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Volumn 20, Issue 14, 2009, Pages 3422-3435

Focal adhesion kinase signaling regulates the expression of caveolin 3 and β1 integrin, genes essential for normal myoblast fusion

Author keywords

[No Author keywords available]

Indexed keywords

BETA1 INTEGRIN; CAVEOLIN 3; FOCAL ADHESION KINASE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; SMALL INTERFERING RNA;

EID: 67749101848     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E09-02-0175     Document Type: Article
Times cited : (107)

References (87)
  • 3
    • 0030068744 scopus 로고    scopus 로고
    • Myogenin expression, cell cycle withdrawal, and phenotypic differentiation are temporally separable events that precede cell fusion upon myogenesis
    • Andres, V., and Walsh, K. (1996). Myogenin expression, cell cycle withdrawal, and phenotypic differentiation are temporally separable events that precede cell fusion upon myogenesis. J. Cell Biol. 132, 657-666.
    • (1996) J. Cell Biol , vol.132 , pp. 657-666
    • Andres, V.1    Walsh, K.2
  • 4
    • 0032521681 scopus 로고    scopus 로고
    • Knockout and knockin of the beta1 exon D define distinct roles for integrin splice variants in heart function and embryonic development
    • Baudoin, C., Goumans, M. J., Mummery, C., and Sonnenberg, A. (1998). Knockout and knockin of the beta1 exon D define distinct roles for integrin splice variants in heart function and embryonic development. Genes Dev. 12, 1202-1216.
    • (1998) Genes Dev , vol.12 , pp. 1202-1216
    • Baudoin, C.1    Goumans, M.J.2    Mummery, C.3    Sonnenberg, A.4
  • 5
    • 0345550397 scopus 로고    scopus 로고
    • FAK deficiency in cells contributing to the basal lamina results in cortical abnormalities resembling congenital muscular dystrophies
    • Beggs, H. E., Schahin-Reed, D., Zang, K., Goebbels, S., Nave, K. A., Gorski, J., Jones, K. R., Sretavan, D., and Reichardt, L. F. (2003). FAK deficiency in cells contributing to the basal lamina results in cortical abnormalities resembling congenital muscular dystrophies. Neuron 40, 501-514.
    • (2003) Neuron , vol.40 , pp. 501-514
    • Beggs, H.E.1    Schahin-Reed, D.2    Zang, K.3    Goebbels, S.4    Nave, K.A.5    Gorski, J.6    Jones, K.R.7    Sretavan, D.8    Reichardt, L.F.9
  • 6
    • 0029671374 scopus 로고    scopus 로고
    • Beta 1D integrin displaces the beta 1A isoform in striated muscles: Localization at junctional structures and signaling potential in nonmuscle cells
    • Belkin, A. M., Zhidkova, N. I., Balzac, F., Altruda, F., Tomatis, D., Maier, A., Tarone, G., Koteliansky, V. E., and Burridge, K. (1996). Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells. J. Cell Biol. 132, 211-226.
    • (1996) J. Cell Biol , vol.132 , pp. 211-226
    • Belkin, A.M.1    Zhidkova, N.I.2    Balzac, F.3    Altruda, F.4    Tomatis, D.5    Maier, A.6    Tarone, G.7    Koteliansky, V.E.8    Burridge, K.9
  • 7
    • 34547924424 scopus 로고    scopus 로고
    • Increased Wnt signaling during aging alters muscle stem cell fate and increases fibrosis
    • Brack, A. S., Conboy, M. J., Roy, S., Lee, M., Kuo, C. J., Keller, C., and Rando, T. A. (2007). Increased Wnt signaling during aging alters muscle stem cell fate and increases fibrosis. Science 317, 807-810.
    • (2007) Science , vol.317 , pp. 807-810
    • Brack, A.S.1    Conboy, M.J.2    Roy, S.3    Lee, M.4    Kuo, C.J.5    Keller, C.6    Rando, T.A.7
  • 8
    • 0026445719 scopus 로고
    • Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • Burridge, K., Turner, C. E., and Romer, L. H. (1992). Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol. 119, 893-903.
    • (1992) J. Cell Biol , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 10
    • 0033963218 scopus 로고    scopus 로고
    • Integrin signaling's potential for mediating gene expression in hypertrophying skeletal muscle
    • Carson, J. A., and Wei, L. (2000). Integrin signaling's potential for mediating gene expression in hypertrophying skeletal muscle. J. Appl. Physiol. 88, 337-343.
    • (2000) J. Appl. Physiol , vol.88 , pp. 337-343
    • Carson, J.A.1    Wei, L.2
  • 11
    • 33748316507 scopus 로고    scopus 로고
    • Melanoma cell adhesion molecule is a novel marker for human fetal myogenic cells and affects myoblast fusion
    • Cerletti, M., Molloy, M. J., Tomczak, K. K., Yoon, S., Ramoni, M. F., Kho, A. T., Beggs, A. H., and Gussoni, E. (2006). Melanoma cell adhesion molecule is a novel marker for human fetal myogenic cells and affects myoblast fusion. J. Cell Sci. 119, 3117-3127.
