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Volumn 61, Issue 2, 2009, Pages 151-162

Phosphatidylserine decarboxylases, key enzymes of lipid metabolism

Author keywords

Bacteria; Mammals; Phosphatidylethanolamine; Phosphatidylserine decarboxylase; Plant; Yeast

Indexed keywords

PHOSPHATIDYLSERINE DECARBOXYLASE; PROTEIN SUBUNIT; CARBOXYLYASE; PHOSPHATIDYLETHANOLAMINE;

EID: 63449135424     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.159     Document Type: Review
Times cited : (75)

References (100)
  • 1
    • 7444244325 scopus 로고    scopus 로고
    • Biogenesis and cellular dynamics of glycerophospholipids in the yeast Saccharomyces cerevisiae
    • Nebauer, R., Birner-Grünberger, R., and Daum, G. (2003) Biogenesis and cellular dynamics of glycerophospholipids in the yeast Saccharomyces cerevisiae. Top. Curr. Genet. 6, 125-168.
    • (2003) Top. Curr. Genet. , vol.6 , pp. 125-168
    • Nebauer, R.1    Birner-Grünberger, R.2    Daum, G.3
  • 2
    • 2342572271 scopus 로고    scopus 로고
    • Phospholipid synthesis in mammalian cells
    • Vance, J. E. and Vance, D. E. (2004) Phospholipid synthesis in mammalian cells. Biochem. Cell Biol. 82, 113-128.
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 113-128
    • Vance, J.E.1    Vance, D.E.2
  • 3
    • 0026664217 scopus 로고
    • Phosphatidylethanolamine is the donor of the ethanolamine residue linking a glycosylphosphatidylinositol anchor to protein
    • Menon, A. K. and Stevens, V. L. (1992) Phosphatidylethanolamine is the donor of the ethanolamine residue linking a glycosylphosphatidylinositol anchor to protein. J. Biol. Chem. 267, 15277-15280.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15277-15280
    • Menon, A.K.1    Stevens, V.L.2
  • 4
    • 33947532254 scopus 로고    scopus 로고
    • Discovery and characterization of a Ca2+-independent phosphtidylethanolamine N-acyltransferase generating the anandamide precursor and its congeners
    • Jin, X. H., Okamoto, Y., Morishita, J., Tsuboi, K., Tonai, T., and Ueda, N. (2007) Discovery and characterization of a Ca2+-independent phosphtidylethanolamine N-acyltransferase generating the anandamide precursor and its congeners. J. Biol. Chem. 282, 3614-3623.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3614-3623
    • Jin, X.H.1    Okamoto, Y.2    Morishita, J.3    Tsuboi, K.4    Tonai, T.5    Ueda, N.6
  • 6
    • 0037005133 scopus 로고    scopus 로고
    • Autophagy in yeast: A review of the molecular machinery
    • Huang, W. P. and Klionsky, D. J. (2002) Autophagy in yeast: a review of the molecular machinery. Cell. Struct. Funct. 27, 409-420.
    • (2002) Cell. Struct. Funct. , vol.27 , pp. 409-420
    • Huang, W.P.1    Klionsky, D.J.2
  • 7
    • 0033729495 scopus 로고    scopus 로고
    • Functional consequences of lipid packing stress
    • Bezrukov, S. M. (2000) Functional consequences of lipid packing stress. Curr. Opin. Colloid. Interface. Sci. 5, 237-243.
    • (2000) Curr. Opin. Colloid. Interface. Sci. , vol.5 , pp. 237-243
    • Bezrukov, S.M.1
  • 8
    • 0035803487 scopus 로고    scopus 로고
    • 1 complex structure
    • DOI 10.1093/emboj/20.23.6591
    • Lange, C., Nett, J. H., Trumpower, B. L., and Hunte, C. (2001) Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure. EMBO J. 20, 6591-6600. (Pubitemid 33134190)
    • (2001) EMBO Journal , vol.20 , Issue.23 , pp. 6591-6600
    • Lange, C.1    Nett, J.H.2    Trumpower, B.L.3    Hunte, C.4
  • 9
    • 0033665923 scopus 로고    scopus 로고
    • Emerging physiological roles for N-acylphosphatidylethanolamine metabolism in plants: Signal transduction and membrane protection
    • Chapman, K. D. (2000) Emerging physiological roles for N-acylphosphatidylethanolamine metabolism in plants: signal transduction and membrane protection. Chem. Phys. Lipids 108, 237-1230
    • (2000) Chem. Phys. Lipids , vol.108 , pp. 237-1230
    • Chapman, K.D.1
  • 10
    • 0035930634 scopus 로고    scopus 로고
    • Phosphatidylethanolamine has an essential role in Saccharomyces cerevisiae that is independent of its ability to form hexagonal phase structures
    • Storey, M. K., Clay, K. L., Kutateladze, T., Murphy, R. C., Overduin, M., and Voelker, D. R. (2001) Phosphatidylethanolamine has an essential role in Saccharomyces cerevisiae that is independent of its ability to form hexagonal phase structures. J. Biol. Chem. 276, 48539-48548.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48539-48548
    • Storey, M.K.1    Clay, K.L.2    Kutateladze, T.3    Murphy, R.C.4    Overduin, M.5    Voelker, D.R.6
  • 11
    • 34248996854 scopus 로고    scopus 로고
    • Lipids of yeast mitochondria
    • Rosenberger, S. and Daum, G. (2005) Lipids of yeast mitochondria. Res. Signpost 1735, 111-118.
    • (2005) Res. Signpost , vol.1735 , pp. 111-118
    • Rosenberger, S.1    Daum, G.2
  • 12
    • 28044469878 scopus 로고    scopus 로고
    • Phosphatidylserine decarboxylases as genetic and biochemical tools for studying phospholipid traffic
    • Choi, J. Y., Wu, W. I., and Voelker, D. R. (2005) Phosphatidylserine decarboxylases as genetic and biochemical tools for studying phospholipid traffic. Anal. Biochem. 347, 165-175.
