. Rao, S. Watanabe, M. Tsukatsune, and K. Makino Differential transcriptional regulation of two distinct S-adenosylmethionine synthetase genes (SAM1 and SAM2) of Saccharomyces cerevisiae Nucleic Acids Res. Suppl. 3 2003 303 304
    • (2003) Nucleic Acids Res. Suppl. , vol.3 , pp. 303-304
    • Kodaki, T.1    Tsuji, S.2    Otani, N.3    Yamamoto, D.4    Rao, K.S.5    Watanabe, S.6    Tsukatsune, M.7    Makino, K.8
  • 155
    • 0023656673 scopus 로고
    • Yeast phosphatidylethanolamine methylation pathway. Cloning and characterization of two distinct methyltransferase genes
    • T. Kodaki, and S. Yamashita Yeast phosphatidylethanolamine methylation pathway. Cloning and characterization of two distinct methyltransferase genes J. Biol. Chem. 262 1987 15428 15435
    • (1987) J. Biol. Chem. , vol.262 , pp. 15428-15435
    • Kodaki, T.1    Yamashita, S.2
  • 156
    • 0024415718 scopus 로고
    • Characterization of the methyltransferases in the yeast phosphatidylethanolamine methylation pathway by selective gene disruption
    • T. Kodaki, and S. Yamashita Characterization of the methyltransferases in the yeast phosphatidylethanolamine methylation pathway by selective gene disruption Eur. J. Biochem. 185 1989 243 251
    • (1989) Eur. J. Biochem. , vol.185 , pp. 243-251
    • Kodaki, T.1    Yamashita, S.2
  • 157
    • 77952331856 scopus 로고    scopus 로고
    • Triacylglycerol homeostasis: Insights from yeast
    • S.D. Kohlwein Triacylglycerol homeostasis: insights from yeast J. Biol. Chem. 285 2010 15663 15667
    • (2010) J. Biol. Chem. , vol.285 , pp. 15663-15667
    • Kohlwein, S.D.1
  • 158
    • 0027465942 scopus 로고
    • The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum
    • K. Kohno, K. Normington, J. Sambrook, M.J. Gething, and K. Mori The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum Mol. Cell. Biol. 13 1993 877 890
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 877-890
    • Kohno, K.1    Normington, K.2    Sambrook, J.3    Gething, M.J.4    Mori, K.5
  • 159
    • 0029894617 scopus 로고    scopus 로고
    • Functional characterization of the repeated UASINO element in the promoters of the INO1 and CHO2 genes of yeast
    • J. Koipally, B.P. Ashburner, N. Bachhawat, T. Gill, G. Hung, S.A. Henry, and J.M. Lopes Functional characterization of the repeated UASINO element in the promoters of the INO1 and CHO2 genes of yeast Yeast 12 1996 653 665
    • (1996) Yeast , vol.12 , pp. 653-665
    • Koipally, J.1    Ashburner, B.P.2    Bachhawat, N.3    Gill, T.4    Hung, G.5    Henry, S.A.6    Lopes, J.M.7
  • 160
    • 0026696627 scopus 로고
    • A novel transcription factor reveals a functional link between the RNA polymerase II CTD and TFIID
    • A.J. Koleske, S. Buratowski, M. Nonet, and R.A. Young A novel transcription factor reveals a functional link between the RNA polymerase II CTD and TFIID Cell 69 1992 883 894
    • (1992) Cell , vol.69 , pp. 883-894
    • Koleske, A.J.1    Buratowski, S.2    Nonet, M.3    Young, R.A.4
  • 161
    • 84870159094 scopus 로고    scopus 로고
    • Structural basis of the unfolded protein response
    • A. Korennykh, and P. Walter Structural basis of the unfolded protein response Annu. Rev. Cell Dev. Biol. 28 2012 251 277
    • (2012) Annu. Rev. Cell Dev. Biol. , vol.28 , pp. 251-277
    • Korennykh, A.1    Walter, P.2
  • 162
    • 0019074675 scopus 로고
    • Membrane mutants: A yeast mutant with a lesion in phosphatidylserine biosynthesis
    • L. Kovac, I. Gbelska, V. Poliachova, J. Subik, and V. Kovacova Membrane mutants: a yeast mutant with a lesion in phosphatidylserine biosynthesis Eur. J. Biochem. 111 1980 491 501
    • (1980) Eur. J. Biochem. , vol.111 , pp. 491-501
    • Kovac, L.1    Gbelska, I.2    Poliachova, V.3    Subik, J.4    Kovacova, V.5
  • 164
    • 58149308056 scopus 로고    scopus 로고
    • Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression
    • C.F. Kurat, H. Wolinski, J. Petschnigg, S. Kaluarachchi, B. Andrews, K. Natter, and S.D. Kohlwein Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 in yeast links lipolysis to cell-cycle progression Mol. Cell 33 2009 53 63
    • (2009) Mol. Cell , vol.33 , pp. 53-63
    • Kurat, C.F.1    Wolinski, H.2    Petschnigg, J.3    Kaluarachchi, S.4    Andrews, B.5    Natter, K.6    Kohlwein, S.D.7
  • 165
    • 0036649756 scopus 로고    scopus 로고
    • Genome-wide binding map of the histone deacetylase Rpd3 in yeast
    • S.K. Kurdistani, D. Robyr, S. Tavazoie, and M. Grunstein Genome-wide binding map of the histone deacetylase Rpd3 in yeast Nat. Genet. 31 2002 248 254
    • (2002) Nat. Genet. , vol.31 , pp. 248-254
    • Kurdistani, S.K.1    Robyr, D.2    Tavazoie, S.3    Grunstein, M.4
  • 166
    • 0028107569 scopus 로고
    • Dual control of inositol transport in Saccharomyces cerevisiae by irreversible inactivation of permease and regulation of permease synthesis by INO2, INO4, and OPI1
    • K. Lai, and P. McGraw Dual control of inositol transport in Saccharomyces cerevisiae by irreversible inactivation of permease and regulation of permease synthesis by INO2, INO4, and OPI1 J. Biol. Chem. 269 1994 2245 2251
    • (1994) J. Biol. Chem. , vol.269 , pp. 2245-2251
    • Lai, K.1    McGraw, P.2
  • 167
    • 0025951156 scopus 로고
    • Coordinate regulation of phosphatidylserine decarboxylase in Saccharomyces cerevisiae
    • E. Lamping, S.D. Kohlwein, S.A. Henry, and F. Paltauf Coordinate regulation of phosphatidylserine decarboxylase in Saccharomyces cerevisiae J. Bacteriol. 173 1991 6432 6437
    • (1991) J. Bacteriol. , vol.173 , pp. 6432-6437
    • Lamping, E.1    Kohlwein, S.D.2    Henry, S.A.3    Paltauf, F.4
  • 168
    • 0028331723 scopus 로고
    • Isolation and characterization of a mutant of Saccharomyces cerevisiae with pleiotropic deficiencies in transcriptional activation and repression
    • E. Lamping, J. Luckl, F. Paltauf, S.A. Henry, and S.D. Kohlwein Isolation and characterization of a mutant of Saccharomyces cerevisiae with pleiotropic deficiencies in transcriptional activation and repression Genetics 137 1994 55 65
    • (1994) Genetics , vol.137 , pp. 55-65
    • Lamping, E.1    Luckl, J.2    Paltauf, F.3    Henry, S.A.4    Kohlwein, S.D.5
  • 169
    • 77954889740 scopus 로고    scopus 로고
    • Surprising roles for phospholipid binding proteins revealed by high throughput genetics