    • (2006) J. Cell Sci , vol.119 , pp. 3117-3127
    • Cerletti, M.1    Molloy, M.J.2    Tomczak, K.K.3    Yoon, S.4    Ramoni, M.F.5    Kho, A.T.6    Beggs, A.H.7    Gussoni, E.8
  • 13
    • 4143148611 scopus 로고    scopus 로고
    • Towards a molecular pathway for myoblast fusion in Drosophila
    • Chen, E. H., and Olson, E. N. (2004). Towards a molecular pathway for myoblast fusion in Drosophila. Trends Cell Biol. 14, 452-460.
    • (2004) Trends Cell Biol , vol.14 , pp. 452-460
    • Chen, E.H.1    Olson, E.N.2
  • 14
    • 0141426586 scopus 로고    scopus 로고
    • Control of myoblast fusion by a guanine nucleotide exchange factor, loner, and its effector ARF6
    • Chen, E. H., Pryce, B. A., Tzeng, J. A., Gonzalez, G. A., and Olson, E. N. (2003). Control of myoblast fusion by a guanine nucleotide exchange factor, loner, and its effector ARF6. Cell 114, 751-762.
    • (2003) Cell , vol.114 , pp. 751-762
    • Chen, E.H.1    Pryce, B.A.2    Tzeng, J.A.3    Gonzalez, G.A.4    Olson, E.N.5
  • 17
    • 0036230877 scopus 로고    scopus 로고
    • DWnt4 regulates cell movement and focal adhesion kinase during Drosophila ovarian morphogenesis
    • Cohen, E. D., Mariol, M. C., Wallace, R. M., Weyers, J., Kamberov, Y. G., Pradel, J., and Wilder, E. L. (2002). DWnt4 regulates cell movement and focal adhesion kinase during Drosophila ovarian morphogenesis. Dev. Cell 2, 437-448.
    • (2002) Dev. Cell , vol.2 , pp. 437-448
    • Cohen, E.D.1    Mariol, M.C.2    Wallace, R.M.3    Weyers, J.4    Kamberov, Y.G.5    Pradel, J.6    Wilder, E.L.7
  • 18
    • 0027955570 scopus 로고
    • Inactivation of the N-CAM gene in mice results in size reduction of the olfactory bulb and deficits in spatial learning
    • Cremer, H., Lange, R., Christoph, A., Plomann, M., Vopper, G., Roes, J., Brown, R., Baldwin, S., Kraemer, P., and Scheff, S. (1994). Inactivation of the N-CAM gene in mice results in size reduction of the olfactory bulb and deficits in spatial learning. Nature 367, 455-459.
    • (1994) Nature , vol.367 , pp. 455-459
    • Cremer, H.1    Lange, R.2    Christoph, A.3    Plomann, M.4    Vopper, G.5    Roes, J.6    Brown, R.7    Baldwin, S.8    Kraemer, P.9    Scheff, S.10
  • 19
    • 0033548233 scopus 로고    scopus 로고
    • Stress-activated protein kinase-2/p38 and a rapamycin-sensitive pathway are required for C2C12 myogenesis
    • Cuenda, A., and Cohen, P. (1999). Stress-activated protein kinase-2/p38 and a rapamycin-sensitive pathway are required for C2C12 myogenesis. J. Biol. Chem. 274, 4341-4346.
    • (1999) J. Biol. Chem , vol.274 , pp. 4341-4346
    • Cuenda, A.1    Cohen, P.2
  • 20
    • 33745223285 scopus 로고    scopus 로고
    • de Luna, N., Gallardo, E., Soriano, M., Dominguez-Perles, R., de la Torre, C., Rojas-Garcia, R., Garcia-Verdugo, J. M., and Illa, I. (2006). Absence of dysferlin alters myogenin expression and delays human muscle differentiation in vitro. J. Biol. Chem. 281, 17092-17098.
    • de Luna, N., Gallardo, E., Soriano, M., Dominguez-Perles, R., de la Torre, C., Rojas-Garcia, R., Garcia-Verdugo, J. M., and Illa, I. (2006). Absence of dysferlin alters myogenin expression and delays human muscle differentiation "in vitro." J. Biol. Chem. 281, 17092-17098.
  • 21
    • 0033152940 scopus 로고    scopus 로고
    • Integrins: Alternative splicing as a mechanism to regulate ligand binding and integrin signaling events
    • de Melker, A. A., and Sonnenberg, A. (1999). Integrins: alternative splicing as a mechanism to regulate ligand binding and integrin signaling events. Bioessays 21, 499-509.
