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Volumn 27, Issue 4, 2015, Pages 1251-1264

PHOSPHATIDIC ACID PHOSPHOHYDROLASE regulates phosphatidylcholine biosynthesis in arabidopsis by phosphatidic acid-mediated activation of CTP: PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE activityop

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 84928941991     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.15.00037     Document Type: Article
Times cited : (54)

References (76)
  • 2
    • 84862585031 scopus 로고    scopus 로고
    • Feedback regulation of plastidic acetyl-CoA carboxylase by 18:1-acyl carrier protein in Brassica napus
    • Andre, C., Haslam, R.P., and Shanklin, J. (2012). Feedback regulation of plastidic acetyl-CoA carboxylase by 18:1-acyl carrier protein in Brassica napus. Proc. Natl. Acad. Sci. USA 109: 10107–10112.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 10107-10112
    • Andre, C.1    Haslam, R.P.2    Shanklin, J.3
  • 3
    • 0029745175 scopus 로고    scopus 로고
    • Lipid regulation of CTP: Phosphocholine cytidylyltransferase: Electrostatic, hydrophobic, and synergistic interactions of anionic phospholipids and diac-ylglycerol
    • Arnold, R.S., and Cornell, R.B. (1996). Lipid regulation of CTP: phosphocholine cytidylyltransferase: electrostatic, hydrophobic, and synergistic interactions of anionic phospholipids and diac-ylglycerol. Biochemistry 35: 9917–9924.
    • (1996) Biochemistry , vol.35 , pp. 9917-9924
    • Arnold, R.S.1    Cornell, R.B.2
  • 4
    • 77956503704 scopus 로고    scopus 로고
    • Identification of phosphomethylethanol-amine N-methyltransferase from Arabidopsis and its role in choline and phospholipid metabolism
    • BeGora, M.D., Macleod, M.J., McCarry, B.E., Summers, P.S., and Weretilnyk, E.A. (2010). Identification of phosphomethylethanol-amine N-methyltransferase from Arabidopsis and its role in choline and phospholipid metabolism. J. Biol. Chem. 285: 29147–29155.
    • (2010) J. Biol. Chem , vol.285 , pp. 29147-29155
    • Begora, M.D.1    Macleod, M.J.2    McCarry, B.E.3    Summers, P.S.4    Weretilnyk, E.A.5
  • 5
    • 70450225230 scopus 로고    scopus 로고
    • Identification of hydrophobic amino acids required for lipid activation of C. Elegans CTP: Phosphocholine cytidylyltransferase
    • Braker, J.D., Hodel, K.J., Mullins, D.R., and Friesen, J.A. (2009). Identification of hydrophobic amino acids required for lipid activation of C. elegans CTP: phosphocholine cytidylyltransferase. Arch. Biochem. Biophys. 492: 10–16.
    • (2009) Arch. Biochem. Biophys , vol.492 , pp. 10-16
    • Braker, J.D.1    Hodel, K.J.2    Mullins, D.R.3    Friesen, J.A.4
  • 6
    • 0022608640 scopus 로고
    • Fatty acid composition of leaf lipids determined after combined digestion and fatty acid methyl ester formation from fresh tissue
    • Browse, J., McCourt, P.J., and Somerville, C.R. (1986). Fatty acid composition of leaf lipids determined after combined digestion and fatty acid methyl ester formation from fresh tissue. Anal. Biochem. 152: 141–145.
    • (1986) Anal. Biochem , vol.152 , pp. 141-145
    • Browse, J.1    McCourt, P.J.2    Somerville, C.R.3
  • 7
    • 59149106049 scopus 로고    scopus 로고
    • Phosphatidic acid phospha-tase, a key enzyme in the regulation of lipid synthesis
    • Carman, G.M., and Han, G.S. (2009). Phosphatidic acid phospha-tase, a key enzyme in the regulation of lipid synthesis. J. Biol. Chem. 284: 2593–2597.
    • (2009) J. Biol. Chem , vol.284 , pp. 2593-2597
    • Carman, G.M.1    Han, G.S.2
  • 8
    • 38049110718 scopus 로고    scopus 로고
    • Phosphatidic acid plays a central role in the transcriptional regulation of glycerophospholipid synthesis in Saccharomyces cerevisiae
    • Carman, G.M., and Henry, S.A. (2007). Phosphatidic acid plays a central role in the transcriptional regulation of glycerophospholipid synthesis in Saccharomyces cerevisiae. J. Biol. Chem. 282: 37293–37297.
    • (2007) J. Biol. Chem , vol.282 , pp. 37293-37297
    • Carman, G.M.1    Henry, S.A.2
  • 9
    • 0031588602 scopus 로고    scopus 로고
    • Cloning of CTP:Phos-phocholine cytidylyltransferase cDNA from Arabidopsis thaliana
    • Choi, S.-B., Lee, K.W., and Cho, S.H. (1997). Cloning of CTP:phos-phocholine cytidylyltransferase cDNA from Arabidopsis thaliana. Mol. Cells 7: 58–63.