    • M.A. LeBlanc, and C.R. McMaster Surprising roles for phospholipid binding proteins revealed by high throughput genetics Biochem. Cell Biol. 88 2010 565 574
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 565-574
    • Leblanc, M.A.1    McMaster, C.R.2
  • 170
    • 84884738162 scopus 로고    scopus 로고
    • Activation of protein kinase C-mitogen-activated protein kinase signaling in response to inositol starvation triggers Sir2p-dependent telomeric silencing in yeast
    • S. Lee, M.L. Gaspar, M.A. Aregullin, S.A. Jesch, and S.A. Henry Activation of protein kinase C-mitogen-activated protein kinase signaling in response to inositol starvation triggers Sir2p-dependent telomeric silencing in yeast J. Biol. Chem. 288 2013 27861 27871
    • (2013) J. Biol. Chem. , vol.288 , pp. 27861-27871
    • Lee, S.1    Gaspar, M.L.2    Aregullin, M.A.3    Jesch, S.A.4    Henry, S.A.5
  • 171
    • 0009363957 scopus 로고
    • Efficient method for selection of auxotrophic mutants of Neurospora
    • H.E. Lester, and S.R. Gross Efficient method for selection of auxotrophic mutants of Neurospora Science 129 1959 572
    • (1959) Science , vol.129 , pp. 572
    • Lester, H.E.1    Gross, S.R.2
  • 172
    • 0021878906 scopus 로고
    • Regulation of phospholipid synthesis in phosphatidylserine synthase-deficient (chol) mutants of Saccharomyces cerevisiae
    • V.A. Letts, and S.A. Henry Regulation of phospholipid synthesis in phosphatidylserine synthase-deficient (chol) mutants of Saccharomyces cerevisiae J. Bacteriol. 163 1985 560 567
    • (1985) J. Bacteriol. , vol.163 , pp. 560-567
    • Letts, V.A.1    Henry, S.A.2
  • 173
    • 0021089013 scopus 로고
    • Isolation of the yeast structural gene for the membrane-associated enzyme phosphatidylserine synthase
    • V.A. Letts, L.S. Klig, M. Bae-Lee, G.M. Carman, and S.A. Henry Isolation of the yeast structural gene for the membrane-associated enzyme phosphatidylserine synthase Proc. Natl. Acad. Sci. U.S.A. 80 1983 7279 7283
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 7279-7283
    • Letts, V.A.1    Klig, L.S.2    Bae-Lee, M.3    Carman, G.M.4    Henry, S.A.5
  • 174
    • 0025828308 scopus 로고
    • Hyper-resistance to nitrogen mustard in Saccharomyces cerevisiae is caused by defective choline transport
    • Z.Y. Li, E. Haase, and M. Brendel Hyper-resistance to nitrogen mustard in Saccharomyces cerevisiae is caused by defective choline transport Curr. Genet. 19 1991 423 427
    • (1991) Curr. Genet. , vol.19 , pp. 423-427
    • Li, Z.Y.1    Haase, E.2    Brendel, M.3
  • 176
    • 0038558194 scopus 로고    scopus 로고
    • A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP
    • C.J. Loewen, A. Roy, and T.P. Levine A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP EMBO J. 22 2003 2025 2035
    • (2003) EMBO J. , vol.22 , pp. 2025-2035
    • Loewen, C.J.1    Roy, A.2    Levine, T.P.3
  • 177
    • 0021689520 scopus 로고
    • The INO2 and INO4 loci of Saccharomyces cerevisiae are pleiotropic regulatory genes
    • B.S. Loewy, and S.A. Henry The INO2 and INO4 loci of Saccharomyces cerevisiae are pleiotropic regulatory genes Mol. Cell. Biol. 4 1984 2479 2485
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2479-2485
    • Loewy, B.S.1    Henry, S.A.2
  • 178
    • 0025880361 scopus 로고
    • Interaction of trans and cis regulatory elements in the INO1 promoter of Saccharomyces cerevisiae
    • J.M. Lopes, and S.A. Henry Interaction of trans and cis regulatory elements in the INO1 promoter of Saccharomyces cerevisiae Nucleic Acids Res. 19 1991 3987 3994
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3987-3994
    • Lopes, J.M.1    Henry, S.A.2
  • 179
    • 0025755893 scopus 로고
    • Analysis of sequences in the INO1 promoter that are involved in its regulation by phospholipid precursors
    • J.M. Lopes, J.P. Hirsch, P.A. Chorgo, K.L. Schulze, and S.A. Henry Analysis of sequences in the INO1 promoter that are involved in its regulation by phospholipid precursors Nucleic Acids Res. 19 1991 1687 1693
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1687-1693
    • Lopes, J.M.1    Hirsch, J.P.2    Chorgo, P.A.3    Schulze, K.L.4    Henry, S.A.5
  • 180
    • 0027321247 scopus 로고
    • The INO1 promoter of Saccharomyces cerevisiae includes an upstream repressor sequence (URS1) common to a diverse set of yeast genes
    • J.M. Lopes, K.L. Schulze, J.W. Yates, J.P. Hirsch, and S.A. Henry The INO1 promoter of Saccharomyces cerevisiae includes an upstream repressor sequence (URS1) common to a diverse set of yeast genes J. Bacteriol. 175 1993 4235 4238
    • (1993) J. Bacteriol. , vol.175 , pp. 4235-4238
    • Lopes, J.M.1    Schulze, K.L.2    Yates, J.W.3    Hirsch, J.P.4    Henry, S.A.5
  • 181
    • 66349102523 scopus 로고    scopus 로고
    • Phosphoinositide phosphatases and disease
    • P.W. Majerus, and J.D. York Phosphoinositide phosphatases and disease J. Lipid Res. 50 Suppl. 2009 S249 S254
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Majerus, P.W.1    York, J.D.2
  • 182
    • 0141682777 scopus 로고    scopus 로고
    • Diversification and evolution of L-myo-inositol 1-phosphate synthase
    • A.L. Majumder, A. Chatterjee, K. Ghosh Dastidar, and M. Majee Diversification and evolution of L-myo-inositol 1-phosphate synthase FEBS Lett. 553 2003 3 10
    • (2003) FEBS Lett. , vol.553 , pp. 3-10
    • Majumder, A.L.1    Chatterjee, A.2    Ghosh Dastidar, K.3    Majee, M.4
  • 184
    • 53049108345 scopus 로고    scopus 로고
    • S-adenosyl-l-homocysteine hydrolase, key enzyme of methylation metabolism, regulates phosphatidylcholine synthesis and triacylglycerol homeostasis in yeast: Implications for homocysteine as a risk factor of atherosclerosis
    • N. Malanovic, I. Streith, H. Wolinski, G. Rechberger, S.D. Kohlwein, and O. Tehlivets S-adenosyl-l-homocysteine hydrolase, key enzyme of methylation metabolism, regulates phosphatidylcholine synthesis and triacylglycerol homeostasis in yeast: implications for homocysteine as a risk factor of atherosclerosis J. Biol. Chem. 283 2008 23989 23999
    • (2008) J. Biol. Chem. , vol.283 , pp. 23989-23999
    • Malanovic, N.1    Streith, I.2    Wolinski, H.3    Rechberger, G.4    Kohlwein, S.D.5    Tehlivets, O.6
  • 185
    • 0024676686 scopus 로고