    • (1999) Bioessays , vol.21 , pp. 499-509
    • de Melker, A.A.1    Sonnenberg, A.2
  • 22
    • 0033527658 scopus 로고    scopus 로고
    • Integrin-mediated muscle cell spreading. The role of protein kinase c in outside-in and inside-out signaling and evidence of integrin cross-talk
    • Disatnik, M. H., and Rando, T. A. (1999). Integrin-mediated muscle cell spreading. The role of protein kinase c in outside-in and inside-out signaling and evidence of integrin cross-talk. J. Biol. Chem. 274, 32486-32492.
    • (1999) J. Biol. Chem , vol.274 , pp. 32486-32492
    • Disatnik, M.H.1    Rando, T.A.2
  • 23
    • 0030766556 scopus 로고    scopus 로고
    • Genetic analysis of myoblast fusion: Blown fuse is required for progression beyond the prefusion complex
    • Doberstein, S. K., Fetter, R. D., Mehta, A. Y., and Goodman, C. S. (1997). Genetic analysis of myoblast fusion: blown fuse is required for progression beyond the prefusion complex. J. Cell Biol. 136, 1249-1261.
    • (1997) J. Cell Biol , vol.136 , pp. 1249-1261
    • Doberstein, S.K.1    Fetter, R.D.2    Mehta, A.Y.3    Goodman, C.S.4
  • 24
    • 0028979154 scopus 로고
    • Consequences of lack of beta 1 integrin gene expression in mice
    • Fassler, R., and Meyer, M. (1995). Consequences of lack of beta 1 integrin gene expression in mice. Genes Dev. 9, 1896-1908.
    • (1995) Genes Dev , vol.9 , pp. 1896-1908
    • Fassler, R.1    Meyer, M.2
  • 25
    • 0032810190 scopus 로고    scopus 로고
    • Focal adhesion proteins FAK and paxillin increase in hypertrophied skeletal muscle
    • Fluck, M., Carson, J. A., Gordon, S. E., Ziemiecki, A., and Booth, F. W. (1999). Focal adhesion proteins FAK and paxillin increase in hypertrophied skeletal muscle. Am. J. Physiol. 277, C152-C162.
    • (1999) Am. J. Physiol , vol.277
    • Fluck, M.1    Carson, J.A.2    Gordon, S.E.3    Ziemiecki, A.4    Booth, F.W.5
  • 26
    • 35148898347 scopus 로고    scopus 로고
    • Cytoskeletal reorganization in skeletal muscle differentiation: From cell morphology to gene expression
    • suppl 1, 21-8, 21-28
    • Formigli, L., Meacci, E., Zecchi-Orlandini, S., and Orlandini, G. E. (2007). Cytoskeletal reorganization in skeletal muscle differentiation: from cell morphology to gene expression. Eur. J. Histochem. 51 (suppl 1), 21-8, 21-28.
    • (2007) Eur. J. Histochem , vol.51
    • Formigli, L.1    Meacci, E.2    Zecchi-Orlandini, S.3    Orlandini, G.E.4
  • 27
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK
    • Furuta, Y., Ilic, D., Kanazawa, S., Takeda, N., Yamamoto, T., and Aizawa, S. (1995). Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. Oncogene 11, 1989-1995.
    • (1995) Oncogene , vol.11 , pp. 1989-1995
    • Furuta, Y.1    Ilic, D.2    Kanazawa, S.3    Takeda, N.4    Yamamoto, T.5    Aizawa, S.6
  • 28
    • 0035877753 scopus 로고    scopus 로고
    • Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities
    • Galbiati, F., Engelman, J. A., Volonte, D., Zhang, X. L., Minetti, C., Li, M., Hou, H., Jr., Kneitz, B., Edelmann, W., and Lisanti, M. P. (2001). Caveolin-3 null mice show a loss of caveolae, changes in the microdomain distribution of the dystrophin-glycoprotein complex, and t-tubule abnormalities. J. Biol. Chem. 276, 21425-21433.
    • (2001) J. Biol. Chem , vol.276 , pp. 21425-21433
    • Galbiati, F.1    Engelman, J.A.2    Volonte, D.3    Zhang, X.L.4    Minetti, C.5    Li, M.6    Hou Jr., H.7    Kneitz, B.8    Edelmann, W.9    Lisanti, M.P.10
  • 29
    • 12944317278 scopus 로고    scopus 로고
    • Transgenic overexpression of caveolin-3 in skeletal muscle fibers induces a Duchenne-like muscular dystrophy phenotype
    • Galbiati, F., et al. (2000). Transgenic overexpression of caveolin-3 in skeletal muscle fibers induces a Duchenne-like muscular dystrophy phenotype. Proc. Natl. Acad. Sci. USA 97, 9689-9694.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9689-9694
    • Galbiati, F.1
  • 30
    • 0033569755 scopus 로고    scopus 로고
    • Targeted down-regulation of caveolin-3 is sufficient to inhibit myotube formation in differentiating C2C12 myoblasts. Transient activation of p38 mitogen-activated protein kinase is required for induction of caveolin-3 expression and subsequent myotube formation
    • Galbiati, F., Volonte, D., Engelman, J. A., Scherer, P. E., and Lisanti, M. P. (1999). Targeted down-regulation of caveolin-3 is sufficient to inhibit myotube formation in differentiating C2C12 myoblasts. Transient activation of p38 mitogen-activated protein kinase is required for induction of caveolin-3 expression and subsequent myotube formation. J. Biol. Chem. 274, 30315-30321.
