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Volumn 68, Issue 2, 2017, Pages 323-335.e6

mTORC1 Phosphorylates Acetyltransferase p300 to Regulate Autophagy and Lipogenesis

Author keywords

autophagy; cell metabolism; lipogenesis; mTORC1; p300

Indexed keywords

HISTONE ACETYLTRANSFERASE PCAF; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; SERINE; MECHANISTIC TARGET OF RAPAMYCIN COMPLEX 1; MULTIPROTEIN COMPLEX; P300-CBP-ASSOCIATED FACTOR; TARGET OF RAPAMYCIN KINASE;

EID: 85031284714     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2017.09.020     Document Type: Article
Times cited : (134)

References (64)
  • 2
    • 33646341231 scopus 로고    scopus 로고
    • A nuclear transport signal in mammalian target of rapamycin is critical for its cytoplasmic signaling to S6 kinase 1
    • Bachmann, R.A., Kim, J.H., Wu, A.L., Park, I.H., Chen, J., A nuclear transport signal in mammalian target of rapamycin is critical for its cytoplasmic signaling to S6 kinase 1. J. Biol. Chem. 281 (2006), 7357–7363.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7357-7363
    • Bachmann, R.A.1    Kim, J.H.2    Wu, A.L.3    Park, I.H.4    Chen, J.5
  • 3
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister, A.J., Kouzarides, T., The CBP co-activator is a histone acetyltransferase. Nature 384 (1996), 641–643.
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 4
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L.C., The phosphoinositide 3-kinase pathway. Science 296 (2002), 1655–1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 6
    • 0034916613 scopus 로고    scopus 로고
    • p300/CBP proteins: HATs for transcriptional bridges and scaffolds
    • Chan, H.M., La Thangue, N.B., p300/CBP proteins: HATs for transcriptional bridges and scaffolds. J. Cell Sci. 114 (2001), 2363–2373.
    • (2001) J. Cell Sci. , vol.114 , pp. 2363-2373
    • Chan, H.M.1    La Thangue, N.B.2
  • 7
    • 84953638824 scopus 로고    scopus 로고
    • AMPK-dependent phosphorylation of GAPDH triggers Sirt1 activation and is necessary for autophagy upon glucose starvation
    • Chang, C., Su, H., Zhang, D., Wang, Y., Shen, Q., Liu, B., Huang, R., Zhou, T., Peng, C., Wong, C.C., et al. AMPK-dependent phosphorylation of GAPDH triggers Sirt1 activation and is necessary for autophagy upon glucose starvation. Mol. Cell 60 (2015), 930–940.
    • (2015) Mol. Cell , vol.60 , pp. 930-940
    • Chang, C.1    Su, H.2    Zhang, D.3    Wang, Y.4    Shen, Q.5    Liu, B.6    Huang, R.7    Zhou, T.8    Peng, C.9    Wong, C.C.10
  • 8
    • 34848899559 scopus 로고    scopus 로고
    • ERK2-mediated C-terminal serine phosphorylation of p300 is vital to the regulation of epidermal growth factor-induced keratin 16 gene expression
    • Chen, Y.J., Wang, Y.N., Chang, W.C., ERK2-mediated C-terminal serine phosphorylation of p300 is vital to the regulation of epidermal growth factor-induced keratin 16 gene expression. J. Biol. Chem. 282 (2007), 27215–27228.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27215-27228
    • Chen, Y.J.1    Wang, Y.N.2    Chang, W.C.3
  • 11
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das, C., Lucia, M.S., Hansen, K.C., Tyler, J.K., CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature 459 (2009), 113–117.
    • (2009) Nature , vol.459 , pp. 113-117
    • Das, C.1    Lucia, M.S.2    Hansen, K.C.3    Tyler, J.K.4
  • 12
    • 84883743725 scopus 로고    scopus 로고
    • Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation
    • Delvecchio, M., Gaucher, J., Aguilar-Gurrieri, C., Ortega, E., Panne, D., Structure of the p300 catalytic core and implications for chromatin targeting and HAT regulation. Nat. Struct. Mol. Biol. 20 (2013), 1040–1046.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 1040-1046
    • Delvecchio, M.1    Gaucher, J.2    Aguilar-Gurrieri, C.3    Ortega, E.4    Panne, D.5
  • 13
    • 43049121395 scopus 로고    scopus 로고
    • Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt
    • Fulco, M., Cen, Y., Zhao, P., Hoffman, E.P., McBurney, M.W., Sauve, A.A., Sartorelli, V., Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt. Dev. Cell 14 (2008), 661–673.