    • Mutations in the Saccharomyces cerevisiae opi3 gene: Effects on phospholipid methylation, growth and cross-pathway regulation of inositol synthesis
    • P. McGraw, and S.A. Henry Mutations in the Saccharomyces cerevisiae opi3 gene: effects on phospholipid methylation, growth and cross-pathway regulation of inositol synthesis Genetics 122 1989 317 330
    • (1989) Genetics , vol.122 , pp. 317-330
    • McGraw, P.1    Henry, S.A.2
  • 186
    • 0028077593 scopus 로고
    • Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory insights from studies employing null and chimeric sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases
    • C.R. McMaster, and R.M. Bell Phosphatidylcholine biosynthesis in Saccharomyces cerevisiae. Regulatory insights from studies employing null and chimeric sn-1,2-diacylglycerol choline- and ethanolaminephosphotransferases J. Biol. Chem. 269 1994 28010 28016
    • (1994) J. Biol. Chem. , vol.269 , pp. 28010-28016
    • McMaster, C.R.1    Bell, R.M.2
  • 187
    • 0028176089 scopus 로고
    • Phosphatidylcholine biosynthesis via the CDP-choline pathway in Saccharomyces cerevisiae. Multiple mechanisms of regulation
    • C.R. McMaster, and R.M. Bell Phosphatidylcholine biosynthesis via the CDP-choline pathway in Saccharomyces cerevisiae. Multiple mechanisms of regulation J. Biol. Chem. 269 1994 14776 14783
    • (1994) J. Biol. Chem. , vol.269 , pp. 14776-14783
    • McMaster, C.R.1    Bell, R.M.2
  • 188
    • 34547134940 scopus 로고    scopus 로고
    • Evolution of the diverse biological roles of inositols
    • R.H. Michell Evolution of the diverse biological roles of inositols Biochem. Soc. Symp. 74 2007 223 246
    • (2007) Biochem. Soc. Symp. , vol.74 , pp. 223-246
    • Michell, R.H.1
  • 189
    • 0028020126 scopus 로고
    • Studies employing Saccharomyces cerevisiae cpt1 and ept1 null mutants implicate the CPT1 gene in coordinate regulation of phospholipid biosynthesis
    • S.C. Morash, C.R. McMaster, R.H. Hjelmstad, and R.M. Bell Studies employing Saccharomyces cerevisiae cpt1 and ept1 null mutants implicate the CPT1 gene in coordinate regulation of phospholipid biosynthesis J. Biol. Chem. 269 1994 28769 28776
    • (1994) J. Biol. Chem. , vol.269 , pp. 28769-28776
    • Morash, S.C.1    McMaster, C.R.2    Hjelmstad, R.H.3    Bell, R.M.4
  • 190
    • 0027305620 scopus 로고
    • A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus
    • K. Mori, W. Ma, M.J. Gething, and J. Sambrook A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus Cell 74 1993 743 756
    • (1993) Cell , vol.74 , pp. 743-756
    • Mori, K.1    Ma, W.2    Gething, M.J.3    Sambrook, J.4
  • 191
    • 0034712734 scopus 로고    scopus 로고
    • MRNA splicing-mediated C-terminal replacement of transcription factor Hac1p is required for efficient activation of the unfolded protein response
    • K. Mori, N. Ogawa, T. Kawahara, H. Yanagi, and T. Yura mRNA splicing-mediated C-terminal replacement of transcription factor Hac1p is required for efficient activation of the unfolded protein response Proc. Natl. Acad. Sci. U.S.A. 97 2000 4660 4665
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 4660-4665
    • Mori, K.1    Ogawa, N.2    Kawahara, T.3    Yanagi, H.4    Yura, T.5
  • 192
    • 0026628290 scopus 로고
    • A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
    • K. Mori, A. Sant, K. Kohno, K. Normington, M.J. Gething, and J.F. Sambrook A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins EMBO J. 11 1992 2583 2593
    • (1992) EMBO J. , vol.11 , pp. 2583-2593
    • Mori, K.1    Sant, A.2    Kohno, K.3    Normington, K.4    Gething, M.J.5    Sambrook, J.F.6
  • 193
    • 3242790123 scopus 로고    scopus 로고
    • Dynamics of neutral lipid storage in yeast
    • H. Mullner, and G. Daum Dynamics of neutral lipid storage in yeast Acta Biochim. Pol. 51 2004 323 347
    • (2004) Acta Biochim. Pol. , vol.51 , pp. 323-347
    • Mullner, H.1    Daum, G.2
  • 194
    • 0030764899 scopus 로고    scopus 로고
    • Regulation of inositol monophosphatase in Saccharomyces cerevisiae
    • M. Murray, and M.L. Greenberg Regulation of inositol monophosphatase in Saccharomyces cerevisiae Mol. Microbiol. 25 1997 541 546
    • (1997) Mol. Microbiol. , vol.25 , pp. 541-546
    • Murray, M.1    Greenberg, M.L.2
  • 195
    • 0034018540 scopus 로고    scopus 로고
    • Expression of yeast INM1 encoding inositol monophosphatase is regulated by inositol, carbon source and growth stage and is decreased by lithium and valproate
    • M. Murray, and M.L. Greenberg Expression of yeast INM1 encoding inositol monophosphatase is regulated by inositol, carbon source and growth stage and is decreased by lithium and valproate Mol. Microbiol. 36 2000 651 661
    • (2000) Mol. Microbiol. , vol.36 , pp. 651-661
    • Murray, M.1    Greenberg, M.L.2
  • 196
    • 0029860982 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae IRE2/HAC1 is involved in IRE1-mediated KAR2 expression
    • J. Nikawa, M. Akiyoshi, S. Hirata, and T. Fukuda Saccharomyces cerevisiae IRE2/HAC1 is involved in IRE1-mediated KAR2 expression Nucleic Acids Res. 24 1996 4222 4226
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4222-4226
    • Nikawa, J.1    Akiyoshi, M.2    Hirata, S.3    Fukuda, T.4
  • 197
    • 0023214019 scopus 로고
    • Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae
    • J. Nikawa, T. Kodaki, and S. Yamashita Primary structure and disruption of the phosphatidylinositol synthase gene of Saccharomyces cerevisiae J. Biol. Chem. 262 1987 4876 4881
    • (1987) J. Biol. Chem. , vol.262 , pp. 4876-4881
    • Nikawa, J.1    Kodaki, T.2    Yamashita, S.3
  • 198
    • 0023658449 scopus 로고
    • Nucleotide sequence and characterization of the yeast PSS gene encoding phosphatidylserine synthase
    • J. Nikawa, Y. Tsukagoshi, T. Kodaki, and S. Yamashita Nucleotide sequence and characterization of the yeast PSS gene encoding phosphatidylserine synthase Eur. J. Biochem. 167 1987 7 12
    • (1987) Eur. J. Biochem. , vol.167 , pp. 7-12
    • Nikawa, J.1    Tsukagoshi, Y.2    Kodaki, T.3    Yamashita, S.4
  • 199
    • 0022447237 scopus 로고
    • Cloning of a gene encoding choline transport in Saccharomyces cerevisiae
    • J. Nikawa, Y. Tsukagoshi, and S. Yamashita Cloning of a gene encoding choline transport in Saccharomyces cerevisiae J. Bacteriol. 166 1986 328 330