    • (1999) J. Biol. Chem , vol.274 , pp. 30315-30321
    • Galbiati, F.1    Volonte, D.2    Engelman, J.A.3    Scherer, P.E.4    Lisanti, M.P.5
  • 31
    • 38349143073 scopus 로고    scopus 로고
    • Drosophila ELMO/CED-12 interacts with Myoblast city to direct myoblast fusion and ommatidial organization
    • Geisbrecht, E. R., Haralalka, S., Swanson, S. K., Florens, L., Washburn, M. P., and Abmayr, S. M. (2008). Drosophila ELMO/CED-12 interacts with Myoblast city to direct myoblast fusion and ommatidial organization. Dev. Biol. 314, 137-149.
    • (2008) Dev. Biol , vol.314 , pp. 137-149
    • Geisbrecht, E.R.1    Haralalka, S.2    Swanson, S.K.3    Florens, L.4    Washburn, M.P.5    Abmayr, S.M.6
  • 32
    • 0029741102 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation
    • Gilmore, A. P., and Romer, L. H. (1996). Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation. Mol. Biol. Cell 7, 1209-1224.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1209-1224
    • Gilmore, A.P.1    Romer, L.H.2
  • 33
    • 0036097773 scopus 로고    scopus 로고
    • Focal adhesion kinase tyrosine phosphorylation is associated with myogenesis and modulated by insulin
    • Goel, H. L., and Dey, C. S. (2002). Focal adhesion kinase tyrosine phosphorylation is associated with myogenesis and modulated by insulin. Cell Prolif. 35, 131-142.
    • (2002) Cell Prolif , vol.35 , pp. 131-142
    • Goel, H.L.1    Dey, C.S.2
  • 34
    • 12344250987 scopus 로고    scopus 로고
    • Focal adhesion kinase is not required for integrin function or viability in Drosophila
    • Grabbe, C., Zervas, C. G., Hunter, T., Brown, N. H., and Palmer, R. H. (2004). Focal adhesion kinase is not required for integrin function or viability in Drosophila. Development 131, 5795-5805.
    • (2004) Development , vol.131 , pp. 5795-5805
    • Grabbe, C.1    Zervas, C.G.2    Hunter, T.3    Brown, N.H.4    Palmer, R.H.5
  • 35
    • 0032562574 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathway is involved in the differentiation of muscle cells
    • Gredinger, E., Gerber, A. N., Tamir, Y., Tapscott, S. J., and Bengal, E. (1998). Mitogen-activated protein kinase pathway is involved in the differentiation of muscle cells. J. Biol. Chem. 273, 10436-10444.
    • (1998) J. Biol. Chem , vol.273 , pp. 10436-10444
    • Gredinger, E.1    Gerber, A.N.2    Tamir, Y.3    Tapscott, S.J.4    Bengal, E.5
  • 36
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan, J. L., and Shalloway, D. (1992). Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 358, 690-692.
    • (1992) Nature , vol.358 , pp. 690-692
    • Guan, J.L.1    Shalloway, D.2
  • 37
    • 0037481897 scopus 로고    scopus 로고
    • Cell biology: The molecules that make muscle
    • Gullberg, D. (2003). Cell biology: the molecules that make muscle. Nature 424, 138-140.
    • (2003) Nature , vol.424 , pp. 138-140
    • Gullberg, D.1
  • 38
    • 0032531530 scopus 로고    scopus 로고
    • Integrins during muscle development and in muscular dystrophies
    • Gullberg, D., Velling, T., Lohikangas, L., and Tiger, C. F. (1998). Integrins during muscle development and in muscular dystrophies. Front. Biosci. 3, D1039-D1050.
    • (1998) Front. Biosci , vol.3
    • Gullberg, D.1    Velling, T.2    Lohikangas, L.3    Tiger, C.F.4
  • 41
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks, S. K., Calalb, M. B., Harper, M. C., and Patel, S. K. (1992). Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. USA 89, 8487-8491.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 42
    • 0027428367 scopus 로고
    • Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions
    • Hildebrand, J. D., Schaller, M. D., and Parsons, J. T. (1993). Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions. J. Cell Biol. 123, 993-1005.
