메뉴 건너뛰기




Volumn 290, Issue 10, 2015, Pages 6191-6202

Oncoprotein YAP regulates the spindle checkpoint activation in a mitotic phosphorylation-dependent manner through up-regulation of BubR1

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL ACTIVATION; PROTEINS; TRANSCRIPTION;

EID: 84924943415     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.624411     Document Type: Article
Times cited : (22)

References (59)
  • 1
    • 77951837150 scopus 로고    scopus 로고
    • The Hippo-YAP pathway in organ size control and tumorigenesis: An updated version
    • Zhao, B., Li, L., Lei, Q., and Guan, K. L. (2010) The Hippo-YAP pathway in organ size control and tumorigenesis: an updated version. Genes Dev. 24, 862-874
    • (2010) Genes Dev. , vol.24 , pp. 862-874
    • Zhao, B.1    Li, L.2    Lei, Q.3    Guan, K.L.4
  • 2
    • 77957883342 scopus 로고    scopus 로고
    • The hippo signaling pathway in development and cancer
    • Pan, D. (2010) The hippo signaling pathway in development and cancer. Dev. Cell 19, 491-505
    • (2010) Dev. Cell , vol.19 , pp. 491-505
    • Pan, D.1
  • 4
    • 84885182528 scopus 로고    scopus 로고
    • Regulation of the Hippo pathway and implications for anticancer drug development
    • Park, H. W., and Guan, K. L. (2013) Regulation of the Hippo pathway and implications for anticancer drug development. Trends Pharmacol. Sci. 34, 581-589
    • (2013) Trends Pharmacol. Sci. , vol.34 , pp. 581-589
    • Park, H.W.1    Guan, K.L.2
  • 5
    • 84891748709 scopus 로고    scopus 로고
    • The two faces of Hippo: Targeting the Hippo pathway for regenerative medicine and cancer treatment
    • Johnson, R., and Halder, G. (2014) The two faces of Hippo: targeting the Hippo pathway for regenerative medicine and cancer treatment. Nat. Rev. Drug Discov. 13, 63-79
    • (2014) Nat. Rev. Drug Discov. , vol.13 , pp. 63-79
    • Johnson, R.1    Halder, G.2
  • 11
    • 72549090299 scopus 로고    scopus 로고
    • YAP1 is amplified and up-regulated in hedgehog-associated medulloblastomas and mediates Sonic hedgehog-driven neural precursor proliferation
    • Fernandez-L, A., Northcott, P. A., Dalton, J., Fraga, C., Ellison, D., Angers, S., Taylor, M. D., and Kenney, A. M. (2009) YAP1 is amplified and up-regulated in hedgehog-associated medulloblastomas and mediates Sonic hedgehog-driven neural precursor proliferation. Genes Dev. 23, 2729-2741
    • (2009) Genes Dev. , vol.23 , pp. 2729-2741
    • Fernandez-L, A.1    Northcott, P.A.2    Dalton, J.3    Fraga, C.4    Ellison, D.5    Angers, S.6    Taylor, M.D.7    Kenney, A.M.8
  • 12
    • 70349295967 scopus 로고    scopus 로고
    • Yes-associated protein is an independent prognostic marker in hepatocellular carcinoma
    • Xu, M. Z., Yao, T. J., Lee, N. P., Ng, I. O., Chan, Y. T., Zender, L., Lowe, S. W., Poon, R. T., and Luk, J. M. (2009) Yes-associated protein is an independent prognostic marker in hepatocellular carcinoma. Cancer 115, 4576-4585
    • (2009) Cancer , vol.115 , pp. 4576-4585
    • Xu, M.Z.1    Yao, T.J.2    Lee, N.P.3    Ng, I.O.4    Chan, Y.T.5    Zender, L.6    Lowe, S.W.7    Poon, R.T.8    Luk, J.M.9
  • 14
    • 79959658018 scopus 로고    scopus 로고
    • The Hippo pathway transcriptional co-activator, YAP, is an ovarian cancer oncogene