    • (1997) Mol. Cells , vol.7 , pp. 58-63
    • Choi, S.-B.1    Lee, K.W.2    Cho, S.H.3
  • 10
    • 84859488188 scopus 로고    scopus 로고
    • Pho85p-Pho80p phosphorylation of yeast Pah1p phospha-tidate phosphatase regulates its activity, location, abundance, and function in lipid metabolism
    • Choi, H.S., Su, W.M., Han, G.S., Plote, D., Xu, Z., and Carman, G.M. (2012). Pho85p-Pho80p phosphorylation of yeast Pah1p phospha-tidate phosphatase regulates its activity, location, abundance, and function in lipid metabolism. J. Biol. Chem. 287: 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
  • 11
    • 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 phos-phorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase
    • Choi, H.S., Su, W.M., Morgan, J.M., Han, G.S., Xu, Z., Karanasios, E., Siniossoglou, S., and Carman, G.M. (2011). 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 phos-phorylated by CDC28 (CDK1)-encoded cyclin-dependent kinase. J. Biol. Chem. 286: 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
  • 12
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S.J., and Bent, A.F. (1998). Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16: 735–743.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 13
    • 0024364943 scopus 로고
    • Chemical cross-linking reveals a dimeric structure for CTP:Phosphocholine cytidylyltransferase
    • Cornell, R. (1989). Chemical cross-linking reveals a dimeric structure for CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 264: 9077–9082.
    • (1989) J. Biol. Chem , vol.264 , pp. 9077-9082
    • Cornell, R.1
  • 14
    • 0034284083 scopus 로고    scopus 로고
    • Regulation of CTP:Phos-phocholine cytidylyltransferase by amphitropism and relocalization
    • Cornell, R.B., and Northwood, I.C. (2000). Regulation of CTP:phos-phocholine cytidylyltransferase by amphitropism and relocalization. Trends Biochem. Sci. 25: 441–447.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 441-447
    • Cornell, R.B.1    Northwood, I.C.2
  • 16
    • 70350399460 scopus 로고    scopus 로고
    • A conserved serine residue is required for the phosphatidate phosphatase activity but not the transcriptional coactivator functions of lipin-1 and lipin-2
    • Donkor, J., Zhang, P., Wong, S., O’Loughlin, L., Dewald, J., Kok, B.P., Brindley, D.N., and Reue, K. (2009). A conserved serine residue is required for the phosphatidate phosphatase activity but not the transcriptional coactivator functions of lipin-1 and lipin-2. J. Biol. Chem. 284: 29968–29978.
    • (2009) J. Biol. Chem , vol.284 , pp. 29968-29978
    • Donkor, J.1    Zhang, P.2    Wong, S.3    O’Loughlin, L.4    Dewald, J.5    Kok, B.P.6    Brindley, D.N.7    Reue, K.8
  • 17
    • 0029410891 scopus 로고
    • Isolation and characterization of an Arabidopsis mutant deficient in the thylakoid lipid digalactosyl diacylglycerol
    • Dörmann, P., Hoffmann-Benning, S., Balbo, I., and Benning, C. (1995). Isolation and characterization of an Arabidopsis mutant deficient in the thylakoid lipid digalactosyl diacylglycerol. Plant Cell 7: 1801–1810.
    • (1995) Plant Cell , vol.7 , pp. 1801-1810
    • Dörmann, P.1    Hoffmann-Benning, S.2    Balbo, I.3    Benning, C.4
  • 18
  • 19
    • 8544238554 scopus 로고    scopus 로고
    • Cloning and characterization of the acid lipase from castor beans
    • Eastmond, P.J. (2004). Cloning and characterization of the acid lipase from castor beans. J. Biol. Chem. 279: 45540–45545.
    • (2004) J. Biol. Chem , vol.279 , pp. 45540-45545
    • Eastmond, P.J.1
  • 20
    • 77957762449 scopus 로고    scopus 로고
    • Phosphatidic acid phosphohydrolase 1 and 2 regulate phospholipid synthesis at the endoplasmic reticulum in Arabidopsis
    • Eastmond, P.J., Quettier, A.-L., Kroon, J.T., Craddock, C., Adams, N., and Slabas, A.R. (2010). Phosphatidic acid phosphohydrolase 1 and 2 regulate phospholipid synthesis at the endoplasmic reticulum in Arabidopsis. Plant Cell 22: 2796–2811.
    • (2010) Plant Cell , vol.22 , pp. 2796-2811
    • Eastmond, P.J.1    Quettier, A.-L.2    Kroon, J.T.3    Craddock, C.4    Adams, N.5    Slabas, A.R.6
  • 21
    • 77952088459 scopus 로고    scopus 로고
    • An overview of Cdk1-controlled targets and processes
    • Enserink, J.M., and Kolodner, R.D. (2010). An overview of Cdk1-controlled targets and processes. Cell Div. 5: 11.
