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Volumn 11, Issue 4, 2010, Pages 479-490

Glucosylceramide biosynthesis is involved in golgi morphology and protein secretion in plant cells

Author keywords

Endoplasmic reticulum; Glucosylceramide; Golgi bodies; Plant cells; Protein transport; Secretion

Indexed keywords

2 DECANOYLAMINO 3 MORPHOLINO 1 PHENYL 1 PROPANOL; CERAMIDE GLUCOSYLTRANSFERASE; GLUCOSYLCERAMIDE; MEMBRANE LIPID; MEMBRANE PROTEIN; SPHINGOLIPID;

EID: 77951745666     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2009.01030.x     Document Type: Article
Times cited : (51)

References (43)
  • 1
    • 33747360181 scopus 로고    scopus 로고
    • Plant sphingolipids: separation and identification of major sphingolipid classes from leaves
    • Markham JE, Li J, Cahoon EB, Jaworski JG. Plant sphingolipids: separation and identification of major sphingolipid classes from leaves. J Biol Chem 2006, 281:22684-22694.
    • (2006) J Biol Chem , vol.281 , pp. 22684-22694
    • Markham, J.E.1    Li, J.2    Cahoon, E.B.3    Jaworski, J.G.4
  • 2
    • 0038356303 scopus 로고    scopus 로고
    • Plant sphingolipids: structural diversity, biosynthesis, first genes and functions
    • Sperling P, Heinz E. Plant sphingolipids: structural diversity, biosynthesis, first genes and functions. Biochim Biophys Acta 2003, 1632:1-15.
    • (2003) Biochim Biophys Acta , vol.1632 , pp. 1-15
    • Sperling, P.1    Heinz, E.2
  • 6
    • 33947534553 scopus 로고    scopus 로고
    • The essential nature of sphingolipids in plants as revealed by the functional identification and characterization of the Arabidopsis LCB1 subunit of serine palmitoyltransferase
    • Chen M, Han G, Dietrich CR, Dunn TM, Cahoon EB. The essential nature of sphingolipids in plants as revealed by the functional identification and characterization of the Arabidopsis LCB1 subunit of serine palmitoyltransferase. Plant Cell 2006, 18:3576-3593.
    • (2006) Plant Cell , vol.18 , pp. 3576-3593
    • Chen, M.1    Han, G.2    Dietrich, C.R.3    Dunn, T.M.4    Cahoon, E.B.5
  • 7
    • 41849147858 scopus 로고    scopus 로고
    • Loss-of-function mutations and inducible RNAi suppression of Arabidopsis LCB2 genes reveal the critical role of sphingolipids in gametophytic and sporophytic cell viability
    • Dietrich CR, Han G, Chen M, Berg RH, Dunn TM, Cahoon EB. Loss-of-function mutations and inducible RNAi suppression of Arabidopsis LCB2 genes reveal the critical role of sphingolipids in gametophytic and sporophytic cell viability. Plant J 2008, 54:284-298.
    • (2008) Plant J , vol.54 , pp. 284-298
    • Dietrich, C.R.1    Han, G.2    Chen, M.3    Berg, R.H.4    Dunn, T.M.5    Cahoon, E.B.6
  • 8
    • 0022629415 scopus 로고
    • Chemical structure activity relationships of the inhibition of sterol biosynthesis by N-substituted morpholines in higher plant cells
    • Rahier A, Schmitt P, Huss B, Benveniste P, Pommer EH. Chemical structure activity relationships of the inhibition of sterol biosynthesis by N-substituted morpholines in higher plant cells. Pestic Biochem Physiol 1986, 25:112-124.
    • (1986) Pestic Biochem Physiol , vol.25 , pp. 112-124
    • Rahier, A.1    Schmitt, P.2    Huss, B.3    Benveniste, P.4    Pommer, E.H.5
  • 9
    • 0037043514 scopus 로고    scopus 로고
    • Inhibition of the sterol pathway in leek seedlings impairs phosphatidylserine and glucosylceramide synthesis but triggers an accumulation of triacylglycerols
    • Hartmann MA, Perret AM, Carde JP, Cassagne C, Moreau P. Inhibition of the sterol pathway in leek seedlings impairs phosphatidylserine and glucosylceramide synthesis but triggers an accumulation of triacylglycerols. Biochim Biophys Acta 2002, 1583:285-296.