    • (1993) J. Cell Biol , vol.123 , pp. 993-1005
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 43
    • 0029055784 scopus 로고
    • Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase
    • Hildebrand, J. D., Schaller, M. D., and Parsons, J. T. (1995). Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol. Biol. Cell 6, 637-647.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 637-647
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 44
    • 0031696484 scopus 로고    scopus 로고
    • Mouse myoblasts can fuse and form a normal sarcomere in the absence of beta1 integrin expression
    • Hirsch, E., Lohikangas, L., Gullberg, D., Johansson, S., and Fassler, R. (1998). Mouse myoblasts can fuse and form a normal sarcomere in the absence of beta1 integrin expression. J. Cell Sci. 111, 2397-2409.
    • (1998) J. Cell Sci , vol.111 , pp. 2397-2409
    • Hirsch, E.1    Lohikangas, L.2    Gullberg, D.3    Johansson, S.4    Fassler, R.5
  • 45
    • 0036274017 scopus 로고    scopus 로고
    • The cell adhesion molecule M-cadherin is not essential for muscle development and regeneration
    • Hollnagel, A., Grund, C., Franke, W. W., and Arnold, H. H. (2002). The cell adhesion molecule M-cadherin is not essential for muscle development and regeneration. Mol. Cell. Biol. 22, 4760-4770.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 4760-4770
    • Hollnagel, A.1    Grund, C.2    Franke, W.W.3    Arnold, H.H.4
  • 46
    • 0037726553 scopus 로고    scopus 로고
    • IL-4 acts as a myoblast recruitment factor during mammalian muscle growth
    • Horsley, V., Jansen, K. M., Mills, S. T., and Pavlath, G. K. (2003). IL-4 acts as a myoblast recruitment factor during mammalian muscle growth. Cell 113, 483-494.
    • (2003) Cell , vol.113 , pp. 483-494
    • Horsley, V.1    Jansen, K.M.2    Mills, S.T.3    Pavlath, G.K.4
  • 47
    • 1042266471 scopus 로고    scopus 로고
    • Forming a multinucleated cell: Molecules that regulate myoblast fusion
    • Horsley, V., and Pavlath, G. K. (2004). Forming a multinucleated cell: molecules that regulate myoblast fusion. Cells Tissues Organs 176, 67-78.
    • (2004) Cells Tissues Organs , vol.176 , pp. 67-78
    • Horsley, V.1    Pavlath, G.K.2
  • 48
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. (2002). Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 49
    • 84934434314 scopus 로고    scopus 로고
    • Molecular control of mammalian myoblast fusion
    • Jansen, K. M., and Pavlath, G. K. (2008). Molecular control of mammalian myoblast fusion. Methods Mol. Biol. 475, 115-133.
    • (2008) Methods Mol. Biol , vol.475 , pp. 115-133
    • Jansen, K.M.1    Pavlath, G.K.2
  • 50
    • 38549126643 scopus 로고    scopus 로고
    • KEGG for linking genomes to life and the environment
    • Kanehisa, M., et al. (2008). KEGG for linking genomes to life and the environment. Nucleic Acids Res. 36, D480-D484.
    • (2008) Nucleic Acids Res , vol.36
    • Kanehisa, M.1
  • 51
    • 34047184207 scopus 로고    scopus 로고
    • A critical function for the actin cytoskeleton in targeted exocytosis of prefusion vesicles during myoblast fusion
    • Kim, S., Shilagardi, K., Zhang, S., Hong, S. N., Sens, K. L., Bo, J., Gonzalez, G. A., and Chen, E. H. (2007). A critical function for the actin cytoskeleton in targeted exocytosis of prefusion vesicles during myoblast fusion. Dev. Cell 12, 571-586.
    • (2007) Dev. Cell , vol.12 , pp. 571-586
    • Kim, S.1    Shilagardi, K.2    Zhang, S.3    Hong, S.N.4    Sens, K.L.5    Bo, J.6    Gonzalez, G.A.7    Chen, E.H.8
  • 52
    • 0025213307 scopus 로고
    • A role for the neural cell adhesion molecule, NCAM, in myoblast interaction during myogenesis
    • Knudsen, K. A., McElwee, S. A., and Myers, L. (1990). A role for the neural cell adhesion molecule, NCAM, in myoblast interaction during myogenesis. Dev. Biol. 138, 159-168.
    • (1990) Dev. Biol , vol.138 , pp. 159-168
    • Knudsen, K.A.1    McElwee, S.A.2    Myers, L.3
  • 53
    • 0027055575 scopus 로고
    • Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
    • Kornberg, L., Earp, H. S., Parsons, J. T., Schaller, M., and Juliano, R. L. (1992). Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J. Biol. Chem. 267, 23439-23442.
    • (1992) J. Biol. Chem , vol.267 , pp. 23439-23442
    • Kornberg, L.1    Earp, H.S.2    Parsons, J.T.3    Schaller, M.4    Juliano, R.L.5
  • 54
    • 0037214312 scopus 로고    scopus 로고
    • Phenotypic analysis of meltrin alpha (ADAM12)-deficient mice: Involvement of meltrin alpha in adipogenesis and myogenesis
    • Kurisaki, T., et al. (2003). Phenotypic analysis of meltrin alpha (ADAM12)-deficient mice: involvement of meltrin alpha in adipogenesis and myogenesis. Mol. Cell. Biol. 23, 55-61.