    • (2008) Dev. Cell , vol.14 , pp. 661-673
    • Fulco, M.1    Cen, Y.2    Zhao, P.3    Hoffman, E.P.4    McBurney, M.W.5    Sauve, A.A.6    Sartorelli, V.7
  • 15
    • 84863109266 scopus 로고    scopus 로고
    • AP1 is essential for generation of autophagosomes from the trans-Golgi network
    • Guo, Y., Chang, C., Huang, R., Liu, B., Bao, L., Liu, W., AP1 is essential for generation of autophagosomes from the trans-Golgi network. J. Cell Sci. 125 (2012), 1706–1715.
    • (2012) J. Cell Sci. , vol.125 , pp. 1706-1715
    • Guo, Y.1    Chang, C.2    Huang, R.3    Liu, B.4    Bao, L.5    Liu, W.6
  • 16
    • 84883242404 scopus 로고    scopus 로고
    • Differences in specificity and selectivity between CBP and p300 acetylation of histone H3 and H3/H4
    • Henry, R.A., Kuo, Y.M., Andrews, A.J., Differences in specificity and selectivity between CBP and p300 acetylation of histone H3 and H3/H4. Biochemistry 52 (2013), 5746–5759.
    • (2013) Biochemistry , vol.52 , pp. 5746-5759
    • Henry, R.A.1    Kuo, Y.M.2    Andrews, A.J.3
  • 17
    • 79958696694 scopus 로고    scopus 로고
    • The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling
    • Hsu, P.P., Kang, S.A., Rameseder, J., Zhang, Y., Ottina, K.A., Lim, D., Peterson, T.R., Choi, Y., Gray, N.S., Yaffe, M.B., et al. The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signaling. Science 332 (2011), 1317–1322.
    • (2011) Science , vol.332 , pp. 1317-1322
    • Hsu, P.P.1    Kang, S.A.2    Rameseder, J.3    Zhang, Y.4    Ottina, K.A.5    Lim, D.6    Peterson, T.R.7    Choi, Y.8    Gray, N.S.9    Yaffe, M.B.10
  • 18
    • 22544466382 scopus 로고    scopus 로고
    • Akt phosphorylation of p300 at Ser-1834 is essential for its histone acetyltransferase and transcriptional activity
    • Huang, W.C., Chen, C.C., Akt phosphorylation of p300 at Ser-1834 is essential for its histone acetyltransferase and transcriptional activity. Mol. Cell. Biol. 25 (2005), 6592–6602.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6592-6602
    • Huang, W.C.1    Chen, C.C.2
  • 20
    • 79959906869 scopus 로고    scopus 로고
    • Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase
    • Jiang, W., Wang, S., Xiao, M., Lin, Y., Zhou, L., Lei, Q., Xiong, Y., Guan, K.L., Zhao, S., Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase. Mol. Cell 43 (2011), 33–44.
    • (2011) Mol. Cell , vol.43 , pp. 33-44
    • Jiang, W.1    Wang, S.2    Xiao, M.3    Lin, Y.4    Zhou, L.5    Lei, Q.6    Xiong, Y.7    Guan, K.L.8    Zhao, S.9
  • 21
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim, J., Kundu, M., Viollet, B., Guan, K.L., AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat. Cell Biol. 13 (2011), 132–141.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 22
    • 84921443304 scopus 로고    scopus 로고
    • mTORC1 phosphorylates UVRAG to negatively regulate autophagosome and endosome maturation
    • Kim, Y.M., Jung, C.H., Seo, M., Kim, E.K., Park, J.M., Bae, S.S., Kim, D.H., mTORC1 phosphorylates UVRAG to negatively regulate autophagosome and endosome maturation. Mol. Cell 57 (2015), 207–218.