    • (2005) Anal. Biochem. , vol.347 , pp. 165-175
    • Choi, J.Y.1    Wu, W.I.2    Voelker, D.R.3
  • 13
    • 0242693130 scopus 로고    scopus 로고
    • Bacterial membrane lipids. Where do we stand?
    • Cronan, J. E. (2003) Bacterial membrane lipids. Where do we stand? Annu. Rev. Microbiol. 57, 203-224.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 203-224
    • Cronan, J.E.1
  • 14
    • 50949084838 scopus 로고    scopus 로고
    • Phosphatidylserine and phosphatidylethanolamine in mammalian cells: Two metabolically-related aminophospholipids
    • Vance, J. E. (2008) Phosphatidylserine and phosphatidylethanolamine in mammalian cells: two metabolically-related aminophospholipids. J. Lipid Res. 49, 1377-1387.
    • (2008) J. Lipid Res. , vol.49 , pp. 1377-1387
    • Vance, J.E.1
  • 15
    • 11144305471 scopus 로고    scopus 로고
    • Phospholipid synthesis and dynamics in plant cells
    • Bessoule, J. J. and Moreau, P. (2004) Phospholipid synthesis and dynamics in plant cells. Top. Curr. Genet. 6, 89-124.
    • (2004) Top. Curr. Genet. , vol.6 , pp. 89-124
    • Bessoule, J.J.1    Moreau, P.2
  • 16
    • 33244479867 scopus 로고    scopus 로고
    • A study of archaeal enzymes involved in polar lipid synthesis linking amino acid sequence information, genomic contexts and lipid composition
    • Daiyasu, H., Kuma, K., Yokoi, T., Morii, H., Koga, Y., and Toh, H. (2005) A study of archaeal enzymes involved in polar lipid synthesis linking amino acid sequence information, genomic contexts and lipid composition. Archaea 1, 399-410. (Pubitemid 43273905)
    • (2005) Archaea , vol.1 , Issue.6 , pp. 399-410
    • Daiyasu, H.1    Kuma, K.-I.2    Yokoi, T.3    Morii, H.4    Koga, Y.5    Toh, H.6
  • 17
    • 0017403288 scopus 로고
    • Pyruvate-containing enzymes
    • Snell, E. E. (1977) Pyruvate-containing enzymes. Trends Biochem. Sci. 2, 131-135.
    • (1977) Trends Biochem. Sci. , vol.2 , pp. 131-135
    • Snell, E.E.1
  • 18
    • 0037269181 scopus 로고    scopus 로고
    • Biogenesis and cellular dynamics of aminoglycerophospholipids
    • Birner, R. and Daum, G. (2003) Biogenesis and cellular dynamics of aminoglycerophospholipids. Int. Rev. Cytol. 225, 273-323.
    • (2003) Int. Rev. Cytol. , vol.225 , pp. 273-323
    • Birner, R.1    Daum, G.2
  • 19
    • 2342597726 scopus 로고    scopus 로고
    • Genetic analysis of intracellular aminoglycero-phospholipid traffic
    • Voelker, D. R. (2004) Genetic analysis of intracellular aminoglycero-phospholipid traffic. Biochem. Cell Biol. 82, 165-169.
    • (2004) Biochem. Cell Biol. , vol.82 , pp. 165-169
    • Voelker, D.R.1
  • 20
    • 0038620481 scopus 로고    scopus 로고
    • New perspectives on the regulation of intermembrane glycerophospholipid traffic
    • DOI 10.1194/jlr.R200020-JLR200
    • Voelker, D. R. (2003) New perspectives on the regulation of intermembrane glycerophospholipid traffic. J. Lipid Res. 44, 441-449. (Pubitemid 37279690)
    • (2003) Journal of Lipid Research , vol.44 , Issue.3 , pp. 441-449
    • Voelker, D.R.1
  • 21
    • 21744445061 scopus 로고    scopus 로고
    • Bridging gaps in phospholipid transport
    • Voelker, D. R. (2005) Bridging gaps in phospholipid transport. Trends Biochem.Sci. 30, 396-404.
    • (2005) Trends Biochem.Sci. , vol.30 , pp. 396-404
    • Voelker, D.R.1
  • 22
    • 1542465944 scopus 로고    scopus 로고
    • Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism
    • Vance, J. E. (2003) Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism. Prog. Nucleic Acid Res. Mol. Biol. 75, 69-111.
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.75 , pp. 69-111
    • Vance, J.E.1
  • 24
    • 0002360622 scopus 로고
    • Enzymatic formation and decarboxylation of phosphatidylserine
    • Borkenhagen, L. F., Kennedy, E. P., and Fielding, L. (1961) Enzymatic formation and decarboxylation of phosphatidylserine. J. Biol. Chem. 236, 28-32.
    • (1961) J. Biol. Chem. , vol.236 , pp. 28-32
    • Borkenhagen, L.F.1    Kennedy, E.P.2    Fielding, L.3
  • 25
    • 0015470777 scopus 로고
    • Intracellular sites of lipid synthesis and the biogenesis of mitochondria
    • Dennis, E. A. and Kennedy, E. P. (1972) Intracellular sites of lipid synthesis and the biogenesis of mitochondria. J. Lipid Res. 13, 263-267.
    • (1972) J. Lipid Res. , vol.13 , pp. 263-267
    • Dennis, E.A.1    Kennedy, E.P.2
  • 26
    • 0025822140 scopus 로고
    • A cloned gene encoding phosphatidylserine decarboxylase complements the phosphatidylserine biosynthetic defect of a Chinese hamster ovary cell mutant
    • Kuge, O., Nishijima, M., and Akamatsu, Y. (1991) A cloned gene encoding phosphatidylserine decarboxylase complements the phosphatidylserine biosynthetic defect of a Chinese hamster ovary cell mutant. J. Biol. Chem. 266, 6370-6376.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6370-6376
    • Kuge, O.1    Nishijima, M.2    Akamatsu, Y.3
  • 28
    • 0020771208 scopus 로고
    • Characterization of brain phosphatidylserine decarboxylase: Localization in the mitochondrial inner membrane
    • Percy, A. K., Moore, J. F., Carson, M. A., and Waechter, C. J. (1983) Characterization of brain phosphatidylserine decarboxylase: localization in the mitochondrial inner membrane. Arch. Biochem. Biophys. 223, 484-494.
    • (1983) Arch. Biochem. Biophys. , vol.223 , pp. 484-494
    • Percy, A.K.1    Moore, J.F.2    Carson, M.A.3    Waechter, C.J.4
  • 29
    • 0020597859 scopus 로고
    • Phosphatidylserine decarboxylase is located on the external side of the inner mitochondrial membrane
    • DOI 10.1016/0014-5793(83)81141-7
    • Zborowski, J., Dygas, A., and Wojtczak, L. (1983) Phosphatidylserine decarboxylase is located on the external side of the inner mitochondrial membrane. FEBS Lett. 157, 179-182. (Pubitemid 13073606)
    • (1983) FEBS Letters , vol.157 , Issue.1 , pp. 179-182
    • Zborowski, J.1    Dygas, A.2    Wojtczak, L.3
  • 30
    • 0027423244 scopus 로고
    • Cloning of a gene (PSD1) encoding phosphatidylserine decarboxylase from Saccharomyces cerevisiae by complementation of an Escherichia coli mutant
    • Clancey, C. J., Chang, S.-C., and Dowhan, W. (1993) Cloning of a gene (PSD1) encoding phosphatidylserine decarboxylase from Saccharomyces cerevisiae by complementation of an Escherichia coli mutant. J. Biol. Chem. 268, 24580-24590.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24580-24590
    • Clancey, C.J.1    Chang, S.-C.2    Dowhan, W.3
  • 31
    • 0027422574 scopus 로고
    • Phosphatidylserine decarboxylase from Saccharomyces cerevisiae. Isolation of mutants, cloning of the gene, and creation of a null allele
    • Trotter, P. J., Pedretti, J., and Voelker, D. R. (1993) Phosphatidylserine decarboxylase from Saccharomyces cerevisiae. Isolation of mutants, cloning of the gene, and creation of a null allele. J. Biol. Chem. 268, 21416-21424.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21416-21424
    • Trotter, P.J.1    Pedretti, J.2    Voelker, D.R.3
  • 32
    • 0028924622 scopus 로고
    • Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae. Cloning and mapping of the gene, heterologous expression, and creation of the null allele
    • Trotter, P. J., Pedretti, J., Yates, R., and Voelker, D. R. (1995) Phosphatidylserine decarboxylase 2 of Saccharomyces cerevisiae. Cloning and mapping of the gene, heterologous expression, and creation of the null allele. J. Biol. Chem. 270, 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
  • 33
    • 0028932671 scopus 로고
    • Identification of a non-mitochondrial phosphatidylserine decarboxylase activity in the yeast Saccharomyces cerevisiae
    • Trotter, P. J. and Voelker, D. R. (1995) Identification of a non-mitochondrial phosphatidylserine decarboxylase activity in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 270, 6062-6070.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6062-6070
    • Trotter, P.J.1    Voelker, D.R.2
  • 34
    • 0031553041 scopus 로고    scopus 로고
    • Phosphatidylserine decarboxylase
    • Elsevier Pub. Co
    • Voelker, D. R. (1997) Phosphatidylserine decarboxylase. Biochim. Biophys. Acta. 1348, 236-244. Elsevier Pub. Co
    • (1997) Biochim. Biophys. Acta. , vol.1348 , pp. 236-244
    • Voelker, D.R.1
  • 35
    • 0026082909 scopus 로고
    • Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae
    • Zinser, E., Sperka-Gottlieb, C. D. M., Fasch, E.-V., Kohlwein, S. D., Paltauf, F., and Daum, G. (1991) Phospholipid synthesis and lipid composition of subcellular membranes in the unicellular eukaryote Saccharomyces cerevisiae. J. Bacteriol. 173, 2026-2034.
    • (1991) J. Bacteriol. , vol.173 , pp. 2026-2034
    • Zinser, E.1    Sperka-Gottlieb, C.D.M.2    Fasch, E.-V.3    Kohlwein, S.D.4    Paltauf, F.5    Daum, G.6
  • 36
    • 0037700594 scopus 로고    scopus 로고
    • Mitochondrial phosphatidylserine decarboxylase from higher plants. Functional complementation in yeast, localization in plants, and overexpression in Arabidopsis
    • Rontein, D., Wu, W.-I., Voelker, D. R., and Hanson, A. D. (2003) Mitochondrial phosphatidylserine decarboxylase from higher plants. Functional complementation in yeast, localization in plants, and overexpression in Arabidopsis. Plant Physiol. 132, 1678-1687.
    • (2003) Plant Physiol. , vol.132 , pp. 1678-1687
    • Rontein, D.1    Wu, W.-I.2    Voelker, D.R.3    Hanson, A.D.4
  • 37
    • 33746942727 scopus 로고    scopus 로고
    • A phosphatidylserine decarboxylase activity in root cells of oat (Avena sativa) is involved in altering membrane phospholipid composition during drought stress acclimation
    • Larsson, K. E., Nystrom, B., and Liljenberg, C. (2006) A phosphatidylserine decarboxylase activity in root cells of oat (Avena sativa) is involved in altering membrane phospholipid composition during drought stress acclimation. Plant Physiol. Biochem. 44, 211-219.
    • (2006) Plant Physiol. Biochem. , vol.44 , pp. 211-219
    • Larsson, K.E.1    Nystrom, B.2    Liljenberg, C.3
  • 38
    • 0016785971 scopus 로고
    • Biogenesis of membrane lipids: Mutants of Escherichia coli with temperature-sensitive phosphatidylserine decarboxylase
    • Hawrot, E. and Kennedy, E. P. (1975) Biogenesis of membrane lipids: mutants of Escherichia coli with temperature-sensitive phosphatidylserine decarboxylase. Proc. Natl. Acad. Sci. USA 72, 1112-1116.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1112-1116
    • Hawrot, E.1    Kennedy, E.P.2
  • 39
    • 0017147105 scopus 로고
    • Conditional lethal phosphatidylserine decarboxylase mutants of Escherichia coli. Mapping of the structural gene for phosphatidylserine decarboxylase
    • Hawrot, E. and Kennedy, E. P. (1976) Conditional lethal phosphatidylserine decarboxylase mutants of Escherichia coli. Mapping of the structural gene for phosphatidylserine decarboxylase. Mol. Gen. Genet. 148, 271-279.
    • (1976) Mol. Gen. Genet. , vol.148 , pp. 271-279
    • Hawrot, E.1    Kennedy, E.P.2
  • 40
    • 0001590175 scopus 로고
    • Metabolism and function of bacterial lipids. II. Biosynthesis of phospholipids in Escherichia coli
    • Kanfer, J. and Kennedy, E. P. (1964) Metabolism and function of bacterial lipids. II. Biosynthesis of phospholipids in Escherichia coli. J. Biol. Chem. 239, 1720-1726.
    • (1964) J. Biol. Chem. , vol.239 , pp. 1720-1726
    • Kanfer, J.1    Kennedy, E.P.2
  • 41
    • 0031983523 scopus 로고    scopus 로고
    • Cloning, sequencing, and disruption of the Bacillus subtilis psd gene coding for phosphatidylserine decarboxylase
    • Matsumoto, K., Okada, M., Horikoshi, Y., Matsuzaki, H., Kishi, T., Itaya, M., and Shibuya, I. (1998) Cloning, sequencing and disruption of the Bacillus subtilis psd gene coding for phosphatidylserine decarboxylase. J. Bacteriol. 180, 100-106. (Pubitemid 28023789)
    • (1998) Journal of Bacteriology , vol.180 , Issue.1 , pp. 100-106
    • Matsumoto, K.1    Okada, M.2    Horikoshi, Y.3    Matsuzaki, H.4    Kishi, T.5    Itaya, M.6    Shibuya, I.7
  • 42
    • 0016155281 scopus 로고
    • Purification and properties of phosphatidylserine decarboxylase from Escherichia coli
    • Dowhan, W., Wickner, W. T., and Kennedy, E. P. (1974) Purification and properties of phosphatidylserine decarboxylase from Escherichia coli. J. Biol. Chem. 249, 3079-3084.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3079-3084
    • Dowhan, W.1    Wickner, W.T.2    Kennedy, E.P.3
  • 43
    • 0015239109 scopus 로고
    • Studies on the membrane of bacilli. I. Phospholipid biosynthesis
    • Patterson, P. H. and Lennarz, W. J. (1971) Studies on the membrane of bacilli. I. Phospholipid biosynthesis. J. Biol. Chem. 246, 1062-1072.
    • (1971) J. Biol. Chem. , Issue.246 , pp. 1062-1072
    • Patterson, P.H.1    Lennarz, W.J.2
  • 44
    • 14644412812 scopus 로고    scopus 로고
    • Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes
    • DOI 10.1128/JB.187.6.2163-2174.2005
    • Nishibori, A., Kusaka, J., Hiroshi, H., Umeda, M., and Matsumoto, K. (2005) Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subitilis membranes. J. Bacteriol. 187, 2163-2174. (Pubitemid 40316247)
    • (2005) Journal of Bacteriology , vol.187 , Issue.6 , pp. 2163-2174
    • Nishibori, A.1    Kusaka, J.2    Hara, H.3    Umeda, M.4    Matsumoto, K.5
  • 45
    • 0021832504 scopus 로고
    • Phosphatidylserine decarboxylase from Clostridium butyricum
    • Verma, J. N. and Goldfine, H. (1985) Phosphatidylserine decarboxylase from Clostridium butyricum. J. Lipid Res. 26, 610-616.
    • (1985) J. Lipid Res. , vol.26 , pp. 610-616
    • Verma, J.N.1    Goldfine, H.2
  • 46
    • 0348225096 scopus 로고    scopus 로고
    • Characterization of a non-mitochondrial type I phosphatidylserine decarboxylase in Plasmodium falciparium
    • Baunaure, F., Eldin, P., Cathiard, A. M., and Vial, H. (2004) Characterization of a non-mitochondrial type I phosphatidylserine decarboxylase in Plasmodium falciparium. Mol. Microbiol. 51, 33-46.
    • (2004) Mol. Microbiol. , vol.51 , pp. 33-46
    • Baunaure, F.1    Eldin, P.2    Cathiard, A.M.3    Vial, H.4
  • 47
    • 34250681384 scopus 로고    scopus 로고
    • Deficiency in phosphatidylserine decarboxylase activity in the psd1 psd2 psd3 triple mutant of arabidopsis affects phosphatidylethanolamine accumulation in mitochondria
    • DOI 10.1104/pp.107.095414
    • Nerlich, A., von Orlow, M., Rontein, D., Hanson, A. D., and Dörmann, P. (2007) Deficiency in phosphatidylserine decarboxylase activity in the psd1 psd2 psd3 triple mutant of Arabidopsis affects phosphatidylethanolamine accumulation in mitochondria. Plant Physiol. 144, 904-914. (Pubitemid 46944753)
    • (2007) Plant Physiology , vol.144 , Issue.2 , pp. 904-914
    • Nerlich, A.1    Von Orlow, M.2    Rontein, D.3    Hanson, A.D.4    Dormann, P.5
  • 50
    • 0023762589 scopus 로고
    • Structural characterization of Escherichia coli phosphatidylserine decarboxylase
    • Li, Q. X. and Dowhan, W. (1988) Structural characterization of Escherichia coli phosphatidylserine decarboxylase. J. Biol. Chem. 263, 11516-11522.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11516-11522
    • Li, Q.X.1    Dowhan, W.2
  • 51
    • 0027984012 scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of the Bacillus subtilis gene for phosphatidylserine synthase
    • Okada, M., Matsuzaki, H., Shibuya, I., and Matsumoto, K. (1994) Cloning, sequencing, and expression in Escherichia coli of the Bacillus subitilis gene for phosphatidylserine synthase. J. Bacteriol. 176, 7456-7461. (Pubitemid 24382022)
    • (1994) Journal of Bacteriology , vol.176 , Issue.24 , pp. 7456-7461
    • Okada, M.1    Matsuzaki, H.2    Shibuya, I.3    Matsumoto, K.4
  • 52
    • 0029846065 scopus 로고    scopus 로고
    • Post-translational processing of the phosphatidylserine decarboxylase gene product in Chinese hamster ovary cells
    • Kuge, O., Saito, K., Kojima, M., Akamatsu, Y., and Nishijima, M. (1996) Post-translational processing of the phosphatidylserine decarboxylase gene product in Chinese hamster ovary cells. Biochem. J. 319, 33-38. (Pubitemid 26394736)
    • (1996) Biochemical Journal , vol.319 , Issue.1 , pp. 33-38
    • Kuge, O.1    Saito, K.2    Kojima, M.3    Akamatsu, Y.4    Nishijima, M.5
  • 53
    • 0028865692 scopus 로고
    • A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody localization of phopshatidylserine-specific binding sites on protein kinase C and phosphatidylserine decarboxylase
    • Igarashi, K., Kaneda, M., Yamaji, A., Saido, T. C., Kikkawa, U., Ono, Y. Inoue, K., and Umeda, M. (1995) A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody localization of phopshatidylserine-specific binding sites on protein kinase C and phosphatidylserine decarboxylase. J. Biol. Chem. 270, 29075-29078.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29075-29078
    • Igarashi, K.1    Kaneda, M.2    Yamaji, A.3    Saido, T.C.4    Kikkawa, U.5    Ono, Y.6    Inoue, K.7    Umeda, M.8
  • 54
    • 0037072811 scopus 로고    scopus 로고
    • The C2 domain of phosphatidylserine decarboxylase 2 is not required for catalysis but is essential for in vivo function
    • Kitamura, H., Wu, W. I., and Voelker, D. R. (2002) The C2 domain of phosphatidylserine decarboxylase 2 is not required for catalysis but is essential for in vivo function. J. Biol. Chem. 277, 33720-33726.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33720-33726
    • Kitamura, H.1    Wu, W.I.2    Voelker, D.R.3
  • 55
    • 0029774146 scopus 로고    scopus 로고
    • The protein import system of mitochondria
    • Schatz, G. (1996) The protein import system of mitochondria. J. Biol. Chem. 271, 31763-31766.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31763-31766
    • Schatz, G.1
  • 56
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Nalefski, E. A. and Falke, J. J. (1996) The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 5, 2375-2390. (Pubitemid 26424851)
    • (1996) Protein Science , vol.5 , Issue.12 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 57
    • 1542286172 scopus 로고    scopus 로고
    • The C2 domains of synaptotagmin - Partners in exocytosis
    • Bai, J. and Chapman, E. R. (2004) The C2 domains of synaptotagmin - partners in exocytosis. Trends Biochem. Sci. 29, 143-151.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 143-151
    • Bai, J.1    Chapman, E.R.2
  • 59
    • 0026519860 scopus 로고
    • Phosphatidylserine decarboxylase from Escherichia coli
    • Dowhan, W. and Li, Q. X. (1992) Phosphatidylserine decarboxylase from Escherichia coli. Methods Enzymol. 209, 348-359.
    • (1992) Methods Enzymol. , vol.209 , pp. 348-359
    • Dowhan, W.1    Li, Q.X.2
  • 60
    • 0025253340 scopus 로고
    • Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli
    • Li, Q. X. and Dowhan, W. (1990) Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli. J. Biol. Chem. 265, 4111-4115.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4111-4115
    • Li, Q.X.1    Dowhan, W.2
  • 61
    • 0019414633 scopus 로고
    • Kinetics and protein subunit interactions of Escherichia coli phosphatidylserine decarboxylase in detergent solution
    • Rizollo, L. J. (1981) Kinetics and protein subunit interactions of Escherichia coli phosphatidylserine decarboxylase in detergent solution. Biochemistry 20, 868-873.
    • (1981) Biochemistry , vol.20 , pp. 868-873
    • Rizollo, L.J.1
  • 62
    • 36249028597 scopus 로고    scopus 로고
    • The phosphatidylethanolamine level of yeast mitochondria is affected by the mitochondrial components Oxa1p and Yme1p
    • DOI 10.1111/j.1742-4658.2007.06138.x
    • Nebauer, R., Schuiki, I., Kulterer, B., Trajanoski, Z., and Daum, G. (2007) The phosphatidylethanolamine level of yeast mitochondria is affected by the mitochondrial components Oxa1p and Yme1p. FEBS J. 274, 6180-6190. (Pubitemid 350135337)
    • (2007) FEBS Journal , vol.274 , Issue.23 , pp. 6180-6190
    • Nebauer, R.1    Schuiki, I.2    Kulterer, B.3    Trajanoski, Z.4    Daum, G.5
  • 63
    • 0033607230 scopus 로고    scopus 로고
    • Isolation of Chinese hamster ovary cell mutant defective in intramitochondrial transport of phosphatidylserine
    • Emoto, K., Kuge, O., Nishijima, M., and Umeda, M. (1999) Isolation of Chinese hamster ovary cell mutant defective in intramitochondrial transport of phosphatidylserine. Proc. Natl. Acad. Sci. 96, 12400-12405.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 12400-12405
    • Emoto, K.1    Kuge, O.2    Nishijima, M.3    Umeda, M.4
  • 64
    • 0017836977 scopus 로고
    • Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli
    • Satre, M. and Kennedy, E. P. (1978) Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli. J. Biol. Chem. 253, 479-483.
    • (1978) J. Biol. Chem. , vol.253 , pp. 479-483
    • Satre, M.1    Kennedy, E.P.2
  • 65
    • 27844505245 scopus 로고    scopus 로고
    • Protein and lipid motifs regulate phosphatidylserine traffic in yeast
    • Voelker, D. R. (2005) Protein and lipid motifs regulate phosphatidylserine traffic in yeast. Biochem. Soc. Trans. 33, 1141-1145.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 1141-1145
    • Voelker, D.R.1
  • 66
    • 2642602889 scopus 로고
    • Steric course of the reaction catalyzed by phosphatidylserine decarboxylase from Escherichia coli
    • No, Z., Sanders C. R. II, Dowhan, W., and Tsai, M. (1988) Steric course of the reaction catalyzed by phosphatidylserine decarboxylase from Escherichia coli. Bioorg. Chem. 16, 184-188.
    • (1988) Bioorg. Chem. , vol.16 , pp. 184-188
    • No, Z.1    Sanders II, C.R.2    Dowhan, W.3    Tsai, M.4
  • 67
    • 0016698233 scopus 로고
    • Action of highly purified, membrane-bound enzyme phosphatidylserine decarboxylase Escherichia coli toward phosphatidylserine in mixed micelles and erythrocyte ghosts in the presence of surfactant
    • Warner, T. G. and Dennis, E. A. (1975) Action of highly purified, membrane-bound enzyme phosphatidylserine decarboxylase Escherichia coli toward phosphatidylserine in mixed micelles and erythrocyte ghosts in the presence of surfactant. J. Biol. Chem. 250, 8004-8009.
    • (1975) J. Biol. Chem. , vol.250 , pp. 8004-8009
    • Warner, T.G.1    Dennis, E.A.2
  • 68
    • 0026561696 scopus 로고
    • Phosphatidylserine decarboxylase from rat liver
    • Voelker, D. R. and Golden, E. B. (1992) Phosphatidylserine decarboxylase from rat liver. Methods Enzymol. 209, 360-365.
    • (1992) Methods Enzymol. , vol.209 , pp. 360-365
    • Voelker, D.R.1    Golden, E.B.2
  • 69
    • 7444256744 scopus 로고    scopus 로고
    • Contribution of different biosynthetic pathways to species selectivity of aminoglycerophospholipids assembled into mitochondrial membranes of the yeast Saccharomyces cerevisiae. Biochim
    • Bürgermeister, M., Birner-Grünberger, R., Heyn, M., and Daum, G. (2004) Contribution of different biosynthetic pathways to species selectivity of aminoglycerophospholipids assembled into mitochondrial membranes of the yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta. 1686, 148-160.
    • (2004) Biophys. Acta. , vol.1686 , pp. 148-160
    • Bürgermeister, M.1    Birner-Grünberger, R.2    Heyn, M.3    Daum, G.4
  • 70
    • 0032488996 scopus 로고    scopus 로고
    • Preferential decarboxylation of hydrophilic phosphatidylserine species in cultured cells. Implications on the mechanism of transport to mitochondria and cellular aminophospholipid species compositions
    • Heikinheimo, L. and Somerharju, P. (1998) Preferential decarboxylation of hydrophilic phosphatidylserine species in cultured cells. Implications on the mechanism of transport to mitochondria and cellular aminophospholipid species compositions. J. Biol. Chem. 273, 3327-3335.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3327-3335
    • Heikinheimo, L.1    Somerharju, P.2
  • 71
    • 0035336903 scopus 로고    scopus 로고
    • Determination of substrate preference in phosphatidylserine decarboxylation by liquid chromatography-electrospray ionization mass spectrometry
    • Kevala, J. H. and Kim, H.-Y. (2001) Determination of substrate preference in phosphatidylserine decarboxylation by liquid chromatography-electrospray ionization mass spectrometry. Anal. Biochem. 292, 130-138.
    • (2001) Anal. Biochem. , vol.292 , pp. 130-138
    • Kevala, J.H.1    Kim, H.-Y.2
  • 72
    • 35349002700 scopus 로고    scopus 로고
    • The CDP-ethanolamine pathway and phosphatidylserine decarboxylation generate different phosphatidylethanolamine molecular species
    • Bleijerveld, O. B., Brouwers, J. F. H. M., Vaandrager, A. B., Helms, J. B., and Houweling, M. (2007) The CDP-ethanolamine pathway and phosphatidylserine decarboxylation generate different phosphatidylethanolamine molecular species. J. Biol. Chem. 282, 28362-28372.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28362-28372
    • Bleijerveld, O.B.1    Brouwers, J.F.H.M.2    Vaandrager, A.B.3    Helms, J.B.4    Houweling, M.5
  • 73
    • 0037168471 scopus 로고    scopus 로고
    • Biosynthesis and trafficking of sphingolipids in the yeast Saccharomyces cerevisiae
    • DOI 10.1021/bi026616d
    • Funato, K., Valée, B., and Riezman, H. (2002) Biosynthesis and trafficking of sphingolipids in the yeast Saccharomyces cerevisiae. Biochemistry 41, 15105-15114. (Pubitemid 36008117)
    • (2002) Biochemistry , vol.41 , Issue.51 , pp. 15105-15114
    • Funato, K.1    Vallee, B.2    Riezman, H.3
  • 74
    • 0036217558 scopus 로고    scopus 로고
    • Phospholipid transfer protein
    • Van Tol, A. (2002) Phospholipid transfer protein. Curr. Opin. Lipidol. 13, 135-139.
    • (2002) Curr. Opin. Lipidol. , vol.13 , pp. 135-139
    • Van Tol, A.1
  • 75
    • 0034717835 scopus 로고    scopus 로고
    • Interorganelle transport of aminoglycerophospholipids
    • Voelker, D. R. (2000) Interorganelle transport of aminoglycerophospholipids. Biochim. Biophys. Acta. 1486, 97-107.
    • (2000) Biochim. Biophys. Acta. , vol.1486 , pp. 97-107
    • Voelker, D.R.1
  • 77
    • 0028105962 scopus 로고
    • Lipid transport processes in eukaryotic cells
    • Trotter, P. J. and Voelker, D. R. (1994) Lipid transport processes in eukaryotic cells. Biochim. Biophys. Acta 1213, 241-262.
    • (1994) Biochim. Biophys. Acta , vol.1213 , pp. 241-262
    • Trotter, P.J.1    Voelker, D.R.2
  • 78
    • 0033199506 scopus 로고    scopus 로고
    • Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact
    • Achleitner, G., Gaigg, B., Krasser, A., Kainersdorfer, E., Kohlwein, S. D., Perktold, A., Zellnig, G., and Daum, G. (1999) Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact. Eur. J. Biochem. 264, 545-553.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 545-553
    • Achleitner, G.1    Gaigg, B.2    Krasser, A.3    Kainersdorfer, E.4    Kohlwein, S.D.5    Perktold, A.6    Zellnig, G.7    Daum, G.8
  • 79
    • 0031470335 scopus 로고    scopus 로고
    • Import of lipids into mitochondria
    • Daum, G. and Vance, J. E. (1997) Import of lipids into mitochondria. Prog. Lipid Res. 36, 103-130.
    • (1997) Prog. Lipid Res. , vol.36 , pp. 103-130
    • Daum, G.1    Vance, J.E.2
  • 80
    • 0027377058 scopus 로고
    • Involvement of mitochondrial contact sites in the subcellular compartmentalization of phospholipid biosynthetic enzymes
    • Ardail, D., Gasnier, F., Lermé, F., Simonot, C., Louisot, P., and Gateau- Roesch, O. (1993) Involvement of mitochondrial contact sites in the subcellular compartmentalization of phospholipid biosynthetic enzymes. J. Biol. Chem. 268, 25985-25992.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25985-25992
    • Ardail, D.1    Gasnier, F.2    Lermé, F.3    Simonot, C.4    Louisot, P.5    Gateau- Roesch, O.6
  • 81
    • 0024847351 scopus 로고
    • Phosphatidylserine translocation to the mitochondrion is an ATP-dependent process in permeabilized animal cells
    • Voelker, D. R. (1989) Phosphatidylserine translocation to the mitochondrion is an ATP-dependent process in permeabilized animal cells. Proc. Natl. Acad. Sci. USA 86, 9921-9925.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9921-9925
    • Voelker, D.R.1
  • 82
    • 0029588529 scopus 로고
    • Synthesis and intracellular transport of aminoglycerophospholipids in permeabilized cells of the yeast, Saccharomyces cerevisiae
    • DOI 10.1074/jbc.270.50.29836
    • Achleitner, G., Zweytick, D., Trotter, P. J., Voelker, D. R., and Daum, G. (1995) Synthesis and intracellular transport of aminoglycerophospholipids in permeabilized cells of the yeast, Saccharomyces cerevisiae. J. Biol. Chem. 270, 29836-29842. (Pubitemid 26001655)
    • (1995) Journal of Biological Chemistry , vol.270 , Issue.50 , pp. 29836-29842
    • Achleitner, G.1    Zweytick, D.2    Trotter, P.J.3    Voelker, D.R.4    Daum, G.5
  • 83
    • 0037185026 scopus 로고    scopus 로고
    • Phosphatidylserine transport to the mitochondria is regulated by ubiquitination
    • Schumacher, M. M., Choi, J.-Y., and Voelker, D. R. (2002) Phosphatidylserine transport to the mitochondria is regulated by ubiquitination. J. Biol. Chem. 277, 51033-51042.
    • (2002) J. Biol. Chem. , vol.277 , pp. 51033-51042
    • Schumacher, M.M.1    Choi, J.-Y.2    Voelker, D.R.3
  • 84
    • 0032557556 scopus 로고    scopus 로고
    • A genetic screen for aminophospholipid transport mutants identifies the phosphatidylinositol 4-kinase, Stt4p, as an essential component in phosphatidylserine metabolism
    • Trotter, P. J., Wu, W. I., Pedretti, J., Yates, R., and Voelker, D. R. (1998) A genetic screen for aminophospholipid transport mutants identifies the phosphatidylinositol 4-kinase, Stt4p, as an essential component in phosphatidylserine metabolism. J. Biol. Chem. 273, 13189-13196.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13189-13196
    • Trotter, P.J.1    Wu, W.I.2    Pedretti, J.3    Yates, R.4    Voelker, D.R.5
  • 85
    • 0034640517 scopus 로고    scopus 로고
    • A new gene involved in the transport-dependent metabolism of phosphatidylserine, PSTB2/PDR17, shares sequence similarity with the gene encoding the phosphatidylinositol/phosphatidylcholine transfer protein
    • Wu, W. I., Routt, S., Bankaitis, V. A., and Voelker, D. R. (2000) A new gene involved in the transport-dependent metabolism of phosphatidylserine, PSTB2/PDR17, shares sequence similarity with the gene encoding the phosphatidylinositol/phosphatidylcholine transfer protein, SEC14. J. Biol. Chem. 275, 14446-14456.
    • (2000) SEC14. J. Biol. Chem. , vol.275 , pp. 14446-14456
    • Wu, W.I.1    Routt, S.2    Bankaitis, V.A.3    Voelker, D.R.4
  • 86
    • 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
  • 87
    • 0025946710 scopus 로고
    • Regulation of phosphatidylserine decarboxylase in Saccharomyces cerevisiae by inositol and choline: Kinetics of repression and derepression
    • Overmeyer, J. H. and Waechter, C. J. (1991) Regulation of phosphatidylserine decarboxylase in Saccharomyces cerevisiae by inositol and choline: kinetics of repression and derepression. Arch. Biochem. Biophys. 290, 511-516.
    • (1991) Arch. Biochem. Biophys. , vol.290 , pp. 511-516
    • Overmeyer, J.H.1    Waechter, C.J.2
  • 88
    • 0030884077 scopus 로고    scopus 로고
    • Regulation of yeast phospholipid biosynthetic genes in phosphatidylserine decarboxylase mutants
    • Griac, P. (1997) Regulation of yeast phospholipid biosynthetic genes in phosphatidylserine decarboxylase mutants. J. Bacteriol. 179, 5843-5848.
    • (1997) J. Bacteriol. , vol.179 , pp. 5843-5848
    • Griac, P.1
  • 89
    • 0025951156 scopus 로고
    • Coordinate regulation of phosphatidylserine decarboxylase in Saccharomyces cerevisiae
    • Lamping, E., Kohlwein, S. D., Henry, S. A., and Paltauf, F. (1991) Coordinate regulation of phosphatidylserine decarboxylase in Saccharomyces cerevisiae. J. Bacteriol. 173, 6432-6437.
    • (1991) J. Bacteriol. , vol.173 , pp. 6432-6437
    • Lamping, E.1    Kohlwein, S.D.2    Henry, S.A.3    Paltauf, F.4
  • 90
    • 2542418840 scopus 로고    scopus 로고
    • Regulation of phospholipid synthesis in Saccharomyces cerevisiae by zinc
    • Iwanyshyn, W. M., Han, G. S., and Carman, G. M. (2004) Regulation of phospholipid synthesis in Saccharomyces cerevisiae by zinc. J. Biol. Chem. 279, 21976-21983.
    • (2004) J. Biol. Chem. , vol.279 , pp. 21976-21983
    • Iwanyshyn, W.M.1    Han, G.S.2    Carman, G.M.3
  • 91
    • 0016785971 scopus 로고
    • Biogenesis of membrane lipids: Mutants of Escherichia coli with temperature-sensitive phosphatidylserine decarboxylase
    • Hawrot, E. and Kennedy, E. P. (1975) Biogenesis of membrane lipids: mutants of Escherichia coli with temperature-sensitive phosphatidylserine decarboxylase. Proc. Natl. Acad. Sci. USA 72, 1112-1116.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1112-1116
    • Hawrot, E.1    Kennedy, E.P.2
  • 92
    • 0018122198 scopus 로고
    • Phospholipid composition and membrane function in phosphatidylserine decarboxylase mutants of Escherichia coli
    • Hawrot, E. and Kennedy, E. P. (1978) Phospholipid composition and membrane function in phosphatidylserine decarboxylase mutants of Escherichia coli. J. Biol. Chem. 253, 8213-8220.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8213-8220
    • Hawrot, E.1    Kennedy, E.P.2
  • 93
    • 0035163738 scopus 로고    scopus 로고
    • Roles of phosphatidylethanolamine and of its several biosynthetic pathways in Saccharomyces cerevisiae
    • Birner, R., Bürgermeister, M., Schneiter, R., and Daum, G. (2001) Roles of phosphatidylethanolamine and of its several biosynthetic pathways in Saccharomyces cerevisiae. Mol. Biol. Cell 12, 997-1007.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 997-1007
    • Birner, R.1    Bürgermeister, M.2    Schneiter, R.3    Daum, G.4
  • 94
    • 0037328667 scopus 로고    scopus 로고
    • Synthetic lethal interaction of the mitochondrial phosphatidylethanolamine biosynthetic machinery with the prohibitin complex of Saccharomyces cerevisiae
    • Birner, R., Nebauer, R., Schneiter, R., and Daum, G. (2003) Synthetic lethal interaction of the mitochondrial phosphatidylethanolamine biosynthetic machinery with the prohibitin complex of Saccharomyces cerevisiae. Mol. Biol. Cell 14, 370-383.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 370-383
    • Birner, R.1    Nebauer, R.2    Schneiter, R.3    Daum, G.4
  • 95
    • 28844440297 scopus 로고    scopus 로고
    • Disruption of the phosphatidylserine decarboxylase gene in mice causes embryonic lethality and mitochondrial defects
    • Steenbergen, R., Nanowski, T. S., Beigneux, A., Kulinski, A., Young, S. G., and Vance, J. E. (2005) Disruption of the phosphatidylserine decarboxylase gene in mice causes embryonic lethality and mitochondrial defects. J. Biol. Chem. 280, 40032-40040.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40032-40040
    • Steenbergen, R.1    Nanowski, T.S.2    Beigneux, A.3    Kulinski, A.4    Young, S.G.5    Vance, J.E.6
  • 96
    • 0025881880 scopus 로고
    • Sequence and inactivation of the pss gene of Escherichia coli. Phosphatidylethanolamine may not be essential for cell viability
    • DeChavigny, A., Heacock, P. N., and Dowhan, W. (1991) Sequence and inactivation of the pss gene of Escherichia coli. Phosphatidylethanolamine may not be essential for cell viability. J. Biol. Chem. 266, 5323-5332.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5323-5332
    • Dechavigny, A.1    Heacock, P.N.2    Dowhan, W.3
  • 97
    • 0030019119 scopus 로고    scopus 로고
    • A regulatory mechanism for the balanced synthesis of membrane phospholipid species in Escherichia coli
    • Saha, S. K., Nishijama, S., Matsuzaki, H., Shibuya, I., and Matsumoto, K. (1996) A regulatory mechanism for the balanced synthesis of membrane phospholipid species in Escherichia coli. Biosci. Biotechnol. Biochem. 60, 111-116.
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 111-116
    • Saha, S.K.1    Nishijama, S.2    Matsuzaki, H.3    Shibuya, I.4    Matsumoto, K.5
  • 98
    • 33745860369 scopus 로고    scopus 로고
    • Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease
    • Xie, J., Bogdanov, M., Heacock, P., and Dowhan, W. (2006) Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease. J. Biol. Chem. 281, 19172-19178.
    • (2006) J. Biol. Chem. , vol.281 , pp. 19172-19178
    • Xie, J.1    Bogdanov, M.2    Heacock, P.3    Dowhan, W.4
  • 99
    • 0027016461 scopus 로고
    • Malarial lipids. An overview
    • Vial, H. and Ancelin, M. L. (1992) Malarial lipids. An overview. Subcell Biochem. 18, 259-306.
    • (1992) Subcell Biochem. , vol.18 , pp. 259-306
    • Vial, H.1    Ancelin, M.L.2
  • 100
    • 52649131910 scopus 로고    scopus 로고
    • Evidence for the bifunctional nature of mitochondrial phosphatiylserine decarboxylase: Role in Pdr3-dependent retrograde regulation of PDR5 expression
    • Gulshan, K., Schmidt, J. A., Shahi, P., and Moye-Rowley, W. S. (2008) Evidence for the bifunctional nature of mitochondrial phosphatiylserine decarboxylase: role in Pdr3-dependent retrograde regulation of PDR5 expression. Mol. Cell. Biol. 28, 5851-5864.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5851-5864
    • Gulshan, K.1    Schmidt, J.A.2    Shahi, P.3    Moye-Rowley, W.S.4


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