    • (2002) Biochim Biophys Acta , vol.1583 , pp. 285-296
    • Hartmann, M.A.1    Perret, A.M.2    Carde, J.P.3    Cassagne, C.4    Moreau, P.5
  • 10
    • 23644447397 scopus 로고    scopus 로고
    • Disruptions of the Arabidopsis enoyl-CoA reductase gene reveal an essential role for very-long-chain fatty acid synthesis in cell expansion during plant morphogenesis
    • Zheng H, Rowland O, Kunst L. Disruptions of the Arabidopsis enoyl-CoA reductase gene reveal an essential role for very-long-chain fatty acid synthesis in cell expansion during plant morphogenesis. Plant cell 2005, 17:1467-1481.
    • (2005) Plant cell , vol.17 , pp. 1467-1481
    • Zheng, H.1    Rowland, O.2    Kunst, L.3
  • 11
    • 0036915634 scopus 로고    scopus 로고
    • A specific structural requirement for ergosterol in long-chain fatty acid synthesis mutants important for maintaining raft domains in yeast
    • Eisenkolb M, Zenzmaier C, Leitner E, Schneiter R. A specific structural requirement for ergosterol in long-chain fatty acid synthesis mutants important for maintaining raft domains in yeast. Mol Biol Cell 2002, 13:4414-4428.
    • (2002) Mol Biol Cell , vol.13 , pp. 4414-4428
    • Eisenkolb, M.1    Zenzmaier, C.2    Leitner, E.3    Schneiter, R.4
  • 12
    • 20444457063 scopus 로고    scopus 로고
    • Synthesis of sphingolipids with very long chain fatty acids but not ergosterol is required for routing of newly synthesized plasma membrane ATPase to the cell surface of yeast
    • Gaigg B, Timischl B, Corbino L, Schneiter R. Synthesis of sphingolipids with very long chain fatty acids but not ergosterol is required for routing of newly synthesized plasma membrane ATPase to the cell surface of yeast. J Biol Chem 2005, 280:22515-22522.
    • (2005) J Biol Chem , vol.280 , pp. 22515-22522
    • Gaigg, B.1    Timischl, B.2    Corbino, L.3    Schneiter, R.4
  • 14
    • 0025993036 scopus 로고
    • Determination of the intracellular sites and topology of glucosylceramide synthesis in rat liver
    • Futerman AH, Pagano RE. Determination of the intracellular sites and topology of glucosylceramide synthesis in rat liver. Biochem J 1991, 280:295-302.
    • (1991) Biochem J , vol.280 , pp. 295-302
    • Futerman, A.H.1    Pagano, R.E.2
  • 16
    • 52649132375 scopus 로고    scopus 로고
    • Systematic analysis of protein subcellular localization and interaction using high-throughput transient transformation of Arabidopsis seedlings
    • Marion J, Bach L, Bellec Y, Meyer C, Gissot L, Faure JD. Systematic analysis of protein subcellular localization and interaction using high-throughput transient transformation of Arabidopsis seedlings. Plant J 2008, 56:169-179.
    • (2008) Plant J , vol.56 , pp. 169-179
    • Marion, J.1    Bach, L.2    Bellec, Y.3    Meyer, C.4    Gissot, L.5    Faure, J.D.6
  • 18
    • 33644847629 scopus 로고    scopus 로고
    • Sec22 and Memb11 are v-SNAREs of the anterograde endoplasmic reticulum-Golgi pathway in tobacco leaf epidermal cells
    • Chatre L, Brandizzi F, Hocquellet A, Hawes C, Moreau P. Sec22 and Memb11 are v-SNAREs of the anterograde endoplasmic reticulum-Golgi pathway in tobacco leaf epidermal cells. Plant Physiol 2005, 139:1244-1254.