    • (2015) Mol. Cell , vol.57 , pp. 207-218
    • Kim, Y.M.1    Jung, C.H.2    Seo, M.3    Kim, E.K.4    Park, J.M.5    Bae, S.S.6    Kim, D.H.7
  • 23
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: from phenomenology to molecular understanding in less than a decade
    • Klionsky, D.J., Autophagy: from phenomenology to molecular understanding in less than a decade. Nat. Rev. Mol. Cell Biol. 8 (2007), 931–937.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 931-937
    • Klionsky, D.J.1
  • 24
    • 65249106104 scopus 로고    scopus 로고
    • Regulation of autophagy by the p300 acetyltransferase
    • Lee, I.H., Finkel, T., Regulation of autophagy by the p300 acetyltransferase. J. Biol. Chem. 284 (2009), 6322–6328.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6322-6328
    • Lee, I.H.1    Finkel, T.2
  • 25
    • 35848970056 scopus 로고    scopus 로고
    • Theaflavins attenuate hepatic lipid accumulation through activating AMPK in human HepG2 cells
    • Lin, C.L., Huang, H.C., Lin, J.K., Theaflavins attenuate hepatic lipid accumulation through activating AMPK in human HepG2 cells. J. Lipid Res. 48 (2007), 2334–2343.
    • (2007) J. Lipid Res. , vol.48 , pp. 2334-2343
    • Lin, C.L.1    Huang, H.C.2    Lin, J.K.3
  • 26
    • 39149109887 scopus 로고    scopus 로고
    • The structural basis of protein acetylation by the p300/CBP transcriptional coactivator
    • Liu, X., Wang, L., Zhao, K., Thompson, P.R., Hwang, Y., Marmorstein, R., Cole, P.A., The structural basis of protein acetylation by the p300/CBP transcriptional coactivator. Nature 451 (2008), 846–850.
    • (2008) Nature , vol.451 , pp. 846-850
    • Liu, X.1    Wang, L.2    Zhao, K.3    Thompson, P.R.4    Hwang, Y.5    Marmorstein, R.6    Cole, P.A.7
  • 27
    • 0034460363 scopus 로고    scopus 로고
    • A novel Rb- and p300-binding protein inhibits transactivation by MyoD
    • MacLellan, W.R., Xiao, G., Abdellatif, M., Schneider, M.D., A novel Rb- and p300-binding protein inhibits transactivation by MyoD. Mol. Cell. Biol. 20 (2000), 8903–8915.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8903-8915
    • MacLellan, W.R.1    Xiao, G.2    Abdellatif, M.3    Schneider, M.D.4
  • 28
    • 85018509261 scopus 로고    scopus 로고
    • AKT/PKB signaling: navigating the network
    • Manning, B.D., Toker, A., AKT/PKB signaling: navigating the network. Cell 169 (2017), 381–405.
    • (2017) Cell , vol.169 , pp. 381-405
    • Manning, B.D.1    Toker, A.2
  • 30
    • 84874352229 scopus 로고    scopus 로고
    • Rag GTPases mediate amino acid-dependent recruitment of TFEB and MITF to lysosomes
    • Martina, J.A., Puertollano, R., Rag GTPases mediate amino acid-dependent recruitment of TFEB and MITF to lysosomes. J. Cell Biol. 200 (2013), 475–491.
    • (2013) J. Cell Biol. , vol.200 , pp. 475-491
    • Martina, J.A.1    Puertollano, R.2
  • 32
    • 1542343973 scopus 로고    scopus 로고
    • mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availability
    • Mayer, C., Zhao, J., Yuan, X., Grummt, I., mTOR-dependent activation of the transcription factor TIF-IA links rRNA synthesis to nutrient availability. Genes Dev. 18 (2004), 423–434.