    • (2010) Cell Div , vol.5 , pp. 11
    • Enserink, J.M.1    Kolodner, R.D.2
  • 22
    • 84912064540 scopus 로고    scopus 로고
    • Arabi-dopsis lipins, PDAT1 acyltransferase, and SDP1 triacylglycerol lipase synergistically direct fatty acids toward b-oxidation, thereby maintaining membrane lipid homeostasis
    • Fan, J., Yan, C., Roston, R., Shanklin, J., and Xu, C. (2014). Arabi-dopsis lipins, PDAT1 acyltransferase, and SDP1 triacylglycerol lipase synergistically direct fatty acids toward b-oxidation, thereby maintaining membrane lipid homeostasis. Plant Cell 26: 4119–4134.
    • (2014) Plant Cell , vol.26 , pp. 4119-4134
    • Fan, J.1    Yan, C.2    Roston, R.3    Shanklin, J.4    Xu, C.5
  • 23
    • 84886574266 scopus 로고    scopus 로고
    • Dual role for phos-pholipid:Diacylglycerol acyltransferase: Enhancing fatty acid synthesis and diverting fatty acids from membrane lipids to triacylglycerol in Arabidopsis leaves
    • Fan, J., Yan, C., Zhang, X., and Xu, C. (2013). Dual role for phos-pholipid:diacylglycerol acyltransferase: enhancing fatty acid synthesis and diverting fatty acids from membrane lipids to triacylglycerol in Arabidopsis leaves. Plant Cell 25: 3506–3518.
    • (2013) Plant Cell , vol.25 , pp. 3506-3518
    • Fan, J.1    Yan, C.2    Zhang, X.3    Xu, C.4
  • 25
    • 0033531947 scopus 로고    scopus 로고
    • Enzymatic and cellular characterization of a catalytic fragment of CTP:Phosphocholine cytidylyltransferase a
    • Friesen, J.A., Campbell, H.A., and Kent, C. (1999). Enzymatic and cellular characterization of a catalytic fragment of CTP:phosphocholine cytidylyltransferase a. J. Biol. Chem. 274: 13384–13389.
    • (1999) J. Biol. Chem , vol.274 , pp. 13384-13389
    • Friesen, J.A.1    Campbell, H.A.2    Kent, C.3
  • 26
    • 0035965005 scopus 로고    scopus 로고
    • Cloning and characterization of a lipid-activated CTP:Phosphocholine cytidylyltransferase from Caenorhabditis elegans: Identification of a 21-residue segment critical for lipid activation
    • Friesen, J.A., Liu, M.F., and Kent, C. (2001a). Cloning and characterization of a lipid-activated CTP:phosphocholine cytidylyltransferase from Caenorhabditis elegans: identification of a 21-residue segment critical for lipid activation. Biochim. Biophys. Acta 1533: 86–98.
    • (2001) Biochim. Biophys. Acta , vol.1533 , pp. 86-98
    • Friesen, J.A.1    Liu, M.F.2    Kent, C.3
  • 27
    • 0034951395 scopus 로고    scopus 로고
    • Purification and kinetic characterization of CTP:Phosphocholine cytidylyltransferase from Saccharomyces cerevisiae
    • Friesen, J.A., Park, Y.S., and Kent, C. (2001b). Purification and kinetic characterization of CTP:phosphocholine cytidylyltransferase from Saccharomyces cerevisiae. Protein Expr. Purif. 21: 141–148.
    • (2001) Protein Expr. Purif , vol.21 , pp. 141-148
    • Friesen, J.A.1    Park, Y.S.2    Kent, C.3
  • 28
    • 68949194442 scopus 로고    scopus 로고
    • Inactivation of the C. Elegans lipin homolog leads to ER disorganization and to defects in the breakdown and reassembly of the nuclear envelope
    • Golden, A., Liu, J., and Cohen-Fix, O. (2009). Inactivation of the C. elegans lipin homolog leads to ER disorganization and to defects in the breakdown and reassembly of the nuclear envelope. J. Cell Sci. 122: 1970–1978.
    • (2009) J. Cell Sci , vol.122 , pp. 1970-1978
    • Golden, A.1    Liu, J.2    Cohen-Fix, O.3
  • 29
    • 68949170697 scopus 로고    scopus 로고
    • Lipin is required for efficient breakdown of the nuclear envelope in Caenorhabditis elegans
    • Gorjánácz, M., and Mattaj, I.W. (2009). Lipin is required for efficient breakdown of the nuclear envelope in Caenorhabditis elegans. J. Cell Sci. 122: 1963–1969.
    • (2009) J. Cell Sci , vol.122 , pp. 1963-1969
    • Gorjánácz, M.1    Mattaj, I.W.2
  • 30
    • 0025288595 scopus 로고
    • Transport of phosphocholine in higher plant cells: 31P nuclear magnetic resonance studies
    • Gout, E., Bligny, R., Roby, C., and Douce, R. (1990). Transport of phosphocholine in higher plant cells: 31P nuclear magnetic resonance studies. Proc. Natl. Acad. Sci. USA 87: 4280–4283.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4280-4283
    • Gout, E.1    Bligny, R.2    Roby, C.3    Douce, R.4
  • 31
    • 37549018969 scopus 로고    scopus 로고
    • The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity
    • Han, G.S., Siniossoglou, S., and Carman, G.M. (2007). The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity. J. Biol. Chem. 282: 37026–37035.