    • (2005) Plant Physiol , vol.139 , pp. 1244-1254
    • Chatre, L.1    Brandizzi, F.2    Hocquellet, A.3    Hawes, C.4    Moreau, P.5
  • 19
    • 0242287992 scopus 로고    scopus 로고
    • Glycosidase inhibitors: update and perspectives on practical use
    • Asano N. Glycosidase inhibitors: update and perspectives on practical use. Glycobiology 2003, 13:93R-104R.
    • (2003) Glycobiology , vol.13
    • Asano, N.1
  • 20
    • 0023258056 scopus 로고
    • Preparation of the active isomer of 1-phenyl-2-decanoylamino-3-morpholino-1-propanol , inhibitor of murine glucocerebroside synthetase
    • Inoguchi J, Radin NS. Preparation of the active isomer of 1-phenyl-2-decanoylamino-3-morpholino-1-propanol , inhibitor of murine glucocerebroside synthetase. J Lipid Res 1987, 28:565-571.
    • (1987) J Lipid Res , vol.28 , pp. 565-571
    • Inoguchi, J.1    Radin, N.S.2
  • 21
    • 0030048470 scopus 로고    scopus 로고
    • Purification and characterization of UDP-glucose:ceramide glucosyltransferase from rat liver Golgi membranes
    • Paul P, Kamisaka Y, Marks DL, Pagano RE. Purification and characterization of UDP-glucose:ceramide glucosyltransferase from rat liver Golgi membranes. J Biol Chem 1996, 271:2287-2293.
    • (1996) J Biol Chem , vol.271 , pp. 2287-2293
    • Paul, P.1    Kamisaka, Y.2    Marks, D.L.3    Pagano, R.E.4
  • 22
    • 25844520678 scopus 로고    scopus 로고
    • An inhibitor of glucosylceramide synthase inhibits the human enzyme, but not enzymes from other organisms
    • Hillig I, Warnecke D, Heinz E. An inhibitor of glucosylceramide synthase inhibits the human enzyme, but not enzymes from other organisms. Biosci Biotechnol Biochem 2005, 69:1782-1785.
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 1782-1785
    • Hillig, I.1    Warnecke, D.2    Heinz, E.3
  • 23
    • 0022419189 scopus 로고
    • Improved one dimensional thin layer chromatographic technique for polar lipids
    • Heape AM, Juguelin H, Boiron F, Cassagne C. Improved one dimensional thin layer chromatographic technique for polar lipids. J Chromatogr 1985, 332:391-395.
    • (1985) J Chromatogr , vol.332 , pp. 391-395
    • Heape, A.M.1    Juguelin, H.2    Boiron, F.3    Cassagne, C.4
  • 25
    • 3142683074 scopus 로고    scopus 로고
    • Targeting of a Nicotiana plumbaginifolia H+ - ATPase to the plasma membrane is not by default and requires cytosolic structural determinants
    • Lefebvre B, Batoko H, Duby G, Boutry M. Targeting of a Nicotiana plumbaginifolia H+ - ATPase to the plasma membrane is not by default and requires cytosolic structural determinants. Plant Cell 2004, 16:1772-1789.
    • (2004) Plant Cell , vol.16 , pp. 1772-1789
    • Lefebvre, B.1    Batoko, H.2    Duby, G.3    Boutry, M.4
  • 26
    • 4444309237 scopus 로고    scopus 로고
    • Systematic analysis of SNARE molecules in Arabidopsis: dissection of the post-Golgi network in plant cells
    • Uemura T, Ueda T, Ohniwa RL, Nakano A, Takeyasu K, Sato MH. Systematic analysis of SNARE molecules in Arabidopsis: dissection of the post-Golgi network in plant cells. Cell Struct Funct 2004, 29:49-65.
    • (2004) Cell Struct Funct , vol.29 , pp. 49-65
    • Uemura, T.1    Ueda, T.2    Ohniwa, R.L.3    Nakano, A.4    Takeyasu, K.5    Sato, M.H.6
  • 27
    • 0035983848 scopus 로고    scopus 로고
    • Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: evidence from selective photobleaching
    • Brandizzi F, Snapp EL, Roberts AG, Lippincott-Schwartz J, Hawes C. Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: evidence from selective photobleaching. Plant Cell 2002, 14:1293-1309.