    • (2003) Mol. Cell. Biol , vol.23 , pp. 55-61
    • Kurisaki, T.1
  • 55
    • 34047164475 scopus 로고    scopus 로고
    • WIP/WASp-based actin-polymerization machinery is essential for myoblast fusion in Drosophila
    • Massarwa, R., Carmon, S., Shilo, B. Z., and Schejter, E. D. (2007). WIP/WASp-based actin-polymerization machinery is essential for myoblast fusion in Drosophila. Dev. Cell 12, 557-569.
    • (2007) Dev. Cell , vol.12 , pp. 557-569
    • Massarwa, R.1    Carmon, S.2    Shilo, B.Z.3    Schejter, E.D.4
  • 56
    • 0023649186 scopus 로고
    • Occupation of the extracellular matrix receptor, integrin, is a control point for myogenic differentiation
    • Menko, A. S., and Boettiger, D. (1987). Occupation of the extracellular matrix receptor, integrin, is a control point for myogenic differentiation. Cell 51, 51-57.
    • (1987) Cell , vol.51 , pp. 51-57
    • Menko, A.S.1    Boettiger, D.2
  • 57
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: In command and control of cell motility
    • Mitra, S. K., Hanson, D. A., and Schlaepfer, D. D. (2005). Focal adhesion kinase: in command and control of cell motility. Nat. Rev. Mol. Cell Biol. 6, 56-68.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 58
    • 34848897173 scopus 로고    scopus 로고
    • A role for the myoblast city homologues Dock1 and Dock5 and the adaptor proteins Crk and Crk-like in zebrafish myoblast fusion
    • Moore, C. A., Parkin, C. A., Bidet, Y., and Ingham, P. W. (2007). A role for the myoblast city homologues Dock1 and Dock5 and the adaptor proteins Crk and Crk-like in zebrafish myoblast fusion. Development 134, 3145-3153.
    • (2007) Development , vol.134 , pp. 3145-3153
    • Moore, C.A.1    Parkin, C.A.2    Bidet, Y.3    Ingham, P.W.4
  • 59
    • 0037077444 scopus 로고    scopus 로고
    • Gene expression changes during mouse skeletal myoblast differentiation revealed by transcriptional profiling
    • Moran, J. L., Li, Y., Hill, A. A., Mounts, W. M., and Miller, C. P. (2002). Gene expression changes during mouse skeletal myoblast differentiation revealed by transcriptional profiling. Physiol. Genomics 10, 103-111.
    • (2002) Physiol. Genomics , vol.10 , pp. 103-111
    • Moran, J.L.1    Li, Y.2    Hill, A.A.3    Mounts, W.M.4    Miller, C.P.5
  • 60
    • 0032519649 scopus 로고    scopus 로고
    • Organization and reorganization of neuromuscular junctions in mice lacking neural cell adhesion molecule, tenascin-C, or fibroblast growth factor-5
    • Moscoso, L. M., Cremer, H., and Sanes, J. R. (1998). Organization and reorganization of neuromuscular junctions in mice lacking neural cell adhesion molecule, tenascin-C, or fibroblast growth factor-5. J. Neurosci. 18, 1465-1477.
    • (1998) J. Neurosci , vol.18 , pp. 1465-1477
    • Moscoso, L.M.1    Cremer, H.2    Sanes, J.R.3
  • 61
    • 0025691659 scopus 로고
    • Muscle cell differentiation and alternative splicing
    • Nadal-Ginard, B. (1990). Muscle cell differentiation and alternative splicing. Curr. Opin. Cell Biol. 2, 1058-1064.
    • (1990) Curr. Opin. Cell Biol , vol.2 , pp. 1058-1064
    • Nadal-Ginard, B.1
  • 62
    • 68849126302 scopus 로고    scopus 로고
    • Nishijo, K., et al. (2009). Biomarker system for studying muscle, stem cells, and cancer in vivo. FASEB J. (in press).
    • Nishijo, K., et al. (2009). Biomarker system for studying muscle, stem cells, and cancer in vivo. FASEB J. (in press).
  • 63
    • 24144480448 scopus 로고    scopus 로고
    • Zebrafish as a model for caveolin-associated muscle disease; caveolin-3 is required for myofibril organization and muscle cell patterning
    • Nixon, S. J., Wegner, J., Ferguson, C., Mery, P. F., Hancock, J. F., Currie, P. D., Key, B., Westerfield, M., and Parton, R. G. (2005). Zebrafish as a model for caveolin-associated muscle disease; caveolin-3 is required for myofibril organization and muscle cell patterning. Hum. Mol. Genet. 14, 1727-1743.
