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Volumn 143, Issue 6, 2008, Pages 803-811

In vitro formation of a novel type of membrane vesicles containing Dpm1p: Putative transport vesicles for lipid droplets in budding yeast

Author keywords

Dpm1p; Erg6p; Lipid droplet; Saccharomyces cerevisiae; Vesicle transport

Indexed keywords

ADENOSINE TRIPHOSPHATE; DOLICHOL PHOSPHATE MANNOSE; DOLICHOL PHOSPHATE MANNOSE SYNTHASE; FAT DROPLET; GLYCEROPHOSPHATE; GREEN FLUORESCENT PROTEIN; OLEOYL COENZYME A; SYNTHETASE;

EID: 46349105757     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvn034     Document Type: Article
Times cited : (8)

References (50)
  • 1
    • 0032911957 scopus 로고    scopus 로고
    • Mechanisms of lipid-body formation
    • Murphy, D.J. and Vance, J. (1999) Mechanisms of lipid-body formation. Trends Biochem. Sci. 24, 109-115
    • (1999) Trends Biochem. Sci , vol.24 , pp. 109-115
    • Murphy, D.J.1    Vance, J.2
  • 2
    • 0034684048 scopus 로고    scopus 로고
    • Intracellular lipid particles of eukaryotic cells
    • Zweytick, D., Athenstaedt, K., and Daum, G. (2000) Intracellular lipid particles of eukaryotic cells. Biochim. Biophys. Acta 1469, 101-120
    • (2000) Biochim. Biophys. Acta , vol.1469 , pp. 101-120
    • Zweytick, D.1    Athenstaedt, K.2    Daum, G.3
  • 3
    • 0035810964 scopus 로고    scopus 로고
    • Lipid droplets: Proteins floating on a pool of fat
    • Brown, D.A. (2001) Lipid droplets: proteins floating on a pool of fat. Curr. Biol. 11, R446-R449
    • (2001) Curr. Biol , vol.11
    • Brown, D.A.1
  • 4
    • 0034903123 scopus 로고    scopus 로고
    • The biogenesis and functions of lipid bodies in animals, plants and microorganisms
    • Murphy, D.J. (2001) The biogenesis and functions of lipid bodies in animals, plants and microorganisms. Prog. Lipid Res. 40, 325-438
    • (2001) Prog. Lipid Res , vol.40 , pp. 325-438
    • Murphy, D.J.1
  • 5
    • 0037113954 scopus 로고    scopus 로고
    • The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition
    • Tauchi-Sato, K., Ozeki, S., Houjou, T., Taguchi, R., and Fujimoto, T. (2002) The surface of lipid droplets is a phospholipid monolayer with a unique fatty acid composition. J. Biol. Chem. 277, 44507-44512
    • (2002) J. Biol. Chem , vol.277 , pp. 44507-44512
    • Tauchi-Sato, K.1    Ozeki, S.2    Houjou, T.3    Taguchi, R.4    Fujimoto, T.5
  • 6
    • 33646168160 scopus 로고    scopus 로고
    • Lipid droplets: A unified view of a dynamic organelle
    • Martin, S. and Parton, R.G. (2006) Lipid droplets: a unified view of a dynamic organelle. Nat. Rev. Mol. Cell Biol. 7, 373-378
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 373-378
    • Martin, S.1    Parton, R.G.2
  • 7
    • 8744267532 scopus 로고    scopus 로고
    • Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes
    • Brasaemle, D.L., Dolios, G., Shapiro, L., and Wang, R. (2004) Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes. J. Biol. Chem. 279, 46835-46842
    • (2004) J. Biol. Chem , vol.279 , pp. 46835-46842
    • Brasaemle, D.L.1    Dolios, G.2    Shapiro, L.3    Wang, R.4
  • 8
    • 0942287191 scopus 로고    scopus 로고
    • Chinese hamster ovary K2 cell lipid droplets appear to be metabolic organelles involved in membrane traffic
    • Liu, P., Ying, Y., Zhao, Y., Mundy, D.I., Zhu, M., and Anderson, R.G. (2004) Chinese hamster ovary K2 cell lipid droplets appear to be metabolic organelles involved in membrane traffic. J. Biol. Chem. 279, 3787-3792
    • (2004) J. Biol. Chem , vol.279 , pp. 3787-3792
    • Liu, P.1    Ying, Y.2    Zhao, Y.3    Mundy, D.I.4    Zhu, M.5    Anderson, R.G.6
  • 12
    • 0035842889 scopus 로고    scopus 로고