    • (2002) Plant Cell , vol.14 , pp. 1293-1309
    • Brandizzi, F.1    Snapp, E.L.2    Roberts, A.G.3    Lippincott-Schwartz, J.4    Hawes, C.5
  • 28
    • 0026755594 scopus 로고
    • Effects of a sphingolipid synthesis inhibitor on membrane transport through the secretory pathway
    • Rosenwald AG, Machamer CE, Pagano RE. Effects of a sphingolipid synthesis inhibitor on membrane transport through the secretory pathway. Biochemistry 1992, 31:3581-3590.
    • (1992) Biochemistry , vol.31 , pp. 3581-3590
    • Rosenwald, A.G.1    Machamer, C.E.2    Pagano, R.E.3
  • 29
    • 0040294722 scopus 로고    scopus 로고
    • Nuclear export of proteins in plants: AtXPO1 is the export receptor for leucine-rich nuclear export signals in Arabidopsis thaliana
    • Haasen D, Köhler C, Neuhaus G, Merkle T. Nuclear export of proteins in plants: AtXPO1 is the export receptor for leucine-rich nuclear export signals in Arabidopsis thaliana. Plant J 1999, 20:695-705.
    • (1999) Plant J , vol.20 , pp. 695-705
    • Haasen, D.1    Köhler, C.2    Neuhaus, G.3    Merkle, T.4
  • 30
    • 34249785671 scopus 로고    scopus 로고
    • De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated
    • Hanton SL, Chatre L, Renna L, Matheson LA, Brandizzi F. De novo formation of plant endoplasmic reticulum export sites is membrane cargo induced and signal mediated. Plant Physiol 2007, 143:1640-1650.
    • (2007) Plant Physiol , vol.143 , pp. 1640-1650
    • Hanton, S.L.1    Chatre, L.2    Renna, L.3    Matheson, L.A.4    Brandizzi, F.5
  • 31
    • 35848960133 scopus 로고    scopus 로고
    • 1-Butanol targets the Golgi apparatus in tobacco BY-2 cells, but in a different way to brefeldin A
    • Langhans M, Robinson DG. 1-Butanol targets the Golgi apparatus in tobacco BY-2 cells, but in a different way to brefeldin A. J Exp Bot 2007, 58:3439-3447.
    • (2007) J Exp Bot , vol.58 , pp. 3439-3447
    • Langhans, M.1    Robinson, D.G.2
  • 32
    • 0037151098 scopus 로고    scopus 로고
    • Ceramide biosynthesis is required for the formation of the oligomeric H+ - ATPase Pma1p in the yeast endoplasmic reticulum
    • Lee MC, Hamamoto S, Schekman R. Ceramide biosynthesis is required for the formation of the oligomeric H+ - ATPase Pma1p in the yeast endoplasmic reticulum. J Biol Chem 2002, 277:22395-22401.
    • (2002) J Biol Chem , vol.277 , pp. 22395-22401
    • Lee, M.C.1    Hamamoto, S.2    Schekman, R.3
  • 34
    • 44949195796 scopus 로고    scopus 로고
    • Identification of a glycosphingolipid transfer protein GLTP1 in Arabidopsis thaliana
    • West G, Viitanen L, Alm C, Mattjus P, Salminen TA, Edqvist J. Identification of a glycosphingolipid transfer protein GLTP1 in Arabidopsis thaliana. FEBS J 2008, 275:3421-3437.
    • (2008) FEBS J , vol.275 , pp. 3421-3437
    • West, G.1    Viitanen, L.2    Alm, C.3    Mattjus, P.4    Salminen, T.A.5    Edqvist, J.6
  • 35
    • 0034525907 scopus 로고    scopus 로고
    • A rab1 GTPase is required for transport between the endoplasmic reticulum and golgi apparatus and for normal golgi movement in plants
    • Batoko H, Zheng HQ, Hawes C, Moore I. A rab1 GTPase is required for transport between the endoplasmic reticulum and golgi apparatus and for normal golgi movement in plants. Plant Cell 2000, 12:2201-2218.