    • (2005) Hum. Mol. Genet , vol.14 , pp. 1727-1743
    • Nixon, S.J.1    Wegner, J.2    Ferguson, C.3    Mery, P.F.4    Hancock, J.F.5    Currie, P.D.6    Key, B.7    Westerfield, M.8    Parton, R.G.9
  • 64
    • 40849119785 scopus 로고    scopus 로고
    • Myoblasts and macrophages share molecular components that contribute to cell-cell fusion
    • Pajcini, K. V., Pomerantz, J. H., Alkan, O., Doyonnas, R., and Blau, H. M. (2008). Myoblasts and macrophages share molecular components that contribute to cell-cell fusion. J. Cell Biol. 180, 1005-1019.
    • (2008) J. Cell Biol , vol.180 , pp. 1005-1019
    • Pajcini, K.V.1    Pomerantz, J.H.2    Alkan, O.3    Doyonnas, R.4    Blau, H.M.5
  • 65
    • 33947100032 scopus 로고    scopus 로고
    • Genetic analysis of p38 MAP kinases in myogenesis: Fundamental role of p38alpha in abrogating myoblast proliferation
    • Perdiguero, E., et al. (2007). Genetic analysis of p38 MAP kinases in myogenesis: fundamental role of p38alpha in abrogating myoblast proliferation. EMBO J. 26, 1245-1256.
    • (2007) EMBO J , vol.26 , pp. 1245-1256
    • Perdiguero, E.1
  • 66
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl, M. W. (2001). A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29, e45.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 67
    • 33646043789 scopus 로고    scopus 로고
    • Focal adhesion kinase is essential for costamerogenesis in cultured skeletal muscle cells
    • Quach, N. L., and Rando, T. A. (2006). Focal adhesion kinase is essential for costamerogenesis in cultured skeletal muscle cells. Dev. Biol. 293, 38-52.
    • (2006) Dev. Biol , vol.293 , pp. 38-52
    • Quach, N.L.1    Rando, T.A.2
  • 68
    • 38349118826 scopus 로고    scopus 로고
    • SCAR/WAVE and Arp2/3 are crucial for cytoskeletal remodeling at the site of myoblast fusion
    • Richardson, B. E., Beckett, K., Nowak, S. J., and Baylies, M. K. (2007). SCAR/WAVE and Arp2/3 are crucial for cytoskeletal remodeling at the site of myoblast fusion. Development 134, 4357-4367.
    • (2007) Development , vol.134 , pp. 4357-4367
    • Richardson, B.E.1    Beckett, K.2    Nowak, S.J.3    Baylies, M.K.4
  • 69
    • 0026708853 scopus 로고
    • Roles for the integrin VLA-4 and its counter receptor VCAM-1 in myogenesis
    • Rosen, G. D., Sanes, J. R., LaChance, R., Cunningham, J. M., Roman, J., and Dean, D. C. (1992). Roles for the integrin VLA-4 and its counter receptor VCAM-1 in myogenesis. Cell 69, 1107-1119.
    • (1992) Cell , vol.69 , pp. 1107-1119
    • Rosen, G.D.1    Sanes, J.R.2    LaChance, R.3    Cunningham, J.M.4    Roman, J.5    Dean, D.C.6
  • 70
    • 0028980059 scopus 로고
    • Mutations in a novel gene, myoblast city, provide evidence in support of the founder cell hypothesis for Drosophila muscle development
    • Rushton, E., Drysdale, R., Abmayr, S. M., Michelson, A. M., and Bate, M. (1995). Mutations in a novel gene, myoblast city, provide evidence in support of the founder cell hypothesis for Drosophila muscle development. Development 121, 1979-1988.
    • (1995) Development , vol.121 , pp. 1979-1988
    • Rushton, E.1    Drysdale, R.2    Abmayr, S.M.3    Michelson, A.M.4    Bate, M.5
  • 71
    • 0031956221 scopus 로고    scopus 로고
    • Myogenic conversion of NIH3T3 cells by exogenous MyoD family members: Dissociation of terminal differentiation from myotube formation
    • Russo, S., Tomatis, D., Collo, G., Tarone, G., and Tato, F. (1998). Myogenic conversion of NIH3T3 cells by exogenous MyoD family members: dissociation of terminal differentiation from myotube formation. J. Cell Sci. 111, 691-700.
    • (1998) J. Cell Sci , vol.111 , pp. 691-700
    • Russo, S.1    Tomatis, D.2    Collo, G.3    Tarone, G.4    Tato, F.5
  • 73
    • 0035948579 scopus 로고    scopus 로고
    • Biochemical signals and biological responses elicited by the focal adhesion kinase
    • Schaller, M. D. (2001). Biochemical signals and biological responses elicited by the focal adhesion kinase. Biochim. Biophys. Acta 1540, 1-21.