    • (1986) J. Bacteriol. , vol.166 , pp. 328-330
    • Nikawa, J.1    Tsukagoshi, Y.2    Yamashita, S.3
  • 200
    • 0026710871 scopus 로고
    • IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae
    • J. Nikawa, and S. Yamashita IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae Mol. Microbiol. 6 1992 1441 1446
    • (1992) Mol. Microbiol. , vol.6 , pp. 1441-1446
    • Nikawa, J.1    Yamashita, S.2
  • 201
    • 0028174955 scopus 로고
    • Functional characterization of the INO2 gene of Saccharomyces cerevisiae. A positive regulator of phospholipid biosynthesis
    • D.M. Nikoloff, and S.A. Henry Functional characterization of the INO2 gene of Saccharomyces cerevisiae. A positive regulator of phospholipid biosynthesis J. Biol. Chem. 269 1994 7402 7411
    • (1994) J. Biol. Chem. , vol.269 , pp. 7402-7411
    • Nikoloff, D.M.1    Henry, S.A.2
  • 202
    • 0027126924 scopus 로고
    • The INO2 gene of Saccharomyces cerevisiae encodes a helix-loop-helix protein that is required for activation of phospholipid synthesis
    • D.M. Nikoloff, P. McGraw, and S.A. Henry The INO2 gene of Saccharomyces cerevisiae encodes a helix-loop-helix protein that is required for activation of phospholipid synthesis Nucleic Acids Res. 20 1992 3253
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3253
    • Nikoloff, D.M.1    McGraw, P.2    Henry, S.A.3
  • 203
    • 0024354605 scopus 로고
    • Intragenic and extragenic suppressors of mutations in the heptapeptide repeat domain of Saccharomyces cerevisiae RNA polymerase II
    • M.L. Nonet, and R.A. Young Intragenic and extragenic suppressors of mutations in the heptapeptide repeat domain of Saccharomyces cerevisiae RNA polymerase II Genetics 123 1989 715 724
    • (1989) Genetics , vol.123 , pp. 715-724
    • Nonet, M.L.1    Young, R.A.2
  • 204
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • P. Novick, C. Field, and R. Schekman Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway Cell 21 1980 205 215
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 205
    • 0000756130 scopus 로고
    • Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae
    • P. Novick, and R. Schekman Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae Proc. Natl. Acad. Sci. U.S.A. 76 1979 1858 1862
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 1858-1862
    • Novick, P.1    Schekman, R.2
  • 209
    • 0034717265 scopus 로고    scopus 로고
    • A lecithin cholesterol acyltransferase-like gene mediates diacylglycerol esterification in yeast
    • P. Oelkers, A. Tinkelenberg, N. Erdeniz, D. Cromley, J.T. Billheimer, and S.L. Sturley 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, J.T.5    Sturley, S.L.6
  • 210
    • 0034731465 scopus 로고    scopus 로고
    • Regulation of the DPP1-encoded diacylglycerol pyrophosphate (DGPP) phosphatase by inositol and growth phase. Inhibition of DGPP phosphatase activity by CDP-diacylglyceron and activation of phosphatidylserine synthase activity by DGPP
    • J. Oshiro, S. Rangaswamy, X. Chen, G.S. Han, J.E. Quinn, and G.M. Carman Regulation of the DPP1-encoded diacylglycerol pyrophosphate (DGPP) phosphatase by inositol and growth phase. Inhibition of DGPP phosphatase activity by CDP-diacylglyceron and activation of phosphatidylserine synthase activity by DGPP J. Biol. Chem. 275 2000 40887 40896
    • (2000) J. Biol. Chem. , vol.275 , pp. 40887-40896
    • Oshiro, J.1    Rangaswamy, S.2    Chen, X.3    Han, G.S.4    Quinn, J.E.5    Carman, G.M.6
  • 211
    • 0000600344 scopus 로고
    • Regulation and compartimentalization of lipid synthesis in yeast
    • J.R. Broach, J.R. Pringle, E.W. Jones, Cold Spring Harbor Press Plainview, NY
    • F.K. Paltauf, S.D. Kohlwein, and S.A. Henry Regulation and compartimentalization of lipid synthesis in yeast J.R. Broach, J.R. Pringle, E.W. Jones, The Molecular Biology of the Yeast Saccharomyces: Gene Expression 1992 Cold Spring Harbor Press Plainview, NY 415 500
    • (1992) The Molecular Biology of the Yeast Saccharomyces: Gene Expression , pp. 415-500
    • Paltauf, F.K.1    Kohlwein, S.D.2    Henry, S.A.3
  • 212
    • 84873197436 scopus 로고    scopus 로고
    • Phosphatidate phosphatase, a key regulator of lipid homeostasis
    • F. Pascual, and G.M. Carman Phosphatidate phosphatase, a key regulator of lipid homeostasis Biochim. Biophys. Acta 1831 2013 514 522
    • (2013) Biochim. Biophys. Acta , vol.1831 , pp. 514-522
    • Pascual, F.1    Carman, G.M.2
  • 213
    • 84890385726 scopus 로고    scopus 로고
    • PAH1-encoded phosphatidate phosphatase plays a role in the growth phase- and inositol-mediated regulation of lipid synthesis in Saccharomyces cerevisiae
    • F. Pascual, A. Soto-Cardalda, and G.M. Carman PAH1-encoded phosphatidate phosphatase plays a role in the growth phase- and inositol-mediated regulation of lipid synthesis in Saccharomyces cerevisiae J. Biol. Chem. 288 2013 35781 35792
    • (2013) J. Biol. Chem. , vol.288 , pp. 35781-35792
    • Pascual, F.1    Soto-Cardalda, A.2    Carman, G.M.3
  • 214
    • 0030861295 scopus 로고    scopus 로고
    • Role of the yeast phosphatidylinositol/phosphatidylcholine transfer protein (Sec14p) in phosphatidylcholine turnover and INO1 regulation
    • J.L. Patton-Vogt, P. Griac, A. Sreenivas, V. Bruno, S. Dowd, M.J. Swede, and S.A. Henry Role of the yeast phosphatidylinositol/phosphatidylcholine transfer protein (Sec14p) in phosphatidylcholine turnover and INO1 regulation J. Biol. Chem. 272 1997 20873 20883
    • (1997) J. Biol. Chem. , vol.272 , pp. 20873-20883
    • Patton-Vogt, J.L.1    Griac, P.2    Sreenivas, A.3    Bruno, V.4    Dowd, S.5    Swede, M.J.6    Henry, S.A.7
  • 215
    • 0035163850 scopus 로고    scopus 로고
    • Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin
    • M. Peterfy, J. Phan, P. Xu, and K. Reue Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin Nat. Genet. 27 2001 121 124
    • (2001) Nat. Genet. , vol.27 , pp. 121-124
    • Peterfy, M.1    Phan, J.2    Xu, P.3    Reue, K.4
  • 216
    • 0026584855 scopus 로고
    • Characterization of the yeast SWI1, SWI2, and SWI3 genes, which encode a global activator of transcription
    • C.L. Peterson, and I. Herskowitz Characterization of the yeast SWI1, SWI2, and SWI3 genes, which encode a global activator of transcription Cell 68 1992 573 583