    • (2000) Plant Cell , vol.12 , pp. 2201-2218
    • Batoko, H.1    Zheng, H.Q.2    Hawes, C.3    Moore, I.4
  • 36
    • 0036016439 scopus 로고    scopus 로고
    • The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain
    • Brandizzi F, Frangne N, Marc-Martin S, Hawes C, Neuhaus JM, Paris N. The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain. Plant Cell 2002, 14:1077-1092.
    • (2002) Plant Cell , vol.14 , pp. 1077-1092
    • Brandizzi, F.1    Frangne, N.2    Marc-Martin, S.3    Hawes, C.4    Neuhaus, J.M.5    Paris, N.6
  • 37
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1986, 72:248-254.
    • (1986) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 38
    • 0029392629 scopus 로고
    • Enzymatic formation of plant cerebroside: properties of UDP-glucose: ceramide glucosyltransferase in radish seedlings
    • Nakayama M, Kojima M, Ohnishi M, Ito S. Enzymatic formation of plant cerebroside: properties of UDP-glucose: ceramide glucosyltransferase in radish seedlings. Biosci Biotechnol Biochem 1995, 59:1882-1886.
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 1882-1886
    • Nakayama, M.1    Kojima, M.2    Ohnishi, M.3    Ito, S.4
  • 39
    • 0031569875 scopus 로고    scopus 로고
    • Ceramide glucosylation in bean hypocotyls microsomes: evidence that steryl glucoside serves as glucose donor
    • Lynch DV, Criss AK, Lahoczky JL, Bui VT. Ceramide glucosylation in bean hypocotyls microsomes: evidence that steryl glucoside serves as glucose donor. Arch Biochem Biosphys 1997, 340:311-316.
    • (1997) Arch Biochem Biosphys , vol.340 , pp. 311-316
    • Lynch, D.V.1    Criss, A.K.2    Lahoczky, J.L.3    Bui, V.T.4
  • 40
    • 0142138695 scopus 로고    scopus 로고
    • Formation of glucosylceramide and sterol glucoside by a UDP-glucose-dependent glucosyl-ceramide synthase from cotton expressed in Pichia pastoris
    • Hillig I, Leipelt M, Ott C, Zahringer U, Warnecke D, Heinz E. Formation of glucosylceramide and sterol glucoside by a UDP-glucose-dependent glucosyl-ceramide synthase from cotton expressed in Pichia pastoris. FEBS Lett 2003, 553:365-369.
    • (2003) FEBS Lett , vol.553 , pp. 365-369
    • Hillig, I.1    Leipelt, M.2    Ott, C.3    Zahringer, U.4    Warnecke, D.5    Heinz, E.6
  • 41
    • 0021072977 scopus 로고
    • Analysis of brain lipids by high performance TLC and densitometry
    • Macala LJ, Yo RK, Ando S. Analysis of brain lipids by high performance TLC and densitometry. J Lipid Res 1983, 24:1243-1250.
    • (1983) J Lipid Res , vol.24 , pp. 1243-1250
    • Macala, L.J.1    Yo, R.K.2    Ando, S.3
  • 42
    • 0033794113 scopus 로고    scopus 로고
    • Sphingolipid extraction and analysis by thin-layer chromatography
    • Van Echten-Deckert G. Sphingolipid extraction and analysis by thin-layer chromatography. Meth Enzymol 2000, 312:64-79.
    • (2000) Meth Enzymol , vol.312 , pp. 64-79
    • Van Echten-Deckert, G.1
  • 43
    • 0034607844 scopus 로고    scopus 로고
    • Functional cloning of an Arabidopsis thaliana cDNA encoding cycloeucalenol cycloisomerase
    • Lovato MA, Hart EA, Segura MJ, Giner JL, Matsuda SP. Functional cloning of an Arabidopsis thaliana cDNA encoding cycloeucalenol cycloisomerase. J Biol Chem 2000, 275:13394-13397.
    • (2000) J Biol Chem , vol.275 , pp. 13394-13397
    • Lovato, M.A.1    Hart, E.A.2    Segura, M.J.3    Giner, J.L.4    Matsuda, S.P.5


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