    • (2007) J. Biol. Chem , vol.282 , pp. 37026-37035
    • Han, G.S.1    Siniossoglou, S.2    Carman, G.M.3
  • 32
    • 33646920976 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme
    • Han, G.S., Wu, W.I., and Carman, G.M. (2006). The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme. J. Biol. Chem. 281: 9210–9218.
    • (2006) J. Biol. Chem , vol.281 , pp. 9210-9218
    • Han, G.S.1    Wu, W.I.2    Carman, G.M.3
  • 33
    • 84876414053 scopus 로고    scopus 로고
    • The membrane-binding domain of an amphitropic enzyme suppresses catalysis by contact with an amphipathic helix flanking its active site
    • Huang, H.K., Taneva, S.G., Lee, J., Silva, L.P., Schriemer, D.C., and Cornell, R.B. (2013). The membrane-binding domain of an amphitropic enzyme suppresses catalysis by contact with an amphipathic helix flanking its active site. J. Mol. Biol. 425:1546–1564.
    • (2013) J. Mol. Biol , vol.425 , pp. 1546-1564
    • Huang, H.K.1    Taneva, S.G.2    Lee, J.3    Silva, L.P.4    Schriemer, D.C.5    Cornell, R.B.6
  • 34
    • 0036859482 scopus 로고    scopus 로고
    • Phosphatidyl-choline biosynthesis at low temperature: Differential expression of CTP: Phosphorylcholine cytidylyltransferase isogenes in Arabidopsis thaliana
    • Inatsugi, R., Nakamura, M., and Nishida, I. (2002). Phosphatidyl-choline biosynthesis at low temperature: differential expression of CTP: phosphorylcholine cytidylyltransferase isogenes in Arabidopsis thaliana. Plant Cell Physiol. 43: 1342–1350.
    • (2002) Plant Cell Physiol , vol.43 , pp. 1342-1350
    • Inatsugi, R.1    Nakamura, M.2    Nishida, I.3
  • 35
    • 70349847645 scopus 로고    scopus 로고
    • Isozyme-specific modes of activation of CTP:Phosphorylcholine cytidylyltransferase in Arabi-dopsis thaliana at low temperature
    • Inatsugi, R., Kawai, H., Yamaoka, Y., Yu, Y., Sekiguchi, A., Nakamura, M., and Nishida, I. (2009). Isozyme-specific modes of activation of CTP:phosphorylcholine cytidylyltransferase in Arabi-dopsis thaliana at low temperature. Plant Cell Physiol. 50: 1727–1735.
    • (2009) Plant Cell Physiol , vol.50 , pp. 1727-1735
    • Inatsugi, R.1    Kawai, H.2    Yamaoka, Y.3    Yu, Y.4    Sekiguchi, A.5    Nakamura, M.6    Nishida, I.7
  • 36
    • 12544260246 scopus 로고    scopus 로고
    • CTP:Phosphocholine cytidy-lyltransferase: Paving the way from gene to membrane
    • Jackowski, S., and Fagone, P. (2005). CTP:phosphocholine cytidy-lyltransferase: paving the way from gene to membrane. J. Biol. Chem. 280: 853–856.
    • (2005) J. Biol. Chem , vol.280 , pp. 853-856
    • Jackowski, S.1    Fagone, P.2
  • 37
    • 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
    • Jesch, S.A., Zhao, X., Wells, M.T., and Henry, S.A. (2005). 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: 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
  • 38
    • 0342444416 scopus 로고
    • GUS fusions: Beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson, R.A., Kavanagh, T.A., and Bevan, M.W. (1987). GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 6: 3901–3907.
    • (1987) EMBO J , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 39
    • 0026737180 scopus 로고
    • Comparison of the lipid regulation of yeast and rat CTP:Phosphocholine cytidylyltransferase expressed in COS cells.
    • Johnson, J.E., Kalmar, G.B., Sohal, P.S., Walkey, C.J., Yamashita, S., and Cornell, R.B. (1992). Comparison of the lipid regulation of yeast and rat CTP:phosphocholine cytidylyltransferase expressed in COS cells. Biochem. J. 285: 815–820.
    • (1992) Biochem. J , vol.285 , pp. 815-820
    • Johnson, J.E.1    Kalmar, G.B.2    Sohal, P.S.3    Walkey, C.J.4    Yamashita, S.5    Cornell, R.B.6
  • 40
    • 14644423932 scopus 로고    scopus 로고
    • Regulatory enzymes of phosphatidylcholine biosynthesis: A personal perspective
    • Kent, C. (2005). Regulatory enzymes of phosphatidylcholine biosynthesis: a personal perspective. Biochim. Biophys. Acta 1733: 53–66.
