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Volumn 120, Issue 3, 2007, Pages 456-467

Filamin links cell shape and cytoskeletal structure to Rho regulation by controlling accumulation of p190RhoGAP in lipid rafts

Author keywords

Actin cytoskeleton; Extracellular matrix; Filamin; p190RhoGAP; Rho

Indexed keywords

ACTIN; FILAMIN; PROTEIN P190; RHO FACTOR; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; SMALL INTERFERING RNA;

EID: 33847419281     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.03353     Document Type: Article
Times cited : (90)

References (59)
  • 1
    • 0035158377 scopus 로고    scopus 로고
    • RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity
    • Arthur, W. T. and Burridge, K. (2001). RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity. Mol. Biol. Cell 12, 2711-2720.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2711-2720
    • Arthur, W.T.1    Burridge, K.2
  • 2
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism
    • Arthur, W. T., Petch, L. A. and Burridge, K. (2000). Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism. Curr. Biol. 10, 719-722.
    • (2000) Curr. Biol. , vol.10 , pp. 719-722
    • Arthur, W.T.1    Petch, L.A.2    Burridge, K.3
  • 3
    • 0034734992 scopus 로고    scopus 로고
    • Evidence that beta3 integrin-induced Rae activation involves the calpain-dependent formation of integrin clusters that are distinct from the focal complexes and focal adhesions that form as Rac and RhoA become active
    • Bialkowska, K., Kulkarni, S., Du, X., Gull, D. E., Saido, T. C. and Fox, J. E. (2000). Evidence that beta3 integrin-induced Rae activation involves the calpain-dependent formation of integrin clusters that are distinct from the focal complexes and focal adhesions that form as Rac and RhoA become active. J. Cell Biol. 151, 685-696.
    • (2000) J. Cell Biol. , vol.151 , pp. 685-696
    • Bialkowska, K.1    Kulkarni, S.2    Du, X.3    Gull, D.E.4    Saido, T.C.5    Fox, J.E.6
  • 4
    • 0035071323 scopus 로고    scopus 로고
    • p190RhoGAP is the pricipal Src substrate in brain and regulates axon outgrowth, guidance and fasciculation
    • Brouns, M. R., Matheson, S. E and Settleman, J. (2001). p190RhoGAP is the pricipal Src substrate in brain and regulates axon outgrowth, guidance and fasciculation Nat. Cell Biol. 3, 361-367.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 361-367
    • Brouns, M.R.1    Matheson, S.E.2    Settleman, J.3
  • 5
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D. A. and London, E. (1998). Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14, 111-136.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 6
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge, K. and Wennerberg, K. (2004). Rho and Rac take center stage. Cell 116 167-179.
    • (2004) Cell , vol.116 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 11
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K. and Tuschl, T. (2001). Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411, 494-498.
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 12
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville, S. and Hall, A. (2002). Rho GTPases in cell biology. Nature 420, 629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 13
    • 7944237936 scopus 로고    scopus 로고
    • The many faces of filamin: A versatile molecular scaffold for cell motility and signalling
    • Feng, Y. and Walsh, C. A. (2004). The many faces of filamin: A versatile molecular scaffold for cell motility and signalling. Nat. Cell Biol. 6, 1034-1038.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1034-1038
    • Feng, Y.1    Walsh, C.A.2
  • 14
    • 2342494362 scopus 로고    scopus 로고
    • Lipid rafts and apical membrane traffic
    • Fullekrug, J. and Simons, K. (2004). Lipid rafts and apical membrane traffic. Ann N.Y. Acad. Sci. 1014, 164-169.
    • (2004) Ann N.Y. Acad. Sci. , vol.1014 , pp. 164-169
    • Fullekrug, J.1    Simons, K.2
  • 15
    • 0036168356 scopus 로고    scopus 로고
    • Cutting to the chase: Calpain proteases in cell motility
    • Glading, A., Lauffenburger, D. A. and Wells, A. (2002). Cutting to the chase: calpain proteases in cell motility. Trends Cell Biol. 12, 46-54.
