메뉴 건너뛰기




Volumn 289, Issue 36, 2014, Pages 24736-24748

Dual functions of the trans-2-enoyl-CoA reductase TER in the sphingosine 1-phosphate metabolic pathway and in fatty acid elongation

Author keywords

[No Author keywords available]

Indexed keywords

GENE ENCODING; LIPIDS; METABOLISM; SPHINGOSINES;

EID: 84906965129     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.571869     Document Type: Article
Times cited : (38)

References (52)
  • 1
    • 58149196187 scopus 로고    scopus 로고
    • Tracking microdomain dynamics in cell membranes
    • Day, C. A., and Kenworthy, A. K. (2009) Tracking microdomain dynamics in cell membranes. Biochim. Biophys. Acta 1788, 245-253
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 245-253
    • Day, C.A.1    Kenworthy, A.K.2
  • 2
    • 79951873360 scopus 로고    scopus 로고
    • Lipid mediators in life science
    • Murakami, M. (2011) Lipid mediators in life science. Exp. Anim. 60, 7-20
    • (2011) Exp. Anim. , vol.60 , pp. 7-20
    • Murakami, M.1
  • 3
    • 84859341928 scopus 로고    scopus 로고
    • Targeting protein lipidation in disease
    • Resh, M. D. (2012) Targeting protein lipidation in disease. Trends Mol. Med. 18, 206-214
    • (2012) Trends Mol. Med. , vol.18 , pp. 206-214
    • Resh, M.D.1
  • 4
    • 84897954501 scopus 로고    scopus 로고
    • Sphingolipids as modulators of membrane proteins
    • Ernst, A. M., and Brügger, B. (2014) Sphingolipids as modulators of membrane proteins. Biochim. Biophys. Acta 1841, 665-670
    • (2014) Biochim. Biophys. Acta , vol.1841 , pp. 665-670
    • Ernst, A.M.1    Brügger, B.2
  • 5
    • 34247520569 scopus 로고    scopus 로고
    • Metabolism and biological functions of two phosphorylated sphingolipids, sphingosine 1-phosphate and ceramide 1-phosphate
    • Kihara, A., Mitsutake, S., Mizutani, Y., and Igarashi, Y. (2007) Metabolism and biological functions of two phosphorylated sphingolipids, sphingosine 1-phosphate and ceramide 1-phosphate. Prog. Lipid Res. 46, 126-144
    • (2007) Prog. Lipid Res. , vol.46 , pp. 126-144
    • Kihara, A.1    Mitsutake, S.2    Mizutani, Y.3    Igarashi, Y.4
  • 6
    • 84861430003 scopus 로고    scopus 로고
    • The Sjögren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway
    • Nakahara, K., Ohkuni, A., Kitamura, T., Abe, K., Naganuma, T., Ohno, Y., Zoeller, R. A., and Kihara, A. (2012) The Sjögren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway. Mol. Cell 46, 461-471
    • (2012) Mol. Cell , vol.46 , pp. 461-471
    • Nakahara, K.1    Ohkuni, A.2    Kitamura, T.3    Abe, K.4    Naganuma, T.5    Ohno, Y.6    Zoeller, R.A.7    Kihara, A.8
  • 7
    • 84867096429 scopus 로고    scopus 로고
    • Sphingolipid signaling in metabolic disorders
    • Hla, T., and Dannenberg, A. J. (2012) Sphingolipid signaling in metabolic disorders. Cell Metab. 16, 420-434
    • (2012) Cell Metab. , vol.16 , pp. 420-434
    • Hla, T.1    Dannenberg, A.J.2
  • 8
    • 84897954605 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate is a key metabolite linking sphingolipids to glycerophospholipids
    • Kihara, A. (2014) Sphingosine 1-phosphate is a key metabolite linking sphingolipids to glycerophospholipids. Biochim. Biophys. Acta 1841, 766-772
    • (2014) Biochim. Biophys. Acta , vol.1841 , pp. 766-772
    • Kihara, A.1
  • 9
    • 0038218405 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate: An enigmatic signalling lipid
    • Spiegel, S., and Milstien, S. (2003) Sphingosine-1-phosphate: an enigmatic signalling lipid. Nat. Rev. Mol. Cell Biol. 4, 397-407
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 397-407
    • Spiegel, S.1    Milstien, S.2
  • 10
    • 49949109713 scopus 로고    scopus 로고
    • Production and release of sphingosine 1-phosphate and the phosphorylated form of the immunomodulator FTY720