    • Zhang, X., George, J., Deb, S., Degoutin, J. L., Takano, E. A., Fox, S. B., AOCS Study group, Bowtell, D. D., and Harvey, K. F. (2011) The Hippo pathway transcriptional co-activator, YAP, is an ovarian cancer oncogene. Oncogene 30, 2810-2822
    • (2011) Oncogene , vol.30 , pp. 2810-2822
    • Zhang, X.1    George, J.2    Deb, S.3    Degoutin, J.L.4    Takano, E.A.5    Fox, S.B.6    Bowtell, D.D.7    Harvey, K.F.8
  • 16
    • 84868103798 scopus 로고    scopus 로고
    • New insights into the troubles of aneuploidy
    • Siegel, J. J., and Amon, A. (2012) New insights into the troubles of aneuploidy. Annu. Rev. Cell Dev. Biol. 28, 189-214
    • (2012) Annu. Rev. Cell Dev. Biol. , vol.28 , pp. 189-214
    • Siegel, J.J.1    Amon, A.2
  • 18
    • 84871530214 scopus 로고    scopus 로고
    • Microtubule attachment and spindle assembly checkpoint signalling at the kinetochore
    • Foley, E. A., and Kapoor, T. M. (2013) Microtubule attachment and spindle assembly checkpoint signalling at the kinetochore. Nat. Rev. Mol. Cell Biol. 14, 25-37
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 25-37
    • Foley, E.A.1    Kapoor, T.M.2
  • 19
    • 84878156617 scopus 로고    scopus 로고
    • Tracking spindle checkpoint signals from kinetochores to APC/C
    • Jia, L., Kim, S., and Yu, H. (2013) Tracking spindle checkpoint signals from kinetochores to APC/C. Trends Biochem. Sci. 38, 302-311
    • (2013) Trends Biochem. Sci. , vol.38 , pp. 302-311
    • Jia, L.1    Kim, S.2    Yu, H.3
  • 21
    • 79959416796 scopus 로고    scopus 로고
    • Bub1 over-expression induces aneuploidy and tumor formation through Aurora B kinase hyperactivation
    • Ricke, R. M., Jeganathan, K. B., and van Deursen, J. M. (2011) Bub1 over-expression induces aneuploidy and tumor formation through Aurora B kinase hyperactivation. J. Cell Biol. 193, 1049-1064
    • (2011) J. Cell Biol. , vol.193 , pp. 1049-1064
    • Ricke, R.M.1    Jeganathan, K.B.2    Van Deursen, J.M.3
  • 22
    • 79958733630 scopus 로고    scopus 로고
    • Mad2 is a critical mediator of the chromosome instability observed upon Rb and p53 pathway inhibition
    • Schvartzman, J. M., Duijf, P. H., Sotillo, R., Coker, C., and Benezra, R. (2011) Mad2 is a critical mediator of the chromosome instability observed upon Rb and p53 pathway inhibition. Cancer Cell 19, 701-714
    • (2011) Cancer Cell , vol.19 , pp. 701-714
    • Schvartzman, J.M.1    Duijf, P.H.2    Sotillo, R.3    Coker, C.4    Benezra, R.5
  • 23
    • 84888309765 scopus 로고    scopus 로고
    • CDK1 Phosphorylation of YAP promotes mitotic defects and cell motility and is essential for neoplastic transformation
    • Yang, S., Zhang, L., Liu, M., Chong, R., Ding, S. J., Chen, Y., and Dong, J. (2013) CDK1 Phosphorylation of YAP promotes mitotic defects and cell motility and is essential for neoplastic transformation. Cancer Res. 73, 6722-6733
    • (2013) Cancer Res. , vol.73 , pp. 6722-6733
    • Yang, S.1    Zhang, L.2    Liu, M.3    Chong, R.4    Ding, S.J.5    Chen, Y.6    Dong, J.7
  • 24
    • 0036222706 scopus 로고    scopus 로고
    • Deregulated human Cdc14A phosphatase disrupts centrosome separation and chromosome segregation
    • Mailand, N., Lukas, C., Kaiser, B. K., Jackson, P. K., Bartek, J., and Lukas, J. (2002) Deregulated human Cdc14A phosphatase disrupts centrosome separation and chromosome segregation. Nat. Cell Biol. 4, 317-322