    • (2002) Trends Cell Biol. , vol.12 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3
  • 17
    • 0036842936 scopus 로고    scopus 로고
    • Reciprocal raft-receptor interactions and the assembly of adhesion complexes
    • Harris, T. J. and Siu, C. H. (2002). Reciprocal raft-receptor interactions and the assembly of adhesion complexes. BioEssays 24, 996-1003.
    • (2002) BioEssays , vol.24 , pp. 996-1003
    • Harris, T.J.1    Siu, C.H.2
  • 18
    • 0142027011 scopus 로고    scopus 로고
    • Mechanisms of force generation and transmission by myofibroblasts
    • Hinz, B. and Gabbiani, G. (2003). Mechanisms of force generation and transmission by myofibroblasts. Curr. Opin. Biotechnol. 14, 538-546.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 538-546
    • Hinz, B.1    Gabbiani, G.2
  • 19
    • 0000463651 scopus 로고    scopus 로고
    • The structural and mechanical complexity of cell-growth control
    • Huang, S. and Ingber, D. E. (1999). The structural and mechanical complexity of cell-growth control. Nat. Cell Biol. 1, E131-E138.
    • (1999) Nat. Cell Biol. , vol.1
    • Huang, S.1    Ingber, D.E.2
  • 20
    • 0031739360 scopus 로고    scopus 로고
    • Control of cyclin D1, p27(Kip1) and cell cycle progression in human capillary endothelial cells by cell shape and cytoskeletal tension
    • Huang, S., Chen, C. S. and Ingber, D. E. (1998). Control of cyclin D1, p27(Kip1) and cell cycle progression in human capillary endothelial cells by cell shape and cytoskeletal tension. Mol. Biol. Cell 9, 3179-3193.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3179-3193
    • Huang, S.1    Chen, C.S.2    Ingber, D.E.3
  • 21
    • 0025998068 scopus 로고
    • Extracellular matrix and cell shape; potential control point for inhibition of angiogenesis
    • Ingber, D. (1991). Extracellular matrix and cell shape; potential control point for inhibition of angiogenesis. J. Cell. Biochem. 47, 236-241.
    • (1991) J. Cell. Biochem. , vol.47 , pp. 236-241
    • Ingber, D.1
  • 22
    • 0025372477 scopus 로고
    • Fibronectin controls capillary endothelial cell growth by modulating cell shape
    • Ingber, D. E. (1990). Fibronectin controls capillary endothelial cell growth by modulating cell shape. Proc. Natl. Acad. Sci. USA 87, 3579-3583.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3579-3583
    • Ingber, D.E.1
  • 23
    • 0037452771 scopus 로고    scopus 로고
    • Mechanosensation through integrins: Cells act locally but think globally
    • Ingber, D. E. (2003). Mechanosensation through integrins: cells act locally but think globally. Proc. Natl. Acad. Sci. USA 100, 1472-1474.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1472-1474
    • Ingber, D.E.1
  • 24
    • 11344265267 scopus 로고    scopus 로고
    • An FF domain-dependent protein interaction mediates a signaling pathway for growth factor-induced gene expression
    • Jiang, W., Sordella, R., Chen, G. C., Hakre, S., Roy, A. L. and Settleman, J. (2005a). An FF domain-dependent protein interaction mediates a signaling pathway for growth factor-induced gene expression. Mol. Cell 17, 23-35.