    • (2004) Genes Dev. , vol.18 , pp. 423-434
    • Mayer, C.1    Zhao, J.2    Yuan, X.3    Grummt, I.4
  • 33
    • 80051714838 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase 1/2-mediated phosphorylation of p300 enhances myosin heavy chain I/beta gene expression via acetylation of nuclear factor of activated T cells c1
    • Meissner, J.D., Freund, R., Krone, D., Umeda, P.K., Chang, K.C., Gros, G., Scheibe, R.J., Extracellular signal-regulated kinase 1/2-mediated phosphorylation of p300 enhances myosin heavy chain I/beta gene expression via acetylation of nuclear factor of activated T cells c1. Nucleic Acids Res. 39 (2011), 5907–5925.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 5907-5925
    • Meissner, J.D.1    Freund, R.2    Krone, D.3    Umeda, P.K.4    Chang, K.C.5    Gros, G.6    Scheibe, R.J.7
  • 34
    • 33645818534 scopus 로고    scopus 로고
    • Acetylation of UBF changes during the cell cycle and regulates the interaction of UBF with RNA polymerase I
    • Meraner, J., Lechner, M., Loidl, A., Goralik-Schramel, M., Voit, R., Grummt, I., Loidl, P., Acetylation of UBF changes during the cell cycle and regulates the interaction of UBF with RNA polymerase I. Nucleic Acids Res. 34 (2006), 1798–1806.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1798-1806
    • Meraner, J.1    Lechner, M.2    Loidl, A.3    Goralik-Schramel, M.4    Voit, R.5    Grummt, I.6    Loidl, P.7
  • 35
    • 80052511813 scopus 로고    scopus 로고
    • The AMPK signalling pathway coordinates cell growth, autophagy and metabolism
    • Mihaylova, M.M., Shaw, R.J., The AMPK signalling pathway coordinates cell growth, autophagy and metabolism. Nat. Cell Biol. 13 (2011), 1016–1023.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1016-1023
    • Mihaylova, M.M.1    Shaw, R.J.2
  • 38
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: process and function
    • Mizushima, N., Autophagy: process and function. Genes Dev. 21 (2007), 2861–2873.
    • (2007) Genes Dev. , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 40
    • 0037507252 scopus 로고    scopus 로고
    • The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif
    • Nojima, H., Tokunaga, C., Eguchi, S., Oshiro, N., Hidayat, S., Yoshino, K., Hara, K., Tanaka, N., Avruch, J., Yonezawa, K., The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif. J. Biol. Chem. 278 (2003), 15461–15464.
    • (2003) J. Biol. Chem. , vol.278 , pp. 15461-15464
    • Nojima, H.1    Tokunaga, C.2    Eguchi, S.3    Oshiro, N.4    Hidayat, S.5    Yoshino, K.6    Hara, K.7    Tanaka, N.8    Avruch, J.9    Yonezawa, K.10
  • 41
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko, V.V., Schiltz, R.L., Russanova, V., Howard, B.H., Nakatani, Y., The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87 (1996), 953–959.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, V.V.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 44
    • 52949137425 scopus 로고    scopus 로고
    • Cytoplasmic and nuclear distribution of the protein complexes mTORC1 and mTORC2: rapamycin triggers dephosphorylation and delocalization of the mTORC2 components rictor and sin1
    • Rosner, M., Hengstschläger, M., Cytoplasmic and nuclear distribution of the protein complexes mTORC1 and mTORC2: rapamycin triggers dephosphorylation and delocalization of the mTORC2 components rictor and sin1. Hum. Mol. Genet. 17 (2008), 2934–2948.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2934-2948
    • Rosner, M.1    Hengstschläger, M.2
  • 45
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A.L., Nada, S., Sabatini, D.M., Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141 (2010), 290–303.
    • (2010) Cell , vol.141 , pp. 290-303
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3    Markhard, A.L.4    Nada, S.5    Sabatini, D.M.6
  • 47
    • 85014844261 scopus 로고    scopus 로고
    • mTOR signaling in growth, metabolism, and disease
    • Saxton, R.A., Sabatini, D.M., mTOR signaling in growth, metabolism, and disease. Cell 168 (2017), 960–976.