    • Vesicular and non-vesicular transport of ceramide from ER to the Golgi apparatus in yeast
    • Funato, K. and Riezman, H. (2001) Vesicular and non-vesicular transport of ceramide from ER to the Golgi apparatus in yeast. J. Cell Biol. 155, 949-959
    • (2001) J. Cell Biol , vol.155 , pp. 949-959
    • Funato, K.1    Riezman, H.2
  • 14
    • 0024807217 scopus 로고
    • A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus
    • Nakano, A. and Muramatsu, M. (1989) A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Biol. 109, 2677-2691
    • (1989) J. Cell Biol , vol.109 , pp. 2677-2691
    • Nakano, A.1    Muramatsu, M.2
  • 15
    • 0032495477 scopus 로고    scopus 로고
    • COPII-cargo interactions direct protein sorting into ER-derived transport vesicles
    • Kuehn, M.J., Herrmann, J.M., and Schekman, R. (1998) COPII-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature 391, 187-190
    • (1998) Nature , vol.391 , pp. 187-190
    • Kuehn, M.J.1    Herrmann, J.M.2    Schekman, R.3
  • 16
    • 0029831539 scopus 로고    scopus 로고
    • Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro
    • Kuehn, M.J., Schekman, R., and Ljungdahl, P.O. (1996) Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro. J. Cell Biol. 135, 585-595
    • (1996) J. Cell Biol , vol.135 , pp. 585-595
    • Kuehn, M.J.1    Schekman, R.2    Ljungdahl, P.O.3
  • 17
    • 0035809210 scopus 로고    scopus 로고
    • Erv41p and Erv46p: New components of COPII vesicles involved in transport between the ER and Golgi complex
    • Otte, S., Belden, W.J., Heidtman, M., Liu, J., Jensen, O.N., and Barlowe, C. (2001) Erv41p and Erv46p: new components of COPII vesicles involved in transport between the ER and Golgi complex. J. Cell Biol. 152, 503-518
    • (2001) J. Cell Biol , vol.152 , pp. 503-518
    • Otte, S.1    Belden, W.J.2    Heidtman, M.3    Liu, J.4    Jensen, O.N.5    Barlowe, C.6
  • 18
    • 0036329213 scopus 로고    scopus 로고
    • Emp47p and its close homolog Emp46p have a tyrosine-containing endoplasmic reticulum exit signal and function in glycoprotein secretion in Saccharomyces cerevisiae
    • Sato, K. and Nakano, A. (2002) Emp47p and its close homolog Emp46p have a tyrosine-containing endoplasmic reticulum exit signal and function in glycoprotein secretion in Saccharomyces cerevisiae. Mol. Biol. Cell 13, 2518-2532
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2518-2532
    • Sato, K.1    Nakano, A.2
  • 19
    • 0037119988 scopus 로고    scopus 로고
    • Sec16p potentiates the action of COPII proteins to bud transport vesicles
    • Supek, F., Madden, D.T., Hamamoto, S., Orci, L., and Schekman, R. (2002) Sec16p potentiates the action of COPII proteins to bud transport vesicles. J. Cell Biol. 158, 1029-1038
    • (2002) J. Cell Biol , vol.158 , pp. 1029-1038
    • Supek, F.1    Madden, D.T.2    Hamamoto, S.3    Orci, L.4    Schekman, R.5
  • 20
    • 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
  • 21
    • 0038491550 scopus 로고    scopus 로고
    • Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane
    • Umebayashi, K. and Nakano, A. (2003) Ergosterol is required for targeting of tryptophan permease to the yeast plasma membrane. J. Cell Biol. 161, 1117-1131
    • (2003) J. Cell Biol , vol.161 , pp. 1117-1131
    • Umebayashi, K.1    Nakano, A.2
  • 22
    • 0030292930 scopus 로고    scopus 로고
    • An Arabidopsis gene isolated by a novel method for detecting genetic interaction in yeast encodes the GDP dissociation inhibitor of Ara4 GTPase
    • Ueda, T., Matsuda, N., Anai, T., Tsukaya, H., Uchimiya, H., and Nakano, A. (1996) An Arabidopsis gene isolated by a novel method for detecting genetic interaction in yeast encodes the GDP dissociation inhibitor of Ara4 GTPase. Plant Cell 8, 2079-2091