    • (2005) Biochim. Biophys. Acta , vol.1733 , pp. 53-66
    • Kent, C.1
  • 41
    • 67650129378 scopus 로고    scopus 로고
    • Functional characterization of phospholipid N-methyltransferases from Arabidopsis and soybean
    • Keogh, M.R., Courtney, P.D., Kinney, A.J., and Dewey, R.E. (2009). Functional characterization of phospholipid N-methyltransferases from Arabidopsis and soybean. J. Biol. Chem. 284: 15439–15447.
    • (2009) J. Biol. Chem , vol.284 , pp. 15439-15447
    • Keogh, M.R.1    Courtney, P.D.2    Kinney, A.J.3    Dewey, R.E.4
  • 42
    • 0023654195 scopus 로고
    • The regulation of phosphatidylcholine biosynthesis in rye (Secale cereale) roots. Stimulation of the nucleotide pathway by low temperature.
    • Kinney, A.J., Clarkson, D.T., and Loughman, B.C. (1987). The regulation of phosphatidylcholine biosynthesis in rye (Secale cereale) roots. Stimulation of the nucleotide pathway by low temperature. Biochem. J. 242: 755–759.
    • (1987) Biochem. J , vol.242 , pp. 755-759
    • Kinney, A.J.1    Clarkson, D.T.2    Loughman, B.C.3
  • 43
    • 0023656669 scopus 로고
    • Phosphatidylcholine synthesis in castor bean endosperm: The localization and control of CTP: Choline-phosphate cytidylyltransferase activity
    • Kinney, A.J., and Moore, T.S., Jr. (1987). Phosphatidylcholine synthesis in castor bean endosperm: the localization and control of CTP: choline-phosphate cytidylyltransferase activity. Arch. Bio-chem. Biophys. 259: 15–21.
    • (1987) Arch. Bio-Chem. Biophys , vol.259 , pp. 15-21
    • Kinney, A.J.1    Moore, T.S.2
  • 44
    • 78049319504 scopus 로고    scopus 로고
    • A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphati-date phosphatase
    • Karanasios, E., Han, G.S., Xu, Z., Carman, G.M., and Siniossoglou, S. (2010). A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphati-date phosphatase. Proc. Natl. Acad. Sci. USA 107: 17539–17544.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17539-17544
    • Karanasios, E.1    Han, G.S.2    Xu, Z.3    Carman, G.M.4    Siniossoglou, S.5
  • 45
    • 84892648364 scopus 로고    scopus 로고
    • Structural basis for autoinhibition of CTP:Phosphocholine cytidylyltransferase (CCT), the regulatory enzyme in phosphatidyl-choline synthesis, by its membrane-binding amphipathic helix
    • Lee, J., Taneva, S.G., Holland, B.W., Tieleman, D.P., and Cornell, R.B. (2014). Structural basis for autoinhibition of CTP:phosphocholine cytidylyltransferase (CCT), the regulatory enzyme in phosphatidyl-choline synthesis, by its membrane-binding amphipathic helix. J. Biol. Chem. 289: 1742–1755.
    • (2014) J. Biol. Chem , vol.289 , pp. 1742-1755
    • Lee, J.1    Taneva, S.G.2    Holland, B.W.3    Tieleman, D.P.4    Cornell, R.B.5
  • 46
    • 32544433476 scopus 로고    scopus 로고
    • EDGE: Extraction and analysis of differential gene expression
    • Leek, J.T., Monsen, E., Dabney, A.R., and Storey, J.D. (2006). EDGE: extraction and analysis of differential gene expression. Bioinformatics 22: 507–508.
    • (2006) Bioinformatics , vol.22 , pp. 507-508
    • Leek, J.T.1    Monsen, E.2    Dabney, A.R.3    Storey, J.D.4
  • 47
    • 77953219475 scopus 로고    scopus 로고
    • BZIP28 and NF-Y transcription factors are activated by ER stress and assemble into a transcrip-tional complex to regulate stress response genes in Arabidopsis
    • Liu, J.X., and Howell, S.H. (2010). bZIP28 and NF-Y transcription factors are activated by ER stress and assemble into a transcrip-tional complex to regulate stress response genes in Arabidopsis. Plant Cell 22: 782–796.
    • (2010) Plant Cell , vol.22 , pp. 782-796
    • Liu, J.X.1    Howell, S.H.2
  • 48
    • 2942677427 scopus 로고    scopus 로고
    • Phospholipid metabolism regulated by a transcription factor sensing phosphatidic acid
    • Loewen, C.J., Gaspar, M.L., Jesch, S.A., Delon, C., Ktistakis, N.T., Henry, S.A., and Levine, T.P. (2004). Phospholipid metabolism regulated by a transcription factor sensing phosphatidic acid. Science 304: 1644–1647.
    • (2004) Science , vol.304 , pp. 1644-1647
    • Loewen, C.J.1    Gaspar, M.L.2    Jesch, S.A.3    Delon, C.4    Ktistakis, N.T.5    Henry, S.A.6    Levine, T.P.7
  • 50
    • 79951904580 scopus 로고    scopus 로고
    • Lipins from plants are phosphatidate phosphatases that restore lipid synthesis in a pah1D mutant strain of Saccharomyces cerevisiae
    • Mietkiewska, E., Siloto, R.M., Dewald, J., Shah, S., Brindley, D.N., and Weselake, R.J. (2011). Lipins from plants are phosphatidate phosphatases that restore lipid synthesis in a pah1D mutant strain of Saccharomyces cerevisiae. FEBS J. 278: 764–775.