    • (1992) Cell , vol.68 , pp. 573-583
    • Peterson, C.L.1    Herskowitz, I.2
  • 217
    • 80655136471 scopus 로고    scopus 로고
    • Survival of starving yeast is correlated with oxidative stress response and nonrespiratory mitochondrial function
    • A.A. Petti, C.A. Crutchfield, J.D. Rabinowitz, and D. Botstein Survival of starving yeast is correlated with oxidative stress response and nonrespiratory mitochondrial function Proc. Natl. Acad. Sci. U.S.A. 108 2011 E1089 E1098
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108
    • Petti, A.A.1    Crutchfield, C.A.2    Rabinowitz, J.D.3    Botstein, D.4
  • 218
    • 84864751060 scopus 로고    scopus 로고
    • Combinatorial control of diverse metabolic and physiological functions by transcriptional regulators of the yeast sulfur assimilation pathway
    • A.A. Petti, R.S. McIsaac, O. Ho-Shing, H.J. Bussemaker, and D. Botstein Combinatorial control of diverse metabolic and physiological functions by transcriptional regulators of the yeast sulfur assimilation pathway Mol. Biol. Cell 23 2012 3008 3024
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3008-3024
    • Petti, A.A.1    McIsaac, R.S.2    Ho-Shing, O.3    Bussemaker, H.J.4    Botstein, D.5
  • 219
    • 15944375261 scopus 로고    scopus 로고
    • Lipin, a lipodystrophy and obesity gene
    • J. Phan, and K. Reue Lipin, a lipodystrophy and obesity gene Cell Metab. 1 2005 73 83
    • (2005) Cell Metab. , vol.1 , pp. 73-83
    • Phan, J.1    Reue, K.2
  • 220
    • 77955023666 scopus 로고    scopus 로고
    • BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response
    • D. Pincus, M.W. Chevalier, T. Aragon, E. van Anken, S.E. Vidal, H. El-Samad, and P. Walter BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response PLoS Biol. 8 2010 e1000415
    • (2010) PLoS Biol. , vol.8 , pp. 1000415
    • Pincus, D.1    Chevalier, M.W.2    Aragon, T.3    Van Anken, E.4    Vidal, S.E.5    El-Samad, H.6    Walter, P.7
  • 221
    • 33947232747 scopus 로고    scopus 로고
    • Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae
    • M. Pittet, and A. Conzelmann Biosynthesis and function of GPI proteins in the yeast Saccharomyces cerevisiae Biochim. Biophys. Acta 1771 2007 405 420
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 405-420
    • Pittet, M.1    Conzelmann, A.2
  • 222
    • 0022998293 scopus 로고
    • Regulation of phosphatidylserine synthase from Saccharomyces cerevisiae by phospholipid precursors
    • M.A. Poole, M.J. Homann, M.S. Bae-Lee, and G.M. Carman Regulation of phosphatidylserine synthase from Saccharomyces cerevisiae by phospholipid precursors J. Bacteriol. 168 1986 668 672
    • (1986) J. Bacteriol. , vol.168 , pp. 668-672
    • Poole, M.A.1    Homann, M.J.2    Bae-Lee, M.S.3    Carman, G.M.4
  • 223
    • 80052825784 scopus 로고    scopus 로고
    • Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways
    • T. Promlek, Y. Ishiwata-Kimata, M. Shido, M. Sakuramoto, K. Kohno, and Y. Kimata Membrane aberrancy and unfolded proteins activate the endoplasmic reticulum stress sensor Ire1 in different ways Mol. Biol. Cell 22 2011 3520 3532
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3520-3532
    • Promlek, T.1    Ishiwata-Kimata, Y.2    Shido, M.3    Sakuramoto, M.4    Kohno, K.5    Kimata, Y.6
  • 224
    • 0027533267 scopus 로고
    • Cytosolic Sec13p complex is required for vesicle formation from the endoplasmic reticulum in vitro
    • N.K. Pryer, N.R. Salama, R. Schekman, and C.A. Kaiser Cytosolic Sec13p complex is required for vesicle formation from the endoplasmic reticulum in vitro J. Cell Biol. 120 1993 865 875
    • (1993) J. Cell Biol. , vol.120 , pp. 865-875
    • Pryer, N.K.1    Salama, N.R.2    Schekman, R.3    Kaiser, C.A.4
  • 225
    • 0037380112 scopus 로고    scopus 로고
    • Sir3p phosphorylation by the Slt2p pathway effects redistribution of silencing function and shortened lifespan
    • A. Ray, R.E. Hector, N. Roy, J.H. Song, K.L. Berkner, and K.W. Runge Sir3p phosphorylation by the Slt2p pathway effects redistribution of silencing function and shortened lifespan Nat. Genet. 33 2003 522 526
    • (2003) Nat. Genet. , vol.33 , pp. 522-526
    • Ray, A.1    Hector, R.E.2    Roy, N.3    Song, J.H.4    Berkner, K.L.5    Runge, K.W.6
  • 226
    • 0042402556 scopus 로고
    • Unbalanced growth of yeast due to inositol deficiency
    • G.J. Ridgway, and H.C. Douglas Unbalanced growth of yeast due to inositol deficiency J. Bacteriol. 76 1958 163 166
    • (1958) J. Bacteriol. , vol.76 , pp. 163-166
    • Ridgway, G.J.1    Douglas, H.C.2
  • 227
    • 0029897489 scopus 로고    scopus 로고
    • SPT20/ADA5 encodes a novel protein functionally related to the TATA-binding protein and important for transcription in Saccharomyces cerevisiae
    • S.M. Roberts, and F. Winston SPT20/ADA5 encodes a novel protein functionally related to the TATA-binding protein and important for transcription in Saccharomyces cerevisiae Mol. Cell. Biol. 16 1996 3206 3213
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3206-3213
    • Roberts, S.M.1    Winston, F.2
  • 228
    • 0034164664 scopus 로고    scopus 로고
    • Survey and summary: Saccharomyces cerevisiae basic helix-loop-helix proteins regulate diverse biological processes
    • K.A. Robinson, and J.M. Lopes Survey and summary: Saccharomyces cerevisiae basic helix-loop-helix proteins regulate diverse biological processes Nucleic Acids Res. 28 2000 1499 1505
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1499-1505
    • Robinson, K.A.1    Lopes, J.M.2
  • 229
    • 0027454503 scopus 로고
    • The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins
    • N.R. Salama, T. Yeung, and R.W. Schekman The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins EMBO J. 12 1993 4073 4082
    • (1993) EMBO J. , vol.12 , pp. 4073-4082
    • Salama, N.R.1    Yeung, T.2    Schekman, R.W.3
  • 230
    • 0034473817 scopus 로고    scopus 로고
    • An acyl-CoA:cholesterol acyltransferase (ACAT)-related gene is involved in the accumulation of triacylglycerols in Saccharomyces cerevisiae
    • L. Sandager, A. Dahlqvist, A. Banas, U. Stahl, M. Lenman, M. Gustavsson, and S. Stymne An acyl-CoA:cholesterol acyltransferase (ACAT)-related gene is involved in the accumulation of triacylglycerols in Saccharomyces cerevisiae Biochem. Soc. Trans. 28 2000 700 702