    • (2017) Cell , vol.168 , pp. 960-976
    • Saxton, R.A.1    Sabatini, D.M.2
  • 51
    • 84894523716 scopus 로고    scopus 로고
    • Making new contacts: the mTOR network in metabolism and signalling crosstalk
    • Shimobayashi, M., Hall, M.N., Making new contacts: the mTOR network in metabolism and signalling crosstalk. Nat. Rev. Mol. Cell Biol. 15 (2014), 155–162.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 155-162
    • Shimobayashi, M.1    Hall, M.N.2
  • 53
    • 85028036190 scopus 로고    scopus 로고
    • VPS34 acetylation controls its lipid kinase activity and the initiation of canonical and non-canonical autophagy
    • Su, H., Yang, F., Wang, Q., Shen, Q., Huang, J., Peng, C., Zhang, Y., Wan, W., Wong, C.C.L., Sun, Q., et al. VPS34 acetylation controls its lipid kinase activity and the initiation of canonical and non-canonical autophagy. Mol. Cell 67 (2017), 907–921 e907.
    • (2017) Mol. Cell , vol.67 , pp. 907-921 e907
    • Su, H.1    Yang, F.2    Wang, Q.3    Shen, Q.4    Huang, J.5    Peng, C.6    Zhang, Y.7    Wan, W.8    Wong, C.C.L.9    Sun, Q.10
  • 57
    • 33947538050 scopus 로고    scopus 로고
    • Rapamycin induces feedback activation of Akt signaling through an IGF-1R-dependent mechanism
    • Wan, X., Harkavy, B., Shen, N., Grohar, P., Helman, L.J., Rapamycin induces feedback activation of Akt signaling through an IGF-1R-dependent mechanism. Oncogene 26 (2007), 1932–1940.
    • (2007) Oncogene , vol.26 , pp. 1932-1940
    • Wan, X.1    Harkavy, B.2    Shen, N.3    Grohar, P.4    Helman, L.J.5
  • 59
    • 84976274890 scopus 로고    scopus 로고
    • TP53INP2/DOR, a mediator of cell autophagy, promotes rDNA transcription via facilitating the assembly of the POLR1/RNA polymerase I preinitiation complex at rDNA promoters
    • Xu, Y., Wan, W., Shou, X., Huang, R., You, Z., Shou, Y., Wang, L., Zhou, T., Liu, W., TP53INP2/DOR, a mediator of cell autophagy, promotes rDNA transcription via facilitating the assembly of the POLR1/RNA polymerase I preinitiation complex at rDNA promoters. Autophagy 12 (2016), 1118–1128.
    • (2016) Autophagy , vol.12 , pp. 1118-1128
    • Xu, Y.1    Wan, W.2    Shou, X.3    Huang, R.4    You, Z.5    Shou, Y.6    Wang, L.7    Zhou, T.8    Liu, W.9
  • 60
    • 0038313055 scopus 로고    scopus 로고
    • Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice
    • Yadav, N., Lee, J., Kim, J., Shen, J., Hu, M.C., Aldaz, C.M., Bedford, M.T., Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice. Proc. Natl. Acad. Sci. USA 100 (2003), 6464–6468.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6464-6468
    • Yadav, N.1    Lee, J.2    Kim, J.3    Shen, J.4    Hu, M.C.5    Aldaz, C.M.6    Bedford, M.T.7
  • 61
    • 0035914324 scopus 로고    scopus 로고
    • Regulation of transcription by AMP-activated protein kinase: phosphorylation of p300 blocks its interaction with nuclear receptors
    • Yang, W., Hong, Y.H., Shen, X.Q., Frankowski, C., Camp, H.S., Leff, T., Regulation of transcription by AMP-activated protein kinase: phosphorylation of p300 blocks its interaction with nuclear receptors. J. Biol. Chem. 276 (2001), 38341–38344.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38341-38344
    • Yang, W.1    Hong, Y.H.2    Shen, X.Q.3    Frankowski, C.4    Camp, H.S.5    Leff, T.6
  • 63
    • 0037008730 scopus 로고    scopus 로고
    • Predominant nuclear localization of mammalian target of rapamycin in normal and malignant cells in culture
    • Zhang, X., Shu, L., Hosoi, H., Murti, K.G., Houghton, P.J., Predominant nuclear localization of mammalian target of rapamycin in normal and malignant cells in culture. J. Biol. Chem. 277 (2002), 28127–28134.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28127-28134
    • Zhang, X.1    Shu, L.2    Hosoi, H.3    Murti, K.G.4    Houghton, P.J.5


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