    • (2011) FEBS J , vol.278 , pp. 764-775
    • Mietkiewska, E.1    Siloto, R.M.2    Dewald, J.3    Shah, S.4    Brindley, D.N.5    Weselake, R.J.6
  • 51
    • 73949130073 scopus 로고    scopus 로고
    • Arabidopsis lipins mediate eukaryotic pathway of lipid metabolism and cope critically with phosphate starvation
    • Nakamura, Y., Koizumi, R., Shui, G., Shimojima, M., Wenk, M.R., Ito, T., and Ohta, H. (2009). Arabidopsis lipins mediate eukaryotic pathway of lipid metabolism and cope critically with phosphate starvation. Proc. Natl. Acad. Sci. USA 106: 20978–20983.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20978-20983
    • Nakamura, Y.1    Koizumi, R.2    Shui, G.3    Shimojima, M.4    Wenk, M.R.5    Ito, T.6    Ohta, H.7
  • 52
    • 0030152042 scopus 로고    scopus 로고
    • Cloning of Brassica napus CTP: Phosphocholine cytidylyltransfer-ase cDNAs by complementation in a yeast cct mutant
    • Nishida, I., Swinhoe, R., Slabas, A.R., and Murata, N. (1996). Cloning of Brassica napus CTP: phosphocholine cytidylyltransfer-ase cDNAs by complementation in a yeast cct mutant. Plant Mol. Biol. 31: 205–211.
    • (1996) Plant Mol. Biol , vol.31 , pp. 205-211
    • Nishida, I.1    Swinhoe, R.2    Slabas, A.R.3    Murata, N.4
  • 53
    • 33751256342 scopus 로고    scopus 로고
    • Control of phospholipid synthesis by phosphorylation of the yeast lipin Pah1p/Smp2p Mg2+-dependent phosphatidate phosphatase
    • O’Hara, L., Han, G.S., Peak-Chew, S., Grimsey, N., Carman, G.M., and Siniossoglou, S. (2006). Control of phospholipid synthesis by phosphorylation of the yeast lipin Pah1p/Smp2p Mg2+-dependent phosphatidate phosphatase. J. Biol. Chem. 281: 34537–34548.
    • (2006) J. Biol. Chem , vol.281 , pp. 34537-34548
    • O’Hara, L.1    Han, G.S.2    Peak-Chew, S.3    Grimsey, N.4    Carman, G.M.5    Siniossoglou, S.6
  • 54
    • 0029328579 scopus 로고
    • Lipid biosynthesis
    • Ohlrogge, J., and Browse, J. (1995). Lipid biosynthesis. Plant Cell 7: 957–970.
    • (1995) Plant Cell , vol.7 , pp. 957-970
    • Ohlrogge, J.1    Browse, J.2
  • 55
    • 20044394137 scopus 로고    scopus 로고
    • Functional genomic analysis of the AUXIN RESPONSE FACTOR gene family members in Arabidopsis thaliana: Unique and overlapping functions of ARF7 and ARF19
    • Okushima, Y., et al. (2005). Functional genomic analysis of the AUXIN RESPONSE FACTOR gene family members in Arabidopsis thaliana: unique and overlapping functions of ARF7 and ARF19. Plant Cell 17: 444–463.
    • (2005) Plant Cell , vol.17 , pp. 444-463
    • Okushima, Y.1
  • 56
    • 0032950673 scopus 로고    scopus 로고
    • Modulation of phosphatidyl-choline biosynthesis in celery by exogenous fatty acids
    • Parkin, E.T., and Rolph, C.E. (1999). Modulation of phosphatidyl-choline biosynthesis in celery by exogenous fatty acids. Phyto-chemistry 50: 47–51.
    • (1999) Phyto-Chemistry , vol.50 , pp. 47-51
    • Parkin, E.T.1    Rolph, C.E.2
  • 57
    • 84873197436 scopus 로고    scopus 로고
    • Phosphatidate phosphatase, a key regulator of lipid homeostasis
    • Pascual, F., and Carman, G.M. (2013). Phosphatidate phosphatase, a key regulator of lipid homeostasis. Biochim. Biophys. Acta 1831: 514–522.
    • (2013) Biochim. Biophys. Acta , vol.1831 , pp. 514-522
    • Pascual, F.1    Carman, G.M.2
  • 58
    • 0035163850 scopus 로고    scopus 로고
    • Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin
    • Péterfy, M., Phan, J., Xu, P., and Reue, K. (2001). Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin. Nat. Genet. 27: 121–124.