    • Kihara, A., and Igarashi, Y. (2008) Production and release of sphingosine 1-phosphate and the phosphorylated form of the immunomodulator FTY720. Biochim. Biophys. Acta 1781, 496-502
    • (2008) Biochim. Biophys. Acta , vol.1781 , pp. 496-502
    • Kihara, A.1    Igarashi, Y.2
  • 11
    • 84876119766 scopus 로고    scopus 로고
    • Fingolimod: Direct CNS effects of sphingosine 1-phosphate (S1P) receptor modulation and implications in multiple sclerosis therapy
    • Groves, A., Kihara, Y., and Chun, J. (2013) Fingolimod: direct CNS effects of sphingosine 1-phosphate (S1P) receptor modulation and implications in multiple sclerosis therapy. J. Neurol. Sci. 328, 9-18
    • (2013) J. Neurol. Sci. , vol.328 , pp. 9-18
    • Groves, A.1    Kihara, Y.2    Chun, J.3
  • 12
    • 3242696730 scopus 로고    scopus 로고
    • Physiological and pathological actions of sphingosine 1-phosphate
    • Hla, T. (2004) Physiological and pathological actions of sphingosine 1-phosphate. Semin. Cell Dev. Biol. 15, 513-520
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 513-520
    • Hla, T.1
  • 13
    • 0032567648 scopus 로고    scopus 로고
    • Identification of the first mammalian sphingosine phosphate lyase gene and its functional expression in yeast
    • Zhou, J., and Saba, J. D. (1998) Identification of the first mammalian sphingosine phosphate lyase gene and its functional expression in yeast. Biochem. Biophys. Res. Commun. 242, 502-507
    • (1998) Biochem. Biophys. Res. Commun. , vol.242 , pp. 502-507
    • Zhou, J.1    Saba, J.D.2
  • 14
    • 70449700288 scopus 로고    scopus 로고
    • Discontinued postnatal thymocyte development in sphingosine 1-phosphate-lyase-deficient mice
    • Weber, C., Krueger, A., Münk, A., Bode, C., Van Veldhoven, P. P., and Gräler, M. H. (2009) Discontinued postnatal thymocyte development in sphingosine 1-phosphate-lyase-deficient mice. J. Immunol. 183, 4292-4301
    • (2009) J. Immunol. , vol.183 , pp. 4292-4301
    • Weber, C.1    Krueger, A.2    Münk, A.3    Bode, C.4    Van Veldhoven, P.P.5    Gräler, M.H.6
  • 15
    • 58149474166 scopus 로고    scopus 로고
    • Incomplete inhibition of sphingosine 1-phosphate lyase modulates immune system function yet prevents early lethality and non-lymphoid lesions
    • Vogel, P., Donoviel, M. S., Read, R., Hansen, G. M., Hazlewood, J., Anderson, S. J., Sun, W., Swaffield, J., and Oravecz, T. (2009) Incomplete inhibition of sphingosine 1-phosphate lyase modulates immune system function yet prevents early lethality and non-lymphoid lesions. PLoS One 4, e4112
    • (2009) PLoS One , vol.4 , pp. e4112
    • Vogel, P.1    Donoviel, M.S.2    Read, R.3    Hansen, G.M.4    Hazlewood, J.5    Anderson, S.J.6    Sun, W.7    Swaffield, J.8    Oravecz, T.9
  • 17
    • 79953190058 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate lyase deficiency produces a pro-inflammatory response while impairing neutrophil trafficking
    • Allende, M. L., Bektas, M., Lee, B. G., Bonifacino, E., Kang, J., Tuymetova, G., Chen, W., Saba, J. D., and Proia, R. L. (2011) Sphingosine-1-phosphate lyase deficiency produces a pro-inflammatory response while impairing neutrophil trafficking. J. Biol. Chem. 286, 7348-7358
    • (2011) J. Biol. Chem. , vol.286 , pp. 7348-7358
    • Allende, M.L.1    Bektas, M.2    Lee, B.G.3    Bonifacino, E.4    Kang, J.5    Tuymetova, G.6    Chen, W.7    Saba, J.D.8    Proia, R.L.9
  • 18
    • 84863348086 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate (S1P) lyase deficiency increases sphingolipid formation via recycling at the expense of de novo biosynthesis in neurons