    • (2002) Nat. Cell Biol. , vol.4 , pp. 317-322
    • Mailand, N.1    Lukas, C.2    Kaiser, B.K.3    Jackson, P.K.4    Bartek, J.5    Lukas, J.6
  • 25
    • 0033514509 scopus 로고    scopus 로고
    • Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway
    • Ramaswamy, S., Nakamura, N., Vazquez, F., Batt, D. B., Perera, S., Roberts, T. M., and Sellers, W. R. (1999) Regulation of G1 progression by the PTEN tumor suppressor protein is linked to inhibition of the phosphatidylinositol 3-kinase/Akt pathway. Proc. Natl. Acad. Sci. U.S.A. 96, 2110-2115
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2110-2115
    • Ramaswamy, S.1    Nakamura, N.2    Vazquez, F.3    Batt, D.B.4    Perera, S.5    Roberts, T.M.6    Sellers, W.R.7
  • 26
    • 27144507324 scopus 로고    scopus 로고
    • Notch 2-positive progenitors with the intrinsic ability to give rise to pancreatic ductal cells
    • Lee, K. M., Yasuda, H., Hollingsworth, M. A., and Ouellette, M. M. (2005) Notch 2-positive progenitors with the intrinsic ability to give rise to pancreatic ductal cells. Lab. Invest. 85, 1003-1012
    • (2005) Lab. Invest. , vol.85 , pp. 1003-1012
    • Lee, K.M.1    Yasuda, H.2    Hollingsworth, M.A.3    Ouellette, M.M.4
  • 27
    • 79953150067 scopus 로고    scopus 로고
    • KIBRA regulates Hippo signaling activity via interactions with large tumor suppressor kinases
    • Xiao, L., Chen, Y., Ji, M., and Dong, J. (2011) KIBRA regulates Hippo signaling activity via interactions with large tumor suppressor kinases. J. Biol. Chem. 286, 7788-7796
    • (2011) J. Biol. Chem. , vol.286 , pp. 7788-7796
    • Xiao, L.1    Chen, Y.2    Ji, M.3    Dong, J.4
  • 28
    • 84867255560 scopus 로고    scopus 로고
    • KIBRA regulates aurora kinase activity and is required for precise chromosome alignment during mitosis
    • Zhang, L., Iyer, J., Chowdhury, A., Ji, M., Xiao, L., Yang, S., Chen, Y., Tsai, M. Y., and Dong, J. (2012) KIBRA regulates aurora kinase activity and is required for precise chromosome alignment during mitosis. J. Biol. Chem. 287, 34069-34077
    • (2012) J. Biol. Chem. , vol.287 , pp. 34069-34077
    • Zhang, L.1    Iyer, J.2    Chowdhury, A.3    Ji, M.4    Xiao, L.5    Yang, S.6    Chen, Y.7    Tsai, M.Y.8    Dong, J.9
  • 29
    • 84866424936 scopus 로고    scopus 로고
    • Phospho-regulation of KIBRA by CDK1 and CDC14 phosphatase controls cell-cycle progression
    • Ji, M., Yang, S., Chen, Y., Xiao, L., Zhang, L., and Dong, J. (2012) Phospho-regulation of KIBRA by CDK1 and CDC14 phosphatase controls cell-cycle progression. Biochem. J. 447, 93-102
    • (2012) Biochem. J. , vol.447 , pp. 93-102
    • Ji, M.1    Yang, S.2    Chen, Y.3    Xiao, L.4    Zhang, L.5    Dong, J.6
  • 30
    • 80054699330 scopus 로고    scopus 로고
    • KIBRA protein phosphorylation is regulated by mitotic kinase aurora and protein phosphatase 1
    • Xiao, L., Chen, Y., Ji, M., Volle, D. J., Lewis, R. E., Tsai, M. Y., and Dong, J. (2011) KIBRA protein phosphorylation is regulated by mitotic kinase aurora and protein phosphatase 1. J. Biol. Chem. 286, 36304-36315
    • (2011) J. Biol. Chem. , vol.286 , pp. 36304-36315
    • Xiao, L.1    Chen, Y.2    Ji, M.3    Volle, D.J.4    Lewis, R.E.5    Tsai, M.Y.6    Dong, J.7