    • (2001) Nat. Genet , vol.27 , pp. 121-124
    • Péterfy, M.1    Phan, J.2    Xu, P.3    Reue, K.4
  • 59
    • 0021063119 scopus 로고
    • Hormonal regulation of phosphatidylcholine synthesis in plants. The inhibition of cytidylyl-transferase activity by indol-3-ylacetic acid
    • Price-Jones, M.J., and Harwood, J.L. (1983). Hormonal regulation of phosphatidylcholine synthesis in plants. The inhibition of cytidylyl-transferase activity by indol-3-ylacetic acid. Biochem. J. 216: 627–631.
    • (1983) Biochem. J , vol.216 , pp. 627-631
    • Price-Jones, M.J.1    Harwood, J.L.2
  • 60
    • 0023050919 scopus 로고
    • The control of CTP: Choline-phosphate cytidylyltransferase activity in pea (Pisum sat-ivum L.).
    • Price-Jones, M.J., and Harwood, J.L. (1986). The control of CTP: choline-phosphate cytidylyltransferase activity in pea (Pisum sat-ivum L.). Biochem. J. 240: 837–842.
    • (1986) Biochem. J. , vol.240 , pp. 837-842
    • Price-Jones, M.J.1    Harwood, J.L.2
  • 61
    • 0043172415 scopus 로고    scopus 로고
    • The SREBP pathway—insights from Insigs and insects
    • Rawson, R.B. (2003). The SREBP pathway—insights from Insigs and insects. Nat. Rev. Mol. Cell Biol. 4: 631–640.
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 631-640
    • Rawson, R.B.1
  • 62
    • 21244480972 scopus 로고    scopus 로고
    • The yeast lipin Smp2 couples phospho-lipid biosynthesis to nuclear membrane growth
    • Santos-Rosa, H., Leung, J., Grimsey, N., Peak-Chew, S., and Siniossoglou, S. (2005). The yeast lipin Smp2 couples phospho-lipid biosynthesis to nuclear membrane growth. EMBO J. 24: 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
  • 63
    • 0031170901 scopus 로고    scopus 로고
    • The plant ER: A dynamic organelle composed of a large number of discrete functional domains
    • Staehelin, L.A. (1997). The plant ER: a dynamic organelle composed of a large number of discrete functional domains. Plant J. 11: 1151–1165.
    • (1997) Plant J , vol.11 , pp. 1151-1165
    • Staehelin, L.A.1
  • 64
    • 84903830620 scopus 로고    scopus 로고
    • Cross-talk phos-phorylations by protein kinase C and Pho85p-Pho80p protein ki-nase regulate Pah1p phosphatidate phosphatase abundance in Saccharomyces cerevisiae
    • Su, W.M., Han, G.S., and Carman, G.M. (2014). Cross-talk phos-phorylations by protein kinase C and Pho85p-Pho80p protein ki-nase regulate Pah1p phosphatidate phosphatase abundance in Saccharomyces cerevisiae. J. Biol. Chem. 289: 18818–18830.
    • (2014) J. Biol. Chem , vol.289 , pp. 18818-18830
    • Su, W.M.1    Han, G.S.2    Carman, G.M.3
  • 65
    • 84866914709 scopus 로고    scopus 로고
    • Protein kinase A-mediated phosphorylation of Pah1p phosphatidate phos-phatase functions in conjunction with the Pho85p-Pho80p and Cdc28p-cyclin B kinases to regulate lipid synthesis in yeast
    • Su, W.M., Han, G.S., Casciano, J., and Carman, G.M. (2012). Protein kinase A-mediated phosphorylation of Pah1p phosphatidate phos-phatase functions in conjunction with the Pho85p-Pho80p and Cdc28p-cyclin B kinases to regulate lipid synthesis in yeast. J. Biol. Chem. 287: 33364–33376.
    • (2012) J. Biol. Chem , vol.287 , pp. 33364-33376
    • Su, W.M.1    Han, G.S.2    Casciano, J.3    Carman, G.M.4
  • 66
    • 40949100818 scopus 로고    scopus 로고
    • Transcriptional regulation of phosphatidylcholine biosynthesis
    • Sugimoto, H., Banchio, C., and Vance, D.E. (2008). Transcriptional regulation of phosphatidylcholine biosynthesis. Prog. Lipid Res. 47: 204–220.
    • (2008) Prog. Lipid Res , vol.47 , pp. 204-220
    • Sugimoto, H.1    Banchio, C.2    Vance, D.E.3
  • 67
    • 33749037973 scopus 로고    scopus 로고
    • Posttranscriptional regulation by the upstream open reading frame of the phosphoethanolamine N-methyltransferase gene
    • Tabuchi, T., Okada, T., Azuma, T., Nanmori, T., and Yasuda, T. (2006). Posttranscriptional regulation by the upstream open reading frame of the phosphoethanolamine N-methyltransferase gene. Biosci. Biotechnol. Biochem. 70: 2330–2334.