    • Hagen-Euteneuer, N., Lütjohann, D., Park, H., Merrill, A. H., Jr., and van Echten-Deckert, G. (2012) Sphingosine 1-phosphate (S1P) lyase deficiency increases sphingolipid formation via recycling at the expense of de novo biosynthesis in neurons. J. Biol. Chem. 287, 9128-9136
    • (2012) J. Biol. Chem. , vol.287 , pp. 9128-9136
    • Hagen-Euteneuer, N.1    Lütjohann, D.2    Park, H.3    Merrill, A.H.4    Van Echten-Deckert, G.5
  • 20
    • 84890130276 scopus 로고    scopus 로고
    • Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway
    • Ohkuni, A., Ohno, Y., and Kihara, A. (2013) Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem. Biophys. Res. Commun. 442, 195-201
    • (2013) Biochem. Biophys. Res. Commun. , vol.442 , pp. 195-201
    • Ohkuni, A.1    Ohno, Y.2    Kihara, A.3
  • 21
    • 33845231217 scopus 로고    scopus 로고
    • Sjögren-Larsson syndrome: Molecular genetics and biochemical pathogenesis of fatty aldehyde dehydrogenase deficiency
    • Rizzo, W. B. (2007) Sjögren-Larsson syndrome: molecular genetics and biochemical pathogenesis of fatty aldehyde dehydrogenase deficiency. Mol. Genet. Metab. 90, 1-9
    • (2007) Mol. Genet. Metab. , vol.90 , pp. 1-9
    • Rizzo, W.B.1
  • 22
    • 0037470063 scopus 로고    scopus 로고
    • Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade
    • Moon, Y. A., and Horton, J. D. (2003) Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade. J. Biol. Chem. 278, 7335-7343
    • (2003) J. Biol. Chem. , vol.278 , pp. 7335-7343
    • Moon, Y.A.1    Horton, J.D.2
  • 23
    • 84868600772 scopus 로고    scopus 로고
    • Very long-chain fatty acids: Elongation, physiology and related disorders
    • Kihara, A. (2012) Very long-chain fatty acids: elongation, physiology and related disorders. J. Biochem. 152, 387-395
    • (2012) J. Biochem. , vol.152 , pp. 387-395
    • Kihara, A.1
  • 24
    • 84897066334 scopus 로고    scopus 로고
    • Metabolism of very long-chain fatty acids: Genes and pathophysiology
    • Sassa, T., and Kihara, A. (2014) Metabolism of very long-chain fatty acids: genes and pathophysiology. Biomol. Ther. (Seoul) 22, 83-92
    • (2014) Biomol. Ther. (Seoul) , vol.22 , pp. 83-92
    • Sassa, T.1    Kihara, A.2
  • 25
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C. B., Davies, A., Cost, G. J., Caputo, E., Li, J., Hieter, P., and Boeke, J. D. (1998) Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14, 115-132
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 26
    • 0032531024 scopus 로고    scopus 로고
    • Functional analysis of yeast essential genes using a promoter-substitution cassette and the tetracycline-regulatable dual expression system
    • Bellí, G., Garí, E., Aldea, M., and Herrero, E. (1998) Functional analysis of yeast essential genes using a promoter-substitution cassette and the tetracycline-regulatable dual expression system. Yeast 14, 1127-1138
    • (1998) Yeast , vol.14 , pp. 1127-1138
    • Bellí, G.1    Garí, E.2    Aldea, M.3    Herrero, E.4
  • 27
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 28
    • 27144458423 scopus 로고    scopus 로고
    • Long-chain base kinase Lcb4 is anchored to the membrane through its palmitoylation by Akr1
    • Kihara, A., Kurotsu, F., Sano, T., Iwaki, S., and Igarashi, Y. (2005) Long-chain base kinase Lcb4 is anchored to the membrane through its palmitoylation by Akr1. Mol. Cell. Biol. 25, 9189-9197
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9189-9197
    • Kihara, A.1    Kurotsu, F.2    Sano, T.3    Iwaki, S.4    Igarashi, Y.5
  • 30
    • 0014815904 scopus 로고
    • Metabolism of sphingosine bases: XIV. Sphinganine (dihydrosphingosine), an effective donor of the alk-1′-enyl chain of plasmalogens
    • Stoffel, W., LeKim, D., and Heyn, G. (1970) Metabolism of sphingosine bases: XIV. sphinganine (dihydrosphingosine), an effective donor of the alk-1′-enyl chain of plasmalogens. Hoppe Seylers Z. Physiol. Chem. 351, 875-883