  • 31
    • 84890058684 scopus 로고    scopus 로고
    • Phosphorylation of KIBRA by the extracellular signal-regulated kinase (ERK)-ribosomal S6 kinase (RSK) cascade modulates cell proliferation and migration
    • Yang, S., Ji, M., Zhang, L., Chen, Y., Wennmann, D. O., Kremerskothen, J., and Dong, J. (2014) Phosphorylation of KIBRA by the extracellular signal-regulated kinase (ERK)-ribosomal S6 kinase (RSK) cascade modulates cell proliferation and migration. Cell Signal. 26, 343-351
    • (2014) Cell Signal. , vol.26 , pp. 343-351
    • Yang, S.1    Ji, M.2    Zhang, L.3    Chen, Y.4    Wennmann, D.O.5    Kremerskothen, J.6    Dong, J.7
  • 32
    • 0032254350 scopus 로고    scopus 로고
    • The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-dependent phosphorylation
    • Visintin, R., Craig, K., Hwang, E. S., Prinz, S., Tyers, M., and Amon, A. (1998) The phosphatase Cdc14 triggers mitotic exit by reversal of Cdk-dependent phosphorylation. Mol. Cell 2, 709-718
    • (1998) Mol. Cell , vol.2 , pp. 709-718
    • Visintin, R.1    Craig, K.2    Hwang, E.S.3    Prinz, S.4    Tyers, M.5    Amon, A.6
  • 33
    • 0034723170 scopus 로고    scopus 로고
    • The human Cdc14 phosphatases interact with and dephosphorylate the tumor suppressor protein p53
    • Li, L., Ljungman, M., and Dixon, J. E. (2000) The human Cdc14 phosphatases interact with and dephosphorylate the tumor suppressor protein p53. J. Biol. Chem. 275, 2410-2414
    • (2000) J. Biol. Chem. , vol.275 , pp. 2410-2414
    • Li, L.1    Ljungman, M.2    Dixon, J.E.3
  • 34
    • 33845636894 scopus 로고    scopus 로고
    • Human Cdc14A reverses CDK1 phosphorylation of Cdc25A on serines 115 and 320
    • Esteban, V., Vázquez-Novelle, M. D., Calvo, E., Bueno, A., and Sacristán, M. P. (2006) Human Cdc14A reverses CDK1 phosphorylation of Cdc25A on serines 115 and 320. Cell Cycle. 5, 2894-2898
    • (2006) Cell Cycle. , vol.5 , pp. 2894-2898
    • Esteban, V.1    Vázquez-Novelle, M.D.2    Calvo, E.3    Bueno, A.4    Sacristán, M.P.5
  • 35
    • 0035930555 scopus 로고    scopus 로고
    • Regulation of the anaphase-promoting complex by the dual specificity phosphatase human Cdc14a
    • Bembenek, J., and Yu, H. (2001) Regulation of the anaphase-promoting complex by the dual specificity phosphatase human Cdc14a. J. Biol. Chem. 276, 48237-48242
    • (2001) J. Biol. Chem. , vol.276 , pp. 48237-48242
    • Bembenek, J.1    Yu, H.2
  • 36
    • 0041312681 scopus 로고    scopus 로고
    • The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase
    • Gray, C. H., Good, V. M., Tonks, N. K., and Barford, D. (2003) The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase. EMBO J. 22, 3524-3535
    • (2003) EMBO J. , vol.22 , pp. 3524-3535
    • Gray, C.H.1    Good, V.M.2    Tonks, N.K.3    Barford, D.4
  • 37
    • 40549097761 scopus 로고    scopus 로고
    • A functional link between the human cell cycle-regulatory phosphatase Cdc14A and the atypical mitogen-activated kinase Erk3
    • Hansen, C. A., Bartek, J., and Jensen, S. (2008) A functional link between the human cell cycle-regulatory phosphatase Cdc14A and the atypical mitogen-activated kinase Erk3. Cell Cycle. 7, 325-334
    • (2008) Cell Cycle. , vol.7 , pp. 325-334