    • (2006) Biosci. Biotechnol. Biochem , vol.70 , pp. 2330-2334
    • Tabuchi, T.1    Okada, T.2    Azuma, T.3    Nanmori, T.4    Yasuda, T.5
  • 68
    • 2442570005 scopus 로고    scopus 로고
    • Regulation of phosphatidylcholine biosynthesis under salt stress involves choline kinases in Arabidopsis thaliana
    • Tasseva, G., Richard, L., and Zachowski, A. (2004). Regulation of phosphatidylcholine biosynthesis under salt stress involves choline kinases in Arabidopsis thaliana. FEBS Lett. 566: 115–120.
    • (2004) FEBS Lett , vol.566 , pp. 115-120
    • Tasseva, G.1    Richard, L.2    Zachowski, A.3
  • 69
    • 0028675642 scopus 로고
    • Signal transduction in yeast
    • Thevelein, J.M. (1994). Signal transduction in yeast. Yeast 10: 1753–1790.
    • (1994) Yeast , vol.10 , pp. 1753-1790
    • Thevelein, J.M.1
  • 70
    • 0027992029 scopus 로고
    • Over-expression of rat liver CTP:Phosphocholine cytidylyltransferase accelerates phosphatidylcholine synthesis and degradation
    • Walkey, C.J., Kalmar, G.B., and Cornell, R.B. (1994). Over-expression of rat liver CTP:phosphocholine cytidylyltransferase accelerates phosphatidylcholine synthesis and degradation. J. Biol. Chem. 269: 5742–5749.
    • (1994) J. Biol. Chem , vol.269 , pp. 5742-5749
    • Walkey, C.J.1    Kalmar, G.B.2    Cornell, R.B.3
  • 71
    • 84916627439 scopus 로고    scopus 로고
    • Deciphering the roles of Arabidopsis LPCAT and PAH in phosphatidylcholine homeostasis and pathway coordination for chloroplast lipid synthesis
    • Wang, L., Kazachkov, M., Shen, W., Bai, M., Wu, H., and Zou, J. (2014). Deciphering the roles of Arabidopsis LPCAT and PAH in phosphatidylcholine homeostasis and pathway coordination for chloroplast lipid synthesis. Plant J. 80: 965–976.
    • (2014) Plant J , vol.80 , pp. 965-976
    • Wang, L.1    Kazachkov, M.2    Shen, W.3    Bai, M.4    Wu, H.5    Zou, J.6
  • 72
    • 0029033139 scopus 로고
    • Identification of an inhibitory domain of CTP:Phosphocholine cytidylyltransferase
    • Wang, Y., and Kent, C. (1995). Identification of an inhibitory domain of CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 270: 18948–18952.
    • (1995) J. Biol. Chem , vol.270 , pp. 18948-18952
    • Wang, Y.1    Kent, C.2
  • 73
    • 0642284453 scopus 로고
    • Phosphatidylcholine biosynthesis in castor bean endosperm: Purification and properties of cytidine 59-triphosphate:Choline-phosphate cytidylyltransferase
    • Wang, X., and Moore, T.S. (1990). Phosphatidylcholine biosynthesis in castor bean endosperm: purification and properties of cytidine 59-triphosphate:choline-phosphate cytidylyltransferase. Plant Physiol. 93: 250–255.
    • (1990) Plant Physiol , vol.93 , pp. 250-255
    • Wang, X.1    Moore, T.S.2
  • 74
    • 0026052613 scopus 로고
    • Micro-somal CTP:Choline phosphate cytidylyltransferase: Kinetic mechanism of fatty acid stimulation
    • Weinhold, P.A., Charles, L.G., and Feldman, D.A. (1991). Micro-somal CTP:choline phosphate cytidylyltransferase: kinetic mechanism of fatty acid stimulation. Biochim. Biophys. Acta 1086: 57–62.
    • (1991) Biochim. Biophys. Acta , vol.1086 , pp. 57-62
    • Weinhold, P.A.1    Charles, L.G.2    Feldman, D.A.3
  • 75
    • 33646004283 scopus 로고    scopus 로고
    • Mutation of the TGD1 chloroplast envelope protein affects phos-phatidate metabolism in Arabidopsis
    • Xu, C., Fan, J., Froehlich, J.E., Awai, K., and Benning, C. (2005). Mutation of the TGD1 chloroplast envelope protein affects phos-phatidate metabolism in Arabidopsis. Plant Cell 17: 3094–3110.
    • (2005) Plant Cell , vol.17 , pp. 3094-3110
    • Xu, C.1    Fan, J.2    Froehlich, J.E.3    Awai, K.4    Benning, C.5
  • 76
    • 0028787406 scopus 로고
    • The association of lipid activators with the amphipathic helical domain of CTP:Phos-phocholine cytidylyltransferase accelerates catalysis by increasing the affinity of the enzyme for CTP
    • Yang, W., Boggs, K.P., and Jackowski, S. (1995). The association of lipid activators with the amphipathic helical domain of CTP:phos-phocholine cytidylyltransferase accelerates catalysis by increasing the affinity of the enzyme for CTP. J. Biol. Chem. 270: 23951–23957.
    • (1995) J. Biol. Chem , vol.270 , pp. 23951-23957
    • Yang, W.1    Boggs, K.P.2    Jackowski, S.3


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