    • (1996) Plant Cell , vol.8 , pp. 2079-2091
    • Ueda, T.1    Matsuda, N.2    Anai, T.3    Tsukaya, H.4    Uchimiya, H.5    Nakano, A.6
  • 23
    • 0032102628 scopus 로고    scopus 로고
    • Isolation of a tobacco cDNA encoding Sar1 GTPase and analysis of its dominant mutations in vesicular traffic using a yeast complementation system
    • Takeuchi, M., Tada, M., Saito, C., Yashiroda, H., and Nakano, A. (1998) Isolation of a tobacco cDNA encoding Sar1 GTPase and analysis of its dominant mutations in vesicular traffic using a yeast complementation system. Plant Cell Physiol. 39, 590-599
    • (1998) Plant Cell Physiol , vol.39 , pp. 590-599
    • Takeuchi, M.1    Tada, M.2    Saito, C.3    Yashiroda, H.4    Nakano, A.5
  • 24
    • 0028964475 scopus 로고
    • The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • Schimmöller, F., Singer-Krüger, B., Schröder, S., Krüger, U., Barlowe, C. and Riezman, H. (1995) The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO J. 14, 1329-1339
    • (1995) EMBO J , vol.14 , pp. 1329-1339
    • Schimmöller, F.1    Singer-Krüger, B.2    Schröder, S.3    Krüger, U.4    Barlowe, C.5    Riezman, H.6
  • 25
  • 26
    • 0027058051 scopus 로고
    • Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum
    • Stirling, C.J., Rothblatt, J., Hosobuchi, M., Deshaies, R., and Schekman, R. (1992) Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum. Mol. Biol. Cell 3, 129-142
    • (1992) Mol. Biol. Cell , vol.3 , pp. 129-142
    • Stirling, C.J.1    Rothblatt, J.2    Hosobuchi, M.3    Deshaies, R.4    Schekman, R.5
  • 27
    • 0038783732 scopus 로고    scopus 로고
    • Oligomerization of a cargo receptor directs protein sorting into COPII-coated transport vesicles
    • Sato, K. and Nakano, A. (2003) Oligomerization of a cargo receptor directs protein sorting into COPII-coated transport vesicles. Mol. Biol. Cell 14, 3055-3063
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3055-3063
    • Sato, K.1    Nakano, A.2
  • 28
    • 0034031442 scopus 로고    scopus 로고
    • Evidence for recycling of cytochrome P450 sterol 14-demethylase from the cis-Golgi compartment to the endoplasmic reticulum (ER) upon saturation of the ER-retention mechanism
    • Homma, K., Yoshida, Y., and Nakano, A. (2000) Evidence for recycling of cytochrome P450 sterol 14-demethylase from the cis-Golgi compartment to the endoplasmic reticulum (ER) upon saturation of the ER-retention mechanism. J. Biochem. (Tokyo) 127, 747-754
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 747-754
    • Homma, K.1    Yoshida, Y.2    Nakano, A.3
  • 29
    • 0027015925 scopus 로고
    • Reconstitution of transport from endoplasmic reticulum to Golgi complex using endoplasmic reticulum-enriched membrane fraction from yeast
    • Wuestehube, L.J. and Schekman, R.W. (1992) Reconstitution of transport from endoplasmic reticulum to Golgi complex using endoplasmic reticulum-enriched membrane fraction from yeast. Methods Enzymol. 219, 124-136
    • (1992) Methods Enzymol , vol.219 , pp. 124-136
    • Wuestehube, L.J.1    Schekman, R.W.2
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G.L. (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83, 346-356
    • (1977) Anal. Biochem , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 32
    • 0031931498 scopus 로고    scopus 로고
    • Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles
    • Leber, R., Landl, K., Zinser, E., Ahorn, H., Spök, A., Kohlwein, S.D., Turnowsky, F., and Daum, G. (1998) Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles. Mol. Biol. Cell 9, 375-386