    • Hansen, C.A.1    Bartek, J.2    Jensen, S.3
  • 38
    • 34447504029 scopus 로고    scopus 로고
    • Regulation of the Rab5 GTPase-activating protein RN-tre by the dual specificity phosphatase Cdc14A in human cells
    • Lanzetti, L., Margaria, V., Melander, F., Virgili, L., Lee, M. H., Bartek, J., and Jensen, S. (2007) Regulation of the Rab5 GTPase-activating protein RN-tre by the dual specificity phosphatase Cdc14A in human cells. J. Biol. Chem. 282, 15258-15270
    • (2007) J. Biol. Chem. , vol.282 , pp. 15258-15270
    • Lanzetti, L.1    Margaria, V.2    Melander, F.3    Virgili, L.4    Lee, M.H.5    Bartek, J.6    Jensen, S.7
  • 39
    • 79951859251 scopus 로고    scopus 로고
    • Human Cdc14B promotes progression through mitosis by dephosphorylating Cdc25 and regulating Cdk1/cyclin B activity
    • Tumurbaatar, I., Cizmecioglu, O., Hoffmann, I., Grummt, I., and Voit, R. (2011) Human Cdc14B promotes progression through mitosis by dephosphorylating Cdc25 and regulating Cdk1/cyclin B activity. PLoS One 6, e14711
    • (2011) PLoS One , vol.6 , pp. e14711
    • Tumurbaatar, I.1    Cizmecioglu, O.2    Hoffmann, I.3    Grummt, I.4    Voit, R.5
  • 41
    • 1842486792 scopus 로고    scopus 로고
    • The spindle checkpoint, aneuploidy, and cancer
    • Bharadwaj, R., and Yu, H. (2004) The spindle checkpoint, aneuploidy, and cancer. Oncogene 23, 2016-2027
    • (2004) Oncogene , vol.23 , pp. 2016-2027
    • Bharadwaj, R.1    Yu, H.2
  • 44
    • 0037586498 scopus 로고    scopus 로고
    • AURORA-A amplification overrides the mitotic spindle assembly checkpoint, inducing resistance to Taxol
    • Anand, S., Penrhyn-Lowe, S., and Venkitaraman, A. R. (2003) AURORA-A amplification overrides the mitotic spindle assembly checkpoint, inducing resistance to Taxol. Cancer Cell 3, 51-62
    • (2003) Cancer Cell , vol.3 , pp. 51-62
    • Anand, S.1    Penrhyn-Lowe, S.2    Venkitaraman, A.R.3
  • 45
    • 43749087380 scopus 로고    scopus 로고
    • B-Raf(V600E) signaling deregulates the mitotic spindle checkpoint through stabilizing Mps1 levels in melanoma cells
    • Cui, Y., and Guadagno, T. M. (2008) B-Raf(V600E) signaling deregulates the mitotic spindle checkpoint through stabilizing Mps1 levels in melanoma cells. Oncogene 27, 3122-3133
    • (2008) Oncogene , vol.27 , pp. 3122-3133
    • Cui, Y.1    Guadagno, T.M.2
  • 46
    • 25844475838 scopus 로고    scopus 로고
    • On the road to cancer: Aneuploidy and the mitotic checkpoint
    • Kops, G. J., Weaver, B. A., and Cleveland, D. W. (2005) On the road to cancer: aneuploidy and the mitotic checkpoint. Nat. Rev. Cancer 5, 773-785
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 773-785
    • Kops, G.J.1    Weaver, B.A.2    Cleveland, D.W.3
  • 47
    • 0347762556 scopus 로고    scopus 로고
    • From polyploidy to aneuploidy, genome instability and cancer
    • Storchova, Z., and Pellman, D. (2004) From polyploidy to aneuploidy, genome instability and cancer. Nat. Rev. Mol. Cell Biol. 5, 45-54
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 45-54
    • Storchova, Z.1    Pellman, D.2
  • 48
    • 84898715615 scopus 로고    scopus 로고
    • The Hippo pathway effectors TAZ and YAP in development, homeostasis and disease
    • Varelas, X. (2014) The Hippo pathway effectors TAZ and YAP in development, homeostasis and disease. Development 141, 1614-1626