    • (2005) Mol. Cell , vol.17 , pp. 23-35
    • Jiang, W.1    Sordella, R.2    Chen, G.C.3    Hakre, S.4    Roy, A.L.5    Settleman, J.6
  • 26
    • 0042733080 scopus 로고    scopus 로고
    • Initiation and transduction of stretch-induced RhoA and Rac 1 activation through caveolae: Cytoskeletal regulation of ERK translocation
    • Kawamura, S., Miyamoto, S. and Brown, J. H. (2003). Initiation and transduction of stretch-induced RhoA and Rac 1 activation through caveolae: cytoskeletal regulation of ERK translocation. J. Biol. Chem. 278, 31111-31117.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31111-31117
    • Kawamura, S.1    Miyamoto, S.2    Brown, J.H.3
  • 27
    • 0037025350 scopus 로고    scopus 로고
    • Calpain cleaves RhoA generating a dominant-negative form that inhibits integrin-induced actin filament assembly an cell spreading
    • Kulkarni, S., Goll, D. E. and Fox, J. E. (2002). Calpain cleaves RhoA generating a dominant-negative form that inhibits integrin-induced actin filament assembly an cell spreading. J. Biol. Chem. 277, 24435-24441.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24435-24441
    • Kulkarni, S.1    Goll, D.E.2    Fox, J.E.3
  • 28
    • 0037447060 scopus 로고    scopus 로고
    • Filamin-A fragment localizes to the nucleus to regulate androgen receptor and coactivator functions
    • Loy, C. J., Sim, K. S. and Yong, E. L. (2003). Filamin-A fragment localizes to the nucleus to regulate androgen receptor and coactivator functions. Proc. Natl. Acad. Sci. USA 100, 4562-4567.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4562-4567
    • Loy, C.J.1    Sim, K.S.2    Yong, E.L.3
  • 29
    • 0037455574 scopus 로고    scopus 로고
    • RhoA is required for cortical retraction and rigidity during mitotic cell rounding
    • Maddox, A. S. and Burridge, K. (2003). RhoA is required for cortical retraction and rigidity during mitotic cell rounding. J Cell Biol. 160, 255-265.
    • (2003) J Cell Biol. , vol.160 , pp. 255-265
    • Maddox, A.S.1    Burridge, K.2
  • 30
    • 2942707853 scopus 로고    scopus 로고
    • Role of RhoA, mDia, and ROCK in cell shape-dependent control of the Skp2-p27kip1 pathway,and the G1/S transition
    • Mammoto, A., Huang, S., Moore, K., Oh, P. and Ingber, D. E. (2004). Role of RhoA, mDia, and ROCK in cell shape-dependent control of the Skp2-p27kip1 pathway,and the G1/S transition. J. Biol. Chem. 279, 26323-26330.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26323-26330
    • Mammoto, A.1    Huang, S.2    Moore, K.3    Oh, P.4    Ingber, D.E.5
  • 31
    • 33644967727 scopus 로고    scopus 로고
    • Cellular adaptation to mechanical stress: Role of integrins, Rho, cytoskeletal tension and mechanosensitive ion channels
    • Matthews, B. D., Overby, D. R., Mannix, R. and Ingber, D. E. (2006). Cellular adaptation to mechanical stress: role of integrins, Rho, cytoskeletal tension and mechanosensitive ion channels. J. Cell Sci. 119, 508-518.
    • (2006) J. Cell Sci. , vol.119 , pp. 508-518
    • Matthews, B.D.1    Overby, D.R.2    Mannix, R.3    Ingber, D.E.4
  • 32
    • 1842426730 scopus 로고    scopus 로고
    • Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage conmitment
    • McBeath, P Pirone, D. M., Nelson, C. M., Bhadriraju, & and Chen, C. (2004). Cell shape, cytoskeletal tension, and RhoA regulate stem cell lineage conmitment. Dev. Cell 6, 483-495.
    • (2004) Dev. Cell , vol.6 , pp. 483-495
    • McBeath, R.1    Pirone, D.M.2    Nelson, C.M.3    Bhadriraju, K.4    Chen, C.S.5
  • 33
    • 0034282248 scopus 로고    scopus 로고
    • Mechanical control of cyclic AM? signalling and gene transcription through integrins
    • Meyer, C. J., Alenghat, F. J., Rim, P., Fong, J. H., Fabry, B. and Ingber, D. E. (2000). Mechanical control of cyclic AM? signalling and gene transcription through integrins. Nat. Cell Biol. 2, 666-668.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 666-668
    • Meyer, C.J.1    Alenghat, F.J.2    Rim, P.3    Fong, J.H.4    Fabry, B.5    Ingber, D.E.6
  • 34
    • 0033597894 scopus 로고    scopus 로고
    • Polarized distribution of endogenous Rac1 and RhoA at the cell surface
    • Michaely, P. A., Mneo, C., Ying, Y. S. and Anderson, R. G. (1999). Polarized distribution of endogenous Rac1 and RhoA at the cell surface. J. Biol. Chem. 274, 21430-21436.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21430-21436
    • Michaely, P.A.1    Mneo, C.2    Ying, Y.S.3    Anderson, R.G.4
  • 35
    • 0025943943 scopus 로고
    • Ligand-sensitive binding of actin-binding protein to immunoglobulin G Fc receptor I (Fc garruna RI)
    • Ohta, Y., Stossel, T. P. and Hartwig, J. H. (1991). Ligand-sensitive binding of actin-binding protein to immunoglobulin G Fc receptor I (Fc garruna RI). Cell 67, 275-282.