    • (1998) Mol. Biol. Cell , vol.9 , pp. 375-386
    • Leber, R.1    Landl, K.2    Zinser, E.3    Ahorn, H.4    Spök, A.5    Kohlwein, S.D.6    Turnowsky, F.7    Daum, G.8
  • 33
    • 0032693609 scopus 로고    scopus 로고
    • Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae
    • Athenstaedt, K., Zweytick, D., Jandrositz, A., Kohlwein, S.D., and Daum, G. (1999) Identification and characterization of major lipid particle proteins of the yeast Saccharomyces cerevisiae. J. Bacteriol. 181, 6441-6448
    • (1999) J. Bacteriol , vol.181 , pp. 6441-6448
    • Athenstaedt, K.1    Zweytick, D.2    Jandrositz, A.3    Kohlwein, S.D.4    Daum, G.5
  • 34
    • 0033618256 scopus 로고    scopus 로고
    • Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast
    • Russell, S.J., Steger, K.A., and Johnston, S.A. (1999) Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast. J. Biol. Chem. 274, 21943-21952
    • (1999) J. Biol. Chem , vol.274 , pp. 21943-21952
    • Russell, S.J.1    Steger, K.A.2    Johnston, S.A.3
  • 35
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipides from animal tissues
    • Folch, J., Lees, M., and Sloane Stanley, G.H. (1957) A simple method for the isolation and purification of total lipides from animal tissues. J. Biol. Chem. 226, 497-509
    • (1957) J. Biol. Chem , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3
  • 36
    • 0014779155 scopus 로고
    • Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser, G., Fkeischer, S., and Yamamoto, A. (1970) Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids 5, 494-496
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fkeischer, S.2    Yamamoto, A.3
  • 37
    • 37049143234 scopus 로고
    • The determination of ergosterol in yeast
    • Shaw, W.H.C. and Jefferies, J.P. (1953) The determination of ergosterol in yeast. The Analyst 78, 509-514
    • (1953) The Analyst , vol.78 , pp. 509-514
    • Shaw, W.H.C.1    Jefferies, J.P.2
  • 38
    • 0029741442 scopus 로고    scopus 로고
    • The glucose transporter (GLUT-4) and vesicle-associated membrane protein-2 (VAMP-2) are segregated from recycling endosomes in insulin-sensitive cells
    • Martin, S., Tellam, J., Livingstone, C., Slot, J.W., Gould, G.W., and James, D.E. (1996) The glucose transporter (GLUT-4) and vesicle-associated membrane protein-2 (VAMP-2) are segregated from recycling endosomes in insulin-sensitive cells. J. Cell Biol. 134, 625-635
    • (1996) J. Cell Biol , vol.134 , pp. 625-635
    • Martin, S.1    Tellam, J.2    Livingstone, C.3    Slot, J.W.4    Gould, G.W.5    James, D.E.6
  • 39
    • 0024297293 scopus 로고
    • Cloning and sequencing of the yeast gene for dolichol phosphate mannose synthase, an essential protein
    • Orlean, P., Albright, C., and Robbins, P.W. (1988) Cloning and sequencing of the yeast gene for dolichol phosphate mannose synthase, an essential protein. J. Biol. Chem. 263, 17499-17507
    • (1988) J. Biol. Chem , vol.263 , pp. 17499-17507
    • Orlean, P.1    Albright, C.2    Robbins, P.W.3
  • 40
    • 0025107479 scopus 로고
    • Dolichol phosphate mannose synthase is required in vivo for glycosyl phosphatidylinositol membrane anchoring, O mannosylation, and N glycosylation of protein in Saccharomyces cerevisiae
    • Orlean, P. (1990) Dolichol phosphate mannose synthase is required in vivo for glycosyl phosphatidylinositol membrane anchoring, O mannosylation, and N glycosylation of protein in Saccharomyces cerevisiae. Mol. Cell. Biol. 10, 5796-5805
    • (1990) Mol. Cell. Biol , vol.10 , pp. 5796-5805
    • Orlean, P.1
  • 42
    • 0034945070 scopus 로고    scopus 로고
    • Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis
    • Sato, M., Fujisaki, S., Sato, K., Nishimura, Y., and Nakano, A. (2001) Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis. Genes Cells 6, 495-506
    • (2001) Genes Cells , vol.6 , pp. 495-506
    • Sato, M.1    Fujisaki, S.2    Sato, K.3    Nishimura, Y.4    Nakano, A.5
  • 43
    • 0032412784 scopus 로고    scopus 로고
    • Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae
    • Daum, G., Lees, N.D., Bard, M., and Dickson, R. (1998) Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae. Yeast 14, 1471-1510
    • (1998) Yeast , vol.14 , pp. 1471-1510
    • Daum, G.1    Lees, N.D.2    Bard, M.3    Dickson, R.4
  • 44
  • 45
    • 0034634727 scopus 로고    scopus 로고
    • Mutagenic study of the structure, function and biogenesis of the yeast plasma membrane H(+)-ATPase
    • Morsomme, P., Slayman, C.W., and Goffeau, A. (2000) Mutagenic study of the structure, function and biogenesis of the yeast plasma membrane H(+)-ATPase. Biochim. Biophys. Acta 1469, 133-157
    • (2000) Biochim. Biophys. Acta , vol.1469 , pp. 133-157
    • Morsomme, P.1    Slayman, C.W.2    Goffeau, A.3
  • 46
    • 0038711498 scopus 로고    scopus 로고
    • A phospholipase D-dependent process forms lipid droplets containing caveolin, adipocyte differentiation-related protein, and vimentin in a cell-free system
    • Marchesan, D., Rutberg, M., Andersson, L., Asp, L., Larsson, T., Borén, J., Johansson, B.R., and Olofsson, S.O. (2003) A phospholipase D-dependent process forms lipid droplets containing caveolin, adipocyte differentiation-related protein, and vimentin in a cell-free system. J. Biol. Chem. 278, 27293-27300
    • (2003) J. Biol. Chem , vol.278 , pp. 27293-27300
    • Marchesan, D.1    Rutberg, M.2    Andersson, L.3    Asp, L.4    Larsson, T.5    Borén, J.6    Johansson, B.R.7    Olofsson, S.O.8
  • 47
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics, A. and Orlean, P. (1993) Glycoprotein biosynthesis in yeast. FASEB J. 7, 540-550
    • (1993) FASEB J , vol.7 , pp. 540-550
    • Herscovics, A.1    Orlean, P.2
  • 48
    • 0026335172 scopus 로고
    • Structure of the yeast endoplasmic reticulum: Localization of ER proteins using immunofluorescence and immunoelectron microscopy
    • Preuss, D., Mulholland, J., Kaiser, C.A., Orlean, P., Albright, C., Rose, M.D., Robbins, P.W., and Botstein, D. (1991) Structure of the yeast endoplasmic reticulum: localization of ER proteins using immunofluorescence and immunoelectron microscopy. Yeast 7, 891-911
    • (1991) Yeast , vol.7 , pp. 891-911
    • Preuss, D.1    Mulholland, J.2    Kaiser, C.A.3    Orlean, P.4    Albright, C.5    Rose, M.D.6    Robbins, P.W.7    Botstein, D.8
  • 49
    • 0024389966 scopus 로고
    • Purification of GDP mannose: Dolichyl-phosphate O-beta-D-mannosyltransferase from Saccharomyces cerevisiae
    • Haselbeck, A. (1989) Purification of GDP mannose: dolichyl-phosphate O-beta-D-mannosyltransferase from Saccharomyces cerevisiae. Eur. J. Biochem. 181, 663-668
    • (1989) Eur. J. Biochem , vol.181 , pp. 663-668
    • Haselbeck, A.1
  • 50
    • 33751161853 scopus 로고    scopus 로고
    • Adipophilin-enriched domains in the ER membrane are sites of lipid droplet biogenesis
    • Robenek, H., Hofnagel, O., Buers, I., Robenek, M.J., Troyer, D., and Severs, N.J. (2006) Adipophilin-enriched domains in the ER membrane are sites of lipid droplet biogenesis. J. Cell Sci. 119, 4215-4224
    • (2006) J. Cell Sci , vol.119 , pp. 4215-4224
    • Robenek, H.1    Hofnagel, O.2    Buers, I.3    Robenek, M.J.4    Troyer, D.5    Severs, N.J.6


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