    • (1970) Hoppe Seylers Z. Physiol. Chem. , vol.351 , pp. 875-883
    • Stoffel, W.1    LeKim, D.2    Heyn, G.3
  • 31
    • 7444239039 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate lyase SPL is an endoplasmic reticulum-resident, integral membrane protein with the pyridoxal 5′-phosphate binding domain exposed to the cytosol
    • Ikeda, M., Kihara, A., and Igarashi, Y. (2004) Sphingosine-1-phosphate lyase SPL is an endoplasmic reticulum-resident, integral membrane protein with the pyridoxal 5′-phosphate binding domain exposed to the cytosol. Biochem. Biophys. Res. Commun. 325, 338-343
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , pp. 338-343
    • Ikeda, M.1    Kihara, A.2    Igarashi, Y.3
  • 32
    • 34547106607 scopus 로고    scopus 로고
    • Dual subcellular localization in the endoplasmic reticulum and peroxisomes and a vital role in protecting against oxidative stress of fatty aldehyde dehydrogenase are achieved by alternative splicing
    • Ashibe, B., Hirai, T., Higashi, K., Sekimizu, K., and Motojima, K. (2007) Dual subcellular localization in the endoplasmic reticulum and peroxisomes and a vital role in protecting against oxidative stress of fatty aldehyde dehydrogenase are achieved by alternative splicing. J. Biol. Chem. 282, 20763-20773
    • (2007) J. Biol. Chem. , vol.282 , pp. 20763-20773
    • Ashibe, B.1    Hirai, T.2    Higashi, K.3    Sekimizu, K.4    Motojima, K.5
  • 33
    • 43249086785 scopus 로고    scopus 로고
    • Mammalian long-chain acyl-CoA synthetases
    • Soupene, E., and Kuypers, F. A. (2008) Mammalian long-chain acyl-CoA synthetases. Exp. Biol. Med. 233, 507-521
    • (2008) Exp. Biol. Med. , vol.233 , pp. 507-521
    • Soupene, E.1    Kuypers, F.A.2
  • 34
    • 0034749756 scopus 로고    scopus 로고
    • Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae
    • Kohlwein, S. D., Eder, S., Oh, C. S., Martin, C. E., Gable, K., Bacikova, D., and Dunn, T. (2001) Tsc13p is required for fatty acid elongation and localizes to a novel structure at the nuclear-vacuolar interface in Saccharomyces cerevisiae. Mol. Cell. Biol. 21, 109-125
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 109-125
    • Kohlwein, S.D.1    Eder, S.2    Oh, C.S.3    Martin, C.E.4    Gable, K.5    Bacikova, D.6    Dunn, T.7
  • 36
    • 0030878240 scopus 로고    scopus 로고
    • ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation
    • Oh, C. S., Toke, D. A., Mandala, S., and Martin, C. E. (1997) ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation. J. Biol. Chem. 272, 17376-17384
    • (1997) J. Biol. Chem. , vol.272 , pp. 17376-17384
    • Oh, C.S.1    Toke, D.A.2    Mandala, S.3    Martin, C.E.4
  • 37
    • 45549088118 scopus 로고    scopus 로고
    • Membrane topology and essential amino acid residues of Phs1, a 3-hydroxyacyl-CoA dehydratase involved in very long-chain fatty acid elongation
    • Kihara, A., Sakuraba, H., Ikeda, M., Denpoh, A., and Igarashi, Y. (2008) Membrane topology and essential amino acid residues of Phs1, a 3-hydroxyacyl-CoA dehydratase involved in very long-chain fatty acid elongation. J. Biol. Chem. 283, 11199-11209
    • (2008) J. Biol. Chem. , vol.283 , pp. 11199-11209
    • Kihara, A.1    Sakuraba, H.2    Ikeda, M.3    Denpoh, A.4    Igarashi, Y.5
  • 38
    • 0030928284 scopus 로고    scopus 로고
    • Lipid remodeling leads to the introduction and exchange of defined ceramides on GPI proteins in the ER and Golgi of Saccharomyces cerevisiae
    • Reggiori, F., Canivenc-Gansel, E., and Conzelmann, A. (1997) Lipid remodeling leads to the introduction and exchange of defined ceramides on GPI proteins in the ER and Golgi of Saccharomyces cerevisiae. EMBOJ. 16, 3506-3518
    • (1997) EMBOJ. , vol.16 , pp. 3506-3518