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 700-702
    • Sandager, L.1    Dahlqvist, A.2    Banas, A.3    Stahl, U.4    Lenman, M.5    Gustavsson, M.6    Stymne, S.7
  • 232
    • 0141866789 scopus 로고    scopus 로고
    • Genome expression analysis in yeast reveals novel transcriptional regulation by inositol and choline and new regulatory functions for Opi1p, Ino2p, and Ino4p
    • T.C. Santiago, and C.B. Mamoun Genome expression analysis in yeast reveals novel transcriptional regulation by inositol and choline and new regulatory functions for Opi1p, Ino2p, and Ino4p J. Biol. Chem. 278 2003 38723 38730
    • (2003) J. Biol. Chem. , vol.278 , pp. 38723-38730
    • Santiago, T.C.1    Mamoun, C.B.2
  • 233
    • 21244480972 scopus 로고    scopus 로고
    • The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth
    • H. Santos-Rosa, J. Leung, N. Grimsey, S. Peak-Chew, and S. Siniossoglou 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
  • 234
    • 0034670379 scopus 로고    scopus 로고
    • Identification of ISC1 (YER019w) as inositol phosphosphingolipid phospholipase C in Saccharomyces cerevisiae
    • H. Sawai, Y. Okamoto, C. Luberto, C. Mao, A. Bielawska, N. Domae, and Y.A. Hannun Identification of ISC1 (YER019w) as inositol phosphosphingolipid phospholipase C in Saccharomyces cerevisiae J. Biol. Chem. 275 2000 39793 39798
    • (2000) J. Biol. Chem. , vol.275 , pp. 39793-39798
    • Sawai, H.1    Okamoto, Y.2    Luberto, C.3    Mao, C.4    Bielawska, A.5    Domae, N.6    Hannun, Y.A.7
  • 235
    • 0025027915 scopus 로고
    • RNA polymerase II C-terminal repeat influences response to transcriptional enhancer signals
    • C. Scafe, D. Chao, J. Lopes, J.P. Hirsch, S. Henry, and R.A. Young RNA polymerase II C-terminal repeat influences response to transcriptional enhancer signals Nature 347 1990 491 494
    • (1990) Nature , vol.347 , pp. 491-494
    • Scafe, C.1    Chao, D.2    Lopes, J.3    Hirsch, J.P.4    Henry, S.5    Young, R.A.6
  • 236
    • 0026529044 scopus 로고
    • Coordinate genetic control of yeast fatty acid synthase genes FAS1 and FAS2 by an upstream activation site common to genes involved in membrane lipid biosynthesis
    • H.J. Schuller, A. Hahn, F. Troster, A. Schutz, and E. Schweizer Coordinate genetic control of yeast fatty acid synthase genes FAS1 and FAS2 by an upstream activation site common to genes involved in membrane lipid biosynthesis EMBO J. 11 1992 107 114
    • (1992) EMBO J. , vol.11 , pp. 107-114
    • Schuller, H.J.1    Hahn, A.2    Troster, F.3    Schutz, A.4    Schweizer, E.5
  • 237
    • 0026463938 scopus 로고
    • Regulatory gene INO4 of yeast phospholipid biosynthesis is positively autoregulated and functions as a transactivator of fatty acid synthase genes FAS1 and FAS2 from Saccharomyces cerevisiae
    • H.J. Schuller, R. Schorr, B. Hoffmann, and E. Schweizer Regulatory gene INO4 of yeast phospholipid biosynthesis is positively autoregulated and functions as a transactivator of fatty acid synthase genes FAS1 and FAS2 from Saccharomyces cerevisiae Nucleic Acids Res. 20 1992 5955 5961
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5955-5961
    • Schuller, H.J.1    Schorr, R.2    Hoffmann, B.3    Schweizer, E.4
  • 238
    • 0028963304 scopus 로고
    • Yeast transcriptional activator INO2 interacts as an Ino2p/Ino4p basic helix-loop-helix heteromeric complex with the inositol/choline-responsive element necessary for expression of phospholipid biosynthetic genes in Saccharomyces cerevisiae
    • S. Schwank, R. Ebbert, K. Rautenstrauss, E. Schweizer, and H.J. Schuller Yeast transcriptional activator INO2 interacts as an Ino2p/Ino4p basic helix-loop-helix heteromeric complex with the inositol/choline-responsive element necessary for expression of phospholipid biosynthetic genes in Saccharomyces cerevisiae Nucleic Acids Res. 23 1995 230 237
    • (1995) Nucleic Acids Res. , vol.23 , pp. 230-237
    • Schwank, S.1    Ebbert, R.2    Rautenstrauss, K.3    Schweizer, E.4    Schuller, H.J.5
  • 239
    • 0030897704 scopus 로고    scopus 로고
    • Regulation of phospholipid biosynthetic enzymes by the level of CDP-diacylglycerol synthase activity
    • H. Shen, and W. Dowhan Regulation of phospholipid biosynthetic enzymes by the level of CDP-diacylglycerol synthase activity J. Biol. Chem. 272 1997 11215 11220
    • (1997) J. Biol. Chem. , vol.272 , pp. 11215-11220
    • Shen, H.1    Dowhan, W.2
  • 240
    • 0032496232 scopus 로고    scopus 로고
    • Regulation of phosphatidylglycerophosphate synthase levels in Saccharomyces cerevisiae
    • H. Shen, and W. Dowhan Regulation of phosphatidylglycerophosphate synthase levels in Saccharomyces cerevisiae J. Biol. Chem. 273 1998 11638 11642
    • (1998) J. Biol. Chem. , vol.273 , pp. 11638-11642
    • Shen, H.1    Dowhan, W.2
  • 241
    • 0030023391 scopus 로고    scopus 로고
    • The CDS1 gene encoding CDP-diacylglycerol synthase in Saccharomyces cerevisiae is essential for cell growth
    • H. Shen, P.N. Heacock, C.J. Clancey, and W. Dowhan The CDS1 gene encoding CDP-diacylglycerol synthase in Saccharomyces cerevisiae is essential for cell growth J. Biol. Chem. 271 1996 789 795
    • (1996) J. Biol. Chem. , vol.271 , pp. 789-795
    • Shen, H.1    Heacock, P.N.2    Clancey, C.J.3    Dowhan, W.4
  • 242
    • 0042671282 scopus 로고    scopus 로고
    • Involvement of actin-related proteins in ATP-dependent chromatin remodeling
    • X. Shen, R. Ranallo, E. Choi, and C. Wu Involvement of actin-related proteins in ATP-dependent chromatin remodeling Mol. Cell 12 2003 147 155
    • (2003) Mol. Cell , vol.12 , pp. 147-155
    • Shen, X.1    Ranallo, R.2    Choi, E.3    Wu, C.4
  • 243
    • 0037414839 scopus 로고    scopus 로고
    • Modulation of ATP-dependent chromatin-remodeling complexes by inositol polyphosphates
    • X. Shen, H. Xiao, R. Ranallo, W.H. Wu, and C. Wu Modulation of ATP-dependent chromatin-remodeling complexes by inositol polyphosphates Science 299 2003 112 114
    • (2003) Science , vol.299 , pp. 112-114
    • Shen, X.1    Xiao, H.2    Ranallo, R.3    Wu, W.H.4    Wu, C.5
  • 244
    • 78649835399 scopus 로고    scopus 로고