    • (1991) Cell , vol.67 , pp. 275-282
    • Ohta, Y.1    Stossel, T.P.2    Hartwig, J.H.3
  • 37
    • 33746658154 scopus 로고    scopus 로고
    • FilGAP, a Rho- and ROCK-regulated GAP for Rae binds filamin A to control actin remodelling
    • Ohta, Y., Hartwig, J. H. and Stossel, T. P. (2006). FilGAP, a Rho- and ROCK-regulated GAP for Rae binds filamin A to control actin remodelling. Nat. Cell Biol. 8,803-814.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 803-814
    • Ohta, Y.1    Hartwig, J.H.2    Stossel, T.P.3
  • 41
    • 0028817908 scopus 로고
    • Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex
    • Plopper, G. E., McNamee, H. P., Dike, L. E., Bojanowski, K. and Ingber, D. E. (1995). Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mot. Biol. Cell 6, 1349-1365.
    • (1995) Mot. Biol. Cell , vol.6 , pp. 1349-1365
    • Plopper, G.E.1    McNamee, H.P.2    Dike, L.E.3    Bojanowski, K.4    Ingber, D.E.5
  • 42
    • 1442276317 scopus 로고    scopus 로고
    • Extracellular matrix controls myosin light chain phosphorylation and cell contractility through modulation of cell shape and cytoskeletal prestress
    • Polte, T. R., Eichler, G. S., Wang, N. and Ingber, D. E. (2004). Extracellular matrix controls myosin light chain phosphorylation and cell contractility through modulation of cell shape and cytoskeletal prestress. Am. J. Physiol. Cell Physiol. 286, C518-C528.
    • (2004) Am. J. Physiol. Cell Physiol. , vol.286
    • Polte, T.R.1    Eichler, G.S.2    Wang, N.3    Ingber, D.E.4
  • 43
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X. D., Mosses, W. B. and Schwartz, M. A. (1999). Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J 18, 578-585.
    • (1999) EMBO J , vol.18 , pp. 578-585
    • Ren, X.D.1    Mosses, W.B.2    Schwartz, M.A.3
  • 44
    • 0033731010 scopus 로고    scopus 로고
    • Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover
    • Ren, X. D., Mosses, W. B., Sieg, D. J., Otey, C. A., Schlaepfer, D. D. and Schwartz, M. A. (2000). Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. J. Cell Sci. 113, 3673-3678.
    • (2000) J. Cell Sci. , vol.113 , pp. 3673-3678
    • Ren, X.D.1    Mosses, W.B.2    Sieg, D.J.3    Otey, C.A.4    Schlaepfer, D.D.5    Schwartz, M.A.6
  • 45
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDial-dependent and ROCK-independent mechanism
    • Riveline, D., Zamir, E., Balaban, N. Q.9 Schwarz, U. S., Ishizaki, T., Narumiya, S., Kam, Z., Geiger, B. and Bershadsky, A. D. (2001). Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDial-dependent and ROCK-independent mechanism. J Cell Biol. 153, 1175-1186.
    • (2001) J Cell Biol. , vol.153 , pp. 1175-1186
    • Riveline, D.1    Zamir, E.2    Balaban, N.Q.3    Schwarz, U.S.4    Ishizaki, T.5    Narumiya, S.6    Kam, Z.7    Geiger, B.8    Bershadsky, A.D.9
  • 46
    • 0037641217 scopus 로고    scopus 로고
    • Effects of rho kinase and actin stress fibers on sustained extracellular signal-regulaLed kinase activity and activation of G(1) phase cyclin-dependent kinases
    • Roovers, K. and Assoian, R. K. (2003). Effects of rho kinase and actin stress fibers on sustained extracellular signal-regulaLed kinase activity and activation of G(1) phase cyclin-dependent kinases. Mol. Cell. Biol. 23, 4283-4294.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4283-4294
    • Roovers, K.1    Assoian, R.K.2
  • 47
    • 0020044056 scopus 로고
    • Action of cytochalasin D on cytoskeletal networks
    • Schliwa, M. (1982). Action of cytochalasin D on cytoskeletal networks. J. Cell Biol. 92, 79-91.
