메뉴 건너뛰기




Volumn 136, Issue 21, 2009, Pages 3597-3606

Talin 1 and 2 are required for myoblast fusion, sarcomere assembly and the maintenance of myotendinous junctions

Author keywords

Dystrophin; Integrin; Mice; Muscular dystrophy; Talin

Indexed keywords

BETA1 INTEGRIN; TALIN; TALIN 1; TALIN 2; UNCLASSIFIED DRUG;

EID: 70350164118     PISSN: 09501991     EISSN: 14779129     Source Type: Journal    
DOI: 10.1242/dev.035857     Document Type: Article
Times cited : (96)

References (62)
  • 1
    • 14044274774 scopus 로고    scopus 로고
    • Expression of connexins during differentiation and regeneration of skeletal muscle: Functional relevance of connexin43
    • Araya, R., Eckardt, D., Maxeiner, S., Kruger, O., Theis, M., Willecke, K. and Saez, J. C. (2005). Expression of connexins during differentiation and regeneration of skeletal muscle: functional relevance of connexin43. J. Cell Sci. 118, 27-37.
    • (2005) J. Cell Sci , vol.118 , pp. 27-37
    • Araya, R.1    Eckardt, D.2    Maxeiner, S.3    Kruger, O.4    Theis, M.5    Willecke, K.6    Saez, J.C.7
  • 3
    • 0028858576 scopus 로고
    • Monoclonal antibody 9EG7 defines a novel beta 1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium
    • Bazzoni, G., Shih, D. T., Buck, C. A. and Hemler, M. E. (1995). Monoclonal antibody 9EG7 defines a novel beta 1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium. J. Biol. Chem. 270, 25570-25577.
    • (1995) J. Biol. Chem , vol.270 , pp. 25570-25577
    • Bazzoni, G.1    Shih, D.T.2    Buck, C.A.3    Hemler, M.E.4
  • 4
    • 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
    • 0035325037 scopus 로고    scopus 로고
    • Purification of mouse primary myoblasts based on alpha 7 integrin expression
    • Blanco-Bose, W. E., Yao, C. C., Kramer, R. H. and Blau, H. M. (2001). Purification of mouse primary myoblasts based on alpha 7 integrin expression. Exp. Cell Res. 265, 212-220.
    • (2001) Exp. Cell Res , vol.265 , pp. 212-220
    • Blanco-Bose, W.E.1    Yao, C.C.2    Kramer, R.H.3    Blau, H.M.4
  • 10
    • 0018351620 scopus 로고
    • Duchenne muscular dystrophy: Plasma membrane loss initiates muscle cell necrosis unless it is repaired
    • Carpenter, S. and Karpati, G. (1979). Duchenne muscular dystrophy: plasma membrane loss initiates muscle cell necrosis unless it is repaired. Brain 102, 147-161.
    • (1979) Brain , vol.102 , pp. 147-161
    • Carpenter, S.1    Karpati, G.2
  • 11
    • 0030994017 scopus 로고    scopus 로고
    • Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages
    • Choquet, D., Felsenfeld, D. P. and Sheetz, M. P. (1997). Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages. Cell 88, 39-48.
    • (1997) Cell , vol.88 , pp. 39-48
    • Choquet, D.1    Felsenfeld, D.P.2    Sheetz, M.P.3
  • 12
    • 46749156984 scopus 로고    scopus 로고
    • Progressive myopathy and defects in the maintenance of myotendinous junctions in mice that lack talin 1 in skeletal muscle
    • Conti, F. J., Felder, A., Monkley, S., Schwander, M., Wood, M. R., Lieber, R., Critchley, D. and Müller, U. (2008). Progressive myopathy and defects in the maintenance of myotendinous junctions in mice that lack talin 1 in skeletal muscle. Development 135, 2043-2053.
    • (2008) Development , vol.135 , pp. 2043-2053
    • Conti, F.J.1    Felder, A.2    Monkley, S.3    Schwander, M.4    Wood, M.R.5    Lieber, R.6    Critchley, D.7    Müller, U.8
  • 13
    • 0142106350 scopus 로고    scopus 로고
    • Talin loss-of-function uncovers roles in cell contractility and migration in C. elegans
    • Cram, E. J., Clark, S. G. and Schwarzbauer, J. E. (2003). Talin loss-of-function uncovers roles in cell contractility and migration in C. elegans. J. Cell Sci. 116, 3871-3878.
    • (2003) J. Cell Sci , vol.116 , pp. 3871-3878
    • Cram, E.J.1    Clark, S.G.2    Schwarzbauer, J.E.3
  • 14
    • 33747753150 scopus 로고    scopus 로고
    • Loss of FilaminC (FLNc) results in severe defects in myogenesis and myotube structure
    • Dalkilic, I., Schienda, J., Thompson, T. G. and Kunkel, L. M. (2006). Loss of FilaminC (FLNc) results in severe defects in myogenesis and myotube structure. Mol. Cell. Biol. 26, 6522-6534.
    • (2006) Mol. Cell. Biol , vol.26 , pp. 6522-6534
    • Dalkilic, I.1    Schienda, J.2    Thompson, T.G.3    Kunkel, L.M.4
  • 17
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith, C. G., Yamada, K. M. and Sheetz, M. P. (2002). The relationship between force and focal complex development. J. Cell Biol. 159, 695-705.
    • (2002) J. Cell Biol , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 18
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk
    • Geiger, B., Bershadsky, A., Pankov, R. and Yamada, K. M. (2001). Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk. Nat. Rev. Mol. Cell Biol. 2, 793-805.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 19
    • 0242361579 scopus 로고    scopus 로고
    • Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation
    • Giannone, G., Jiang, G., Sutton, D. H., Critchley, D. R. and Sheetz, M. P. (2003). Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation. J. Cell Biol. 163, 409-419.
    • (2003) J. Cell Biol , vol.163 , pp. 409-419
    • Giannone, G.1    Jiang, G.2    Sutton, D.H.3    Critchley, D.R.4    Sheetz, M.P.5
  • 20
    • 33947212046 scopus 로고    scopus 로고
    • Myoblast proliferation and syncytial fusion both depend on connexin43 function in transfected skeletal muscle primary cultures
    • Gorbe, A., Krenacs, T., Cook, J. E. and Becker, D. L. (2007). Myoblast proliferation and syncytial fusion both depend on connexin43 function in transfected skeletal muscle primary cultures. Exp. Cell Res. 313, 1135-1148.
    • (2007) Exp. Cell Res , vol.313 , pp. 1135-1148
    • Gorbe, A.1    Krenacs, T.2    Cook, J.E.3    Becker, D.L.4
  • 22
    • 0028170643 scopus 로고
    • Alpha v integrin subunit is predominantly located in nervous tissue and skeletal muscle during mouse development
    • Hirsch, E., Gullberg, D., Balzac, F., Altruda, F., Silengo, L. and Tarone, G. (1994). Alpha v integrin subunit is predominantly located in nervous tissue and skeletal muscle during mouse development. Dev. Dyn. 201, 108-120.
    • (1994) Dev. Dyn , vol.201 , pp. 108-120
    • Hirsch, E.1    Gullberg, D.2    Balzac, F.3    Altruda, F.4    Silengo, L.5    Tarone, G.6
  • 24
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes, R. O. (1992). Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 25
    • 55749114582 scopus 로고    scopus 로고
    • The atypical Rac activator Dock180 (Dock1) regulates myoblast fusion in vivo
    • Laurin, M., Fradet, N., Blangy, A., Hall, A., Vuori, K. and Cote, J. F. (2008). The atypical Rac activator Dock180 (Dock1) regulates myoblast fusion in vivo. Proc. Natl. Acad. Sci. USA 105, 15446-15451.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15446-15451
    • Laurin, M.1    Fradet, N.2    Blangy, A.3    Hall, A.4    Vuori, K.5    Cote, J.F.6
  • 26
    • 0037938677 scopus 로고    scopus 로고
    • Erbb2 regulates neuromuscular synapse formation and is essential for muscle spindle development
    • Leu, M., Bellmunt, E., Schwander, M., Farinas, I., Brenner, H. R. and Muller, U. (2003). Erbb2 regulates neuromuscular synapse formation and is essential for muscle spindle development. Development 130, 2291-2301.
    • (2003) Development , vol.130 , pp. 2291-2301
    • Leu, M.1    Bellmunt, E.2    Schwander, M.3    Farinas, I.4    Brenner, H.R.5    Muller, U.6
  • 27
    • 0033378656 scopus 로고    scopus 로고
    • Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats
    • Li, F., Zhang, Y. and Wu, C. (1999). Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats. J. Cell Sci. 112, 4589-4599.
    • (1999) J. Cell Sci , vol.112 , pp. 4589-4599
    • Li, F.1    Zhang, Y.2    Wu, C.3
  • 28
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-binding proteins
    • Liu, S., Calderwood, D. A. and Ginsberg, M. H. (2000). Integrin cytoplasmic domain-binding proteins. J. Cell Sci. 113, 3563-3571.
    • (2000) J. Cell Sci , vol.113 , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2    Ginsberg, M.H.3
  • 29
    • 0038158092 scopus 로고    scopus 로고
    • Integrins: Redundant or important players in skeletal muscle?
    • Mayer, U. (2003). Integrins: redundant or important players in skeletal muscle? J. Biol. Chem. 278, 14587-14590.
    • (2003) J. Biol. Chem , vol.278 , pp. 14587-14590
    • Mayer, U.1
  • 31
    • 0030908297 scopus 로고    scopus 로고
    • The I/LWEQ module: A conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals
    • McCann, R. O. and Craig, S. W. (1997). The I/LWEQ module: a conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc. Natl. Acad. Sci. USA 94, 5679-5684.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5679-5684
    • McCann, R.O.1    Craig, S.W.2
  • 32
    • 0033539916 scopus 로고    scopus 로고
    • Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein:actin interaction
    • McCann, R. O. and Craig, S. W. (1999). Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein:actin interaction. Biochem. Biophys. Res. Commun. 266, 135-140.
    • (1999) Biochem. Biophys. Res. Commun , vol.266 , pp. 135-140
    • McCann, R.O.1    Craig, S.W.2
  • 33
    • 0033372459 scopus 로고    scopus 로고
    • Organization of the myotendinous junction is dependent on the presence of alpha7beta1 integrin
    • Miosge, N., Klenczar, C., Herken, R., Willem, M. and Mayer, U. (1999). Organization of the myotendinous junction is dependent on the presence of alpha7beta1 integrin. Lab. Invest. 79, 1591-1599.
    • (1999) Lab. Invest , vol.79 , pp. 1591-1599
    • Miosge, N.1    Klenczar, C.2    Herken, R.3    Willem, M.4    Mayer, U.5
  • 36
    • 1642341451 scopus 로고    scopus 로고
    • Talin: An emerging focal point of adhesion dynamics
    • Nayal, A., Webb, D. J. and Horwitz, A. F. (2004). Talin: an emerging focal point of adhesion dynamics. Curr. Opin. Cell Biol. 16, 94-98.
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 94-98
    • Nayal, A.1    Webb