    • Derepression of INO1 transcription requires cooperation between the Ino2p-Ino4p heterodimer and Cbf1p and recruitment of the ISW2 chromatin-remodeling complex
    • A. Shetty, and J.M. Lopes Derepression of INO1 transcription requires cooperation between the Ino2p-Ino4p heterodimer and Cbf1p and recruitment of the ISW2 chromatin-remodeling complex Eukaryot. Cell 9 2010 1845 1855
    • (2010) Eukaryot. Cell , vol.9 , pp. 1845-1855
    • Shetty, A.1    Lopes, J.M.2
  • 245
    • 0034898311 scopus 로고    scopus 로고
    • Inhibition of acetyl coenzyme A carboxylase activity restores expression of the INO1 gene in a snf1 mutant strain of Saccharomyces cerevisiae
    • M.K. Shirra, J. Patton-Vogt, A. Ulrich, O. Liuta-Tehlivets, S.D. Kohlwein, S.A. Henry, and K.M. Arndt Inhibition of acetyl coenzyme A carboxylase activity restores expression of the INO1 gene in a snf1 mutant strain of Saccharomyces cerevisiae Mol. Cell. Biol. 21 2001 5710 5722
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5710-5722
    • Shirra, M.K.1    Patton-Vogt, J.2    Ulrich, A.3    Liuta-Tehlivets, O.4    Kohlwein, S.D.5    Henry, S.A.6    Arndt, K.M.7
  • 246
    • 0030297538 scopus 로고    scopus 로고
    • TRNA ligase is required for regulated mRNA splicing in the unfolded protein response
    • C. Sidrauski, J.S. Cox, and P. Walter tRNA ligase is required for regulated mRNA splicing in the unfolded protein response Cell 87 1996 405 413
    • (1996) Cell , vol.87 , pp. 405-413
    • Sidrauski, C.1    Cox, J.S.2    Walter, P.3
  • 247
    • 0028906430 scopus 로고
    • The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity
    • H.B. Skinner, T.P. McGee, C.R. McMaster, M.R. Fry, R.M. Bell, and V.A. Bankaitis The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity Proc. Natl. Acad. Sci. U.S.A. 92 1995 112 116
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 112-116
    • Skinner, H.B.1    McGee, T.P.2    McMaster, C.R.3    Fry, M.R.4    Bell, R.M.5    Bankaitis, V.A.6
  • 248
    • 0036135597 scopus 로고    scopus 로고
    • Synthesis of triacylglycerols by the acyl-coenzyme A:diacyl-glycerol acyltransferase Dga1p in lipid particles of the yeast Saccharomyces cerevisiae
    • D. Sorger, and G. Daum Synthesis of triacylglycerols by the acyl-coenzyme A:diacyl-glycerol 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
  • 249
    • 0032479169 scopus 로고    scopus 로고
    • A role for phospholipase D (Pld1p) in growth, secretion, and regulation of membrane lipid synthesis in yeast
    • A. Sreenivas, J.L. Patton-Vogt, V. Bruno, P. Griac, and S.A. Henry A role for phospholipase D (Pld1p) in growth, secretion, and regulation of membrane lipid synthesis in yeast J. Biol. Chem. 273 1998 16635 16638
    • (1998) J. Biol. Chem. , vol.273 , pp. 16635-16638
    • Sreenivas, A.1    Patton-Vogt, J.L.2    Bruno, V.3    Griac, P.4    Henry, S.A.5
  • 251
    • 33947199781 scopus 로고    scopus 로고
    • Synthesis and function of membrane phosphoinositides in budding yeast, Saccharomyces cerevisiae
    • T. Strahl, and J. Thorner Synthesis and function of membrane phosphoinositides in budding yeast, Saccharomyces cerevisiae Biochim. Biophys. Acta 1771 2007 353 404
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 353-404
    • Strahl, T.1    Thorner, J.2
  • 252
    • 0031027431 scopus 로고    scopus 로고
    • SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast
    • S. Strahl-Bolsinger, A. Hecht, K. Luo, and M. Grunstein SIR2 and SIR4 interactions differ in core and extended telomeric heterochromatin in yeast Genes Dev. 11 1997 83 93
    • (1997) Genes Dev. , vol.11 , pp. 83-93
    • Strahl-Bolsinger, S.1    Hecht, A.2    Luo, K.3    Grunstein, M.4
  • 253
    • 0024256676 scopus 로고
    • Saccharomyces cerevisiae cho2 mutants are deficient in phospholipid methylation and cross-pathway regulation of inositol synthesis
    • E.F. Summers, V.A. Letts, P. McGraw, and S.A. Henry Saccharomyces cerevisiae cho2 mutants are deficient in phospholipid methylation and cross-pathway regulation of inositol synthesis Genetics 120 1988 909 922
    • (1988) Genetics , vol.120 , pp. 909-922
    • Summers, E.F.1    Letts, V.A.2    McGraw, P.3    Henry, S.A.4
  • 254
    • 0026553117 scopus 로고
    • Strategies for generating phospholipid synthesis mutants in yeast
    • M.J. Swede, K.A. Hudak, J.M. Lopes, and S.A. Henry Strategies for generating phospholipid synthesis mutants in yeast Methods Enzymol. 209 1992 21 34
    • (1992) Methods Enzymol. , vol.209 , pp. 21-34
    • Swede, M.J.1    Hudak, K.A.2    Lopes, J.M.3    Henry, S.A.4
  • 255
    • 8844247896 scopus 로고    scopus 로고
    • S-adenosyl-l-homocysteine hydrolase in yeast: Key enzyme of methylation metabolism and coordinated regulation with phospholipid synthesis
    • O. Tehlivets, M. Hasslacher, and S.D. Kohlwein S-adenosyl-l-homocysteine hydrolase in yeast: key enzyme of methylation metabolism and coordinated regulation with phospholipid synthesis FEBS Lett. 577 2004 501 506
    • (2004) FEBS Lett. , vol.577 , pp. 501-506
    • Tehlivets, O.1    Hasslacher, M.2    Kohlwein, S.D.3
  • 256
    • 0024267104 scopus 로고
    • SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: Physiology and regulation of both enzymes
    • D. Thomas, R. Rothstein, N. Rosenberg, and Y. Surdin-Kerjan SAM2 encodes the second methionine S-adenosyl transferase in Saccharomyces cerevisiae: physiology and regulation of both enzymes Mol. Cell. Biol. 8 1988 5132 5139
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5132-5139
    • Thomas, D.1    Rothstein, R.2    Rosenberg, N.3    Surdin-Kerjan, Y.4
  • 257
    • 0023646110 scopus 로고
    • SAM1, the structural gene for one of the S-adenosylmethionine synthetases in Saccharomyces cerevisiae. Sequence and expression
    • D. Thomas, and Y. Surdin-Kerjan SAM1, the structural gene for one of the S-adenosylmethionine synthetases in Saccharomyces cerevisiae. Sequence and expression J. Biol. Chem. 262 1987 16704 16709
    • (1987) J. Biol. Chem. , vol.262 , pp. 16704-16709
    • Thomas, D.1    Surdin-Kerjan, Y.2
  • 260
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • K.J. Travers, C.K. Patil, L. Wodicka, D.J. Lockhart, J.S. Weissman, and P. Walter Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation Cell 101 2000 249 258
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 261
    • 0027422574 scopus 로고