    • (2001) Biochim. Biophys. Acta , vol.1540 , pp. 1-21
    • Schaller, M.D.1
  • 74
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer, D. D., Hanks, S. K., Hunter, T., and van der Geer, P. (1994). Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 372, 786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    van der Geer, P.4
  • 76
    • 3142521875 scopus 로고    scopus 로고
    • Control of motile and invasive cell phenotypes by focal adhesion kinase
    • Schlaepfer, D. D., Mitra, S. K., and Ilic, D. (2004). Control of motile and invasive cell phenotypes by focal adhesion kinase. Biochim. Biophys. Acta 1692, 77-102.
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 77-102
    • Schlaepfer, D.D.1    Mitra, S.K.2    Ilic, D.3
  • 78
    • 34249793240 scopus 로고    scopus 로고
    • A conserved molecular pathway mediates myoblast fusion in insects and vertebrates
    • Srinivas, B. P., Woo, J., Leong, W. Y., and Roy, S. (2007). A conserved molecular pathway mediates myoblast fusion in insects and vertebrates. Nat. Genet. 39, 781-786.
    • (2007) Nat. Genet , vol.39 , pp. 781-786
    • Srinivas, B.P.1    Woo, J.2    Leong, W.Y.3    Roy, S.4
  • 80
    • 0033598128 scopus 로고    scopus 로고
    • Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance
    • Tachibana, I., and Hemler, M. E. (1999). Role of transmembrane 4 superfamily (TM4SF) proteins CD9 and CD81 in muscle cell fusion and myotube maintenance. J. Cell Biol. 146, 893-904.
    • (1999) J. Cell Biol , vol.146 , pp. 893-904
    • Tachibana, I.1    Hemler, M.E.2
  • 81
    • 0028984183 scopus 로고
    • A novel beta 1 integrin isoform produced by alternative splicing: Unique expression in cardiac and skeletal muscle
    • Van der Flier, A., Kuikman, I., Baudoin, C., van der Neut, R., and Sonnenberg, A. (1995). A novel beta 1 integrin isoform produced by alternative splicing: unique expression in cardiac and skeletal muscle. FEBS Lett. 369, 340-344.
    • (1995) FEBS Lett , vol.369 , pp. 340-344
    • Van der Flier, A.1    Kuikman, I.2    Baudoin, C.3    van der Neut, R.4    Sonnenberg, A.5
  • 82
    • 0035724579 scopus 로고    scopus 로고
    • Function and interactions of integrins
    • Van der Flier, A., and Sonnenberg, A. (2001). Function and interactions of integrins. Cell Tissue Res. 305, 285-298.
    • (2001) Cell Tissue Res , vol.305 , pp. 285-298
    • Van der Flier, A.1    Sonnenberg, A.2
  • 83
    • 0141429991 scopus 로고    scopus 로고
    • Modulation of myoblast fusion by caveolin-3 in dystrophic skeletal muscle cells: Implications for Duchenne muscular dystrophy and limb-girdle muscular dystrophy-1C
    • Volonte, D., Peoples, A. J., and Galbiati, F. (2003). Modulation of myoblast fusion by caveolin-3 in dystrophic skeletal muscle cells: implications for Duchenne muscular dystrophy and limb-girdle muscular dystrophy-1C. Mol. Biol. Cell 14, 4075-4088.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4075-4088
    • Volonte, D.1    Peoples, A.J.2    Galbiati, F.3
  • 85
    • 0029122431 scopus 로고
    • Involvement of M-cadherin in terminal differentiation of skeletal muscle cells
    • Zeschnigk, M., Kozian, D., Kuch, C., Schmoll, M., and Starzinski-Powitz, A. (1995). Involvement of M-cadherin in terminal differentiation of skeletal muscle cells. J. Cell Sci. 108, 2973-2981.
    • (1995) J. Cell Sci , vol.108 , pp. 2973-2981
    • Zeschnigk, M.1    Kozian, D.2    Kuch, C.3    Schmoll, M.4    Starzinski-Powitz, A.5
  • 86
    • 34447520651 scopus 로고    scopus 로고
    • Effect of cyclic stretch on beta1D-integrin expression and activation of FAK and RhoA
    • Zhang, S. J., Truskey, G. A., and Kraus, W. E. (2007). Effect of cyclic stretch on beta1D-integrin expression and activation of FAK and RhoA. Am. J. Physiol. Cell Physiol. 292, C2057-C2069.
    • (2007) Am. J. Physiol. Cell Physiol , vol.292
    • Zhang, S.J.1    Truskey, G.A.2    Kraus, W.E.3
  • 87
    • 0028978745 scopus 로고
    • Novel isoform of beta 1 integrin expressed in skeletal and cardiac muscle
    • Zhidkova, N. I., Belkin, A. M., and Mayne, R. (1995). Novel isoform of beta 1 integrin expressed in skeletal and cardiac muscle. Biochem. Biophys. Res. Commun. 214, 279-285.
    • (1995) Biochem. Biophys. Res. Commun , vol.214 , pp. 279-285
    • Zhidkova, N.I.1    Belkin, A.M.2    Mayne, R.3


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