    • (2014) Development , vol.141 , pp. 1614-1626
    • Varelas, X.1
  • 50
    • 70350572887 scopus 로고    scopus 로고
    • The MST1 and hMOB1 tumor suppressors control human centrosome duplication by regulating NDR kinase phosphorylation
    • Hergovich, A., Kohler, R. S., Schmitz, D., Vichalkovski, A., Cornils, H., and Hemmings, B. A. (2009) The MST1 and hMOB1 tumor suppressors control human centrosome duplication by regulating NDR kinase phosphorylation. Curr. Biol. 19, 1692-1702
    • (2009) Curr. Biol. , vol.19 , pp. 1692-1702
    • Hergovich, A.1    Kohler, R.S.2    Schmitz, D.3    Vichalkovski, A.4    Cornils, H.5    Hemmings, B.A.6
  • 51
    • 65049083167 scopus 로고    scopus 로고
    • MST2- and Furry-mediated activation of NDR1 kinase is critical for precise alignment of mitotic chromosomes
    • Chiba, S., Ikeda, M., Katsunuma, K., Ohashi, K., and Mizuno, K. (2009) MST2- and Furry-mediated activation of NDR1 kinase is critical for precise alignment of mitotic chromosomes. Curr. Biol. 19, 675-681
    • (2009) Curr. Biol. , vol.19 , pp. 675-681
    • Chiba, S.1    Ikeda, M.2    Katsunuma, K.3    Ohashi, K.4    Mizuno, K.5
  • 52
    • 77649183891 scopus 로고    scopus 로고
    • MST1 limits the kinase activity of aurora B to promote stable kinetochore-microtubule attachment
    • Oh, H. J., Kim, M. J., Song, S. J., Kim, T., Lee, D., Kwon, S. H., Choi, E. J., and Lim, D. S. (2010) MST1 limits the kinase activity of aurora B to promote stable kinetochore-microtubule attachment. Curr. Biol. 20, 416-422
    • (2010) Curr. Biol. , vol.20 , pp. 416-422
    • Oh, H.J.1    Kim, M.J.2    Song, S.J.3    Kim, T.4    Lee, D.5    Kwon, S.H.6    Choi, E.J.7    Lim, D.S.8
  • 53
    • 78649870675 scopus 로고    scopus 로고
    • Components of the Hippo pathway cooperate with Nek2 kinase to regulate centrosome disjunction
    • Mardin, B. R., Lange, C., Baxter, J. E., Hardy, T., Scholz, S. R., Fry, A. M., and Schiebel, E. (2010) Components of the Hippo pathway cooperate with Nek2 kinase to regulate centrosome disjunction. Nat. Cell Biol. 12, 1166-1176
    • (2010) Nat. Cell Biol. , vol.12 , pp. 1166-1176
    • Mardin, B.R.1    Lange, C.2    Baxter, J.E.3    Hardy, T.4    Scholz, S.R.5    Fry, A.M.6    Schiebel, E.7
  • 54
    • 84867242120 scopus 로고    scopus 로고
    • Human Mob1 proteins are required for cytokinesis by controlling microtubule stability
    • Florindo, C., Perdigão, J., Fesquet, D., Schiebel, E., Pines, J., and Tavares, A. A. (2012) Human Mob1 proteins are required for cytokinesis by controlling microtubule stability. J. Cell Sci. 125, 3085-3090
    • (2012) J. Cell Sci. , vol.125 , pp. 3085-3090
    • Florindo, C.1    Perdigão, J.2    Fesquet, D.3    Schiebel, E.4    Pines, J.5    Tavares, A.A.6
  • 55
    • 40849139691 scopus 로고    scopus 로고
    • The mob as tumor suppressor gene is essential for early development and regulates tissue growth in Drosophila
    • Shimizu, T., Ho, L. L., and Lai, Z. C. (2008) The mob as tumor suppressor gene is essential for early development and regulates tissue growth in Drosophila. Genetics 178, 957-965
    • (2008) Genetics , vol.178 , pp. 957-965
    • Shimizu, T.1    Ho, L.L.2    Lai, Z.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.