    • (1982) J. Cell Biol. , vol.92 , pp. 79-91
    • Schliwa, M.1
  • 48
  • 49
    • 0028820041 scopus 로고
    • A detergent-free method for purifying caveolac membrane from tissue culture cells
    • Smart, E. J., Ying, Y. S., Mineo, C. and Anderson, R. G. (1995). A detergent-free method for purifying caveolac membrane from tissue culture cells. Proc. Natl. Acad. Sci. USA 92, 10104-10108.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10104-10108
    • Smart, E.J.1    Ying, Y.S.2    Mineo, C.3    Anderson, R.G.4
  • 50
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains
    • Song, K. S., Li, S., Okamoto, T., Quilliam, L. A., Sargiacomo, M. and Lisanti, M. P. (1996). Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae microdomains. Detergent-free purification of caveolae microdomains. J. Biol. Chem. 271, 9690-9697.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9690-9697
    • Song, K.S.1    Li, S.2    Okamoto, T.3    Quilliam, L.A.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 51
    • 0037453716 scopus 로고    scopus 로고
    • Modulation of Rho GTPase signaling regulates a switch between adipogenesis and myogenesis
    • Sordella, R., Jiang, W., Chen, G. C., Carlo, M. and Settleman, J. (2003). Modulation of Rho GTPase signaling regulates a switch between adipogenesis and myogenesis. Cell 113, 147-158.
    • (2003) Cell , vol.113 , pp. 147-158
    • Sordella, R.1    Jiang, W.2    Chen, G.C.3    Carlo, M.4    Settleman, J.5
  • 52
    • 0024360298 scopus 로고
    • Latrunculins - Novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D
    • Spector, I, Shochet, N. R., Blasberger, D. and Kashman, Y, (1989). Latrunculins - novel marine macrolides that disrupt microfilament organization and affect cell growth: I. Comparison with cytochalasin D. Cell Motil. Cytoskeleton 13, 127-144.
    • (1989) Cell Motil. Cytoskeleton , vol.13 , pp. 127-144
    • Spector, I.1    Shochet, N.R.2    Blasberger, D.3    Kashman, Y.4
  • 53
    • 0033973279 scopus 로고    scopus 로고
    • Identification of filamin as a novel ligand for caveolin-1: Evidence for the organization of caveolin- 1 -associated membrane domains by the actin cytoskeleton
    • Stablhut, M. and van Deurs, B. (2000). Identification of filamin as a novel ligand for caveolin-1: evidence for the organization of caveolin- 1 -associated membrane domains by the actin cytoskeleton. Mot. Biol. Cell 11, 325-337.
    • (2000) Mot. Biol. Cell , vol.11 , pp. 325-337
    • Stablhut, M.1    van Deurs, B.2
  • 56
    • 0037459068 scopus 로고    scopus 로고
    • The carboxy-terminal pleckstrin homology domain of ROCK interacts with filarrun-A
    • Ueda, K., Ohta, Y. and Hosoya, H. (2003). The carboxy-terminal pleckstrin homology domain of ROCK interacts with filarrun-A. Biochem. Biophys. Res. Commun. 301, 886-890.
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 886-890
    • Ueda, K.1    Ohta, Y.2    Hosoya, H.3
  • 59
    • 3342896372 scopus 로고    scopus 로고
    • Roles played by a subset of integrin signaling molecules in cadherin-based cell-cell adhesion
    • Yano, H., Mazaki, Y., Kurokawa, K., Hanks, S. K., Matsuda, M. and Sabe, H. (2004). Roles played by a subset of integrin signaling molecules in cadherin-based cell-cell adhesion. J. Cell Biol. 166, 283-295.
    • (2004) J. Cell Biol. , vol.166 , pp. 283-295
    • Yano, H.1    Mazaki, Y.2    Kurokawa, K.3    Hanks, S.K.4    Matsuda, M.5    Sabe, H.6


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