    • Phosphatidylserine decarboxylase from Saccharomyces cerevisiae. Isolation of mutants, cloning of the gene, and creation of a null allele
    • P.J. Trotter, J. Pedretti, and D.R. Voelker Phosphatidylserine decarboxylase from Saccharomyces cerevisiae. Isolation of mutants, cloning of the gene, and creation of a null allele J. Biol. Chem. 268 1993 21416 21424
    • (1993) J. Biol. Chem. , vol.268 , pp. 21416-21424
    • Trotter, P.J.1    Pedretti, J.2    Voelker, D.R.3
  • 262
    • 0028924622 scopus 로고
    • Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae. Cloning and mapping of the gene, heterologous expression, and creation of the null allele
    • P.J. Trotter, J. Pedretti, R. Yates, and D.R. Voelker Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae. Cloning and mapping of the gene, heterologous expression, and creation of the null allele J. Biol. Chem. 270 1995 6071 6080
    • (1995) J. Biol. Chem. , vol.270 , pp. 6071-6080
    • Trotter, P.J.1    Pedretti, J.2    Yates, R.3    Voelker, D.R.4
  • 263
    • 0028932671 scopus 로고
    • Identification of a non-mitochondrial phosphatidylserine decarboxylase activity (PSD2) in the yeast Saccharomyces cerevisiae
    • P.J. Trotter, and D.R. Voelker Identification of a non-mitochondrial phosphatidylserine decarboxylase activity (PSD2) in the yeast Saccharomyces cerevisiae J. Biol. Chem. 270 1995 6062 6070
    • (1995) J. Biol. Chem. , vol.270 , pp. 6062-6070
    • Trotter, P.J.1    Voelker, D.R.2
  • 264
    • 77955294401 scopus 로고    scopus 로고
    • Roles of inositol phosphates and inositol pyrophosphates in development, cell signaling and nuclear processes
    • M.M. Tsui, and J.D. York Roles of inositol phosphates and inositol pyrophosphates in development, cell signaling and nuclear processes Adv. Enzyme Regul. 50 2010 324 337
    • (2010) Adv. Enzyme Regul. , vol.50 , pp. 324-337
    • Tsui, M.M.1    York, J.D.2
  • 265
    • 79551583348 scopus 로고    scopus 로고
    • Genome-wide screen for inositol auxotrophy in Saccharomyces cerevisiae implicates lipid metabolism in stress response signaling
    • M.J. Villa-Garcia, M.S. Choi, F.I. Hinz, M.L. Gaspar, S.A. Jesch, and S.A. Henry Genome-wide screen for inositol auxotrophy in Saccharomyces cerevisiae implicates lipid metabolism in stress response signaling Mol. Genet. Genomics 285 2011 125 149
    • (2011) Mol. Genet. Genomics , vol.285 , pp. 125-149
    • Villa-Garcia, M.J.1    Choi, M.S.2    Hinz, F.I.3    Gaspar, M.L.4    Jesch, S.A.5    Henry, S.A.6
  • 266
    • 84875242776 scopus 로고    scopus 로고
    • Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains
    • R. Volmer, K. van der Ploeg, and D. Ron Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domains Proc. Natl. Acad. Sci. U.S.A. 110 2013 4628 4633
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 4628-4633
    • Volmer, R.1    Van Der Ploeg, K.2    Ron, D.3
  • 267
    • 0015024711 scopus 로고
    • Regulation of phosphatidylcholine biosynthesis in Saccharomyces cerevisiae
    • C.J. Waechter, and R.L. Lester Regulation of phosphatidylcholine biosynthesis in Saccharomyces cerevisiae J. Bacteriol. 105 1971 837 843
    • (1971) J. Bacteriol. , vol.105 , pp. 837-843
    • Waechter, C.J.1    Lester, R.L.2
  • 268
    • 0015802016 scopus 로고
    • Differential regulation of the N-methyl transferases responsible for phosphatidylcholine synthesis in Saccharomyces cerevisiae
    • C.J. Waechter, and R.L. Lester Differential regulation of the N-methyl transferases responsible for phosphatidylcholine synthesis in Saccharomyces cerevisiae Arch. Biochem. Biophys. 158 1973 401 410
    • (1973) Arch. Biochem. Biophys. , vol.158 , pp. 401-410
    • Waechter, C.J.1    Lester, R.L.2
  • 269
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • P. Walter, and D. Ron The unfolded protein response: from stress pathway to homeostatic regulation Science 334 2011 1081 1086
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 270
    • 84878393302 scopus 로고    scopus 로고
    • Inositol pyrophosphates: Between signalling and metabolism
    • M.S. Wilson, T.M. Livermore, and A. Saiardi Inositol pyrophosphates: between signalling and metabolism Biochem. J. 452 2013 369 379
    • (2013) Biochem. J. , vol.452 , pp. 369-379
    • Wilson, M.S.1    Livermore, T.M.2    Saiardi, A.3
  • 271
    • 0030032698 scopus 로고    scopus 로고
    • Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae
    • W.I. Wu, Y. Liu, B. Riedel, J.B. Wissing, A.S. Fischl, and G.M. Carman 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
  • 273
    • 0018902403 scopus 로고
    • Regulation of phosphatidylethanolamine methyltransferase level by myo-inositol in Saccaromyces cerevisiae
    • S. Yamashita, and A. Oshima Regulation of phosphatidylethanolamine methyltransferase level by myo-inositol in Saccaromyces cerevisiae Eur. J. Biochem. 104 1980 611 616
    • (1980) Eur. J. Biochem. , vol.104 , pp. 611-616
    • Yamashita, S.1    Oshima, A.2
  • 274
    • 84883141602 scopus 로고    scopus 로고
    • Regulation of inositol metabolism is fine-tuned by inositol pyrophosphates in Saccharomyces cerevisiae
    • C. Ye, W.M. Bandara, and M.L. Greenberg Regulation of inositol metabolism is fine-tuned by inositol pyrophosphates in Saccharomyces cerevisiae J. Biol. Chem. 288 2013 24898 24908
    • (2013) J. Biol. Chem. , vol.288 , pp. 24898-24908
    • Ye, C.1    Bandara, W.M.2    Greenberg, M.L.3
  • 275
    • 33745244227 scopus 로고    scopus 로고
    • Regulation of nuclear processes by inositol polyphosphates
    • J.D. York Regulation of nuclear processes by inositol polyphosphates Biochim. Biophys. Acta 1761 2006 552 559
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 552-559
    • York, J.D.1
  • 277
    • 2642587371 scopus 로고    scopus 로고
    • Neuropathy target esterase and its yeast homologue degrade phosphatidylcholine to glycerophosphocholine in living cells
    • O. Zaccheo, D. Dinsdale, P.A. Meacock, and P. Glynn Neuropathy target esterase and its yeast homologue degrade phosphatidylcholine to glycerophosphocholine in living cells J. Biol. Chem. 279 2004 24024 24033
    • (2004) J. Biol. Chem. , vol.279 , pp. 24024-24033
    • Zaccheo, O.1    Dinsdale, D.2    Meacock, P.A.3    Glynn, P.4


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