    • Reggiori, F.1    Canivenc-Gansel, E.2    Conzelmann, A.3
  • 39
    • 84865195294 scopus 로고    scopus 로고
    • An essential function of sphingolipids in yeast cell division
    • Epstein, S., Castillon, G. A., Qin, Y., and Riezman, H. (2012) An essential function of sphingolipids in yeast cell division. Mol. Microbiol. 84, 1018-1032
    • (2012) Mol. Microbiol. , vol.84 , pp. 1018-1032
    • Epstein, S.1    Castillon, G.A.2    Qin, Y.3    Riezman, H.4
  • 41
    • 58149462858 scopus 로고    scopus 로고
    • 2-Hydroxy-ceramide synthesis by ceramide synthase family: Enzymatic basis for the preference of FA chain length
    • Mizutani, Y., Kihara, A., Chiba, H., Tojo, H., and Igarashi, Y. (2008) 2-Hydroxy-ceramide synthesis by ceramide synthase family: enzymatic basis for the preference of FA chain length. J. Lipid Res. 49, 2356-2364
    • (2008) J. Lipid Res. , vol.49 , pp. 2356-2364
    • Mizutani, Y.1    Kihara, A.2    Chiba, H.3    Tojo, H.4    Igarashi, Y.5
  • 42
    • 0029902428 scopus 로고    scopus 로고
    • Mammalian mitochondrial β-oxidation
    • Eaton, S., Bartlett, K., and Pourfarzam, M. (1996) Mammalian mitochondrial β-oxidation. Biochem. J. 320, 345-357
    • (1996) Biochem. J. , vol.320 , pp. 345-357
    • Eaton, S.1    Bartlett, K.2    Pourfarzam, M.3
  • 43
    • 84890944352 scopus 로고    scopus 로고
    • Mutation for nonsyndromic mental retardation in the trans-2-enoyl-CoA reductase TER gene involved in fatty acid elongation impairs the enzyme activity and stability, leading to change in sphingolipid profile
    • Abe, K., Ohno, Y., Sassa, T., Taguchi, R., Çalişkan, M., Ober, C., and Kihara, A. (2013) Mutation for nonsyndromic mental retardation in the trans-2-enoyl-CoA reductase TER gene involved in fatty acid elongation impairs the enzyme activity and stability, leading to change in sphingolipid profile. J. Biol. Chem. 288, 36741-36749
    • (2013) J. Biol. Chem. , vol.288 , pp. 36741-36749
    • Abe, K.1    Ohno, Y.2    Sassa, T.3    Taguchi, R.4    Çalişkan, M.5    Ober, C.6    Kihara, A.7
  • 44
    • 4444258170 scopus 로고    scopus 로고
    • Mammalian wax biosynthesis: I. Identification of two fatty acyl-coenzyme A reductases with different substrate specificities and tissue distributions
    • Cheng, J. B., and Russell, D. W. (2004) Mammalian wax biosynthesis: I. identification of two fatty acyl-coenzyme A reductases with different substrate specificities and tissue distributions. J. Biol. Chem. 279, 37789-37797
    • (2004) J. Biol. Chem. , vol.279 , pp. 37789-37797
    • Cheng, J.B.1    Russell, D.W.2
  • 46
  • 48
    • 41949140023 scopus 로고    scopus 로고
    • Characterization of ceramide synthase 2: Tissue distribution, substrate specificity, and inhibition by sphingosine 1-phosphate
    • Laviad, E. L., Albee, L., Pankova-Kholmyansky, I., Epstein, S., Park, H., Merrill, A. H., Jr., and Futerman, A. H. (2008) Characterization of ceramide synthase 2: tissue distribution, substrate specificity, and inhibition by sphingosine 1-phosphate. J. Biol. Chem. 283, 5677-5684
    • (2008) J. Biol. Chem. , vol.283 , pp. 5677-5684
    • Laviad, E.L.1    Albee, L.2    Pankova-Kholmyansky, I.3    Epstein, S.4    Park, H.5    Merrill, A.H.6    Futerman, A.H.7
  • 51
    • 77951932472 scopus 로고    scopus 로고
    • Significance of glycosphingolipid fatty acid chain length on membrane microdomain-mediated signal transduction
    • Iwabuchi, K., Nakayama, H., Iwahara, C., and Takamori, K. (2010) Significance of glycosphingolipid fatty acid chain length on membrane microdomain-mediated signal transduction. FEBS Lett. 584, 1642-1652
    • (2010) FEBS Lett. , vol.584 , pp. 1642-1652
    • Iwabuchi, K.1    Nakayama, H.2    Iwahara, C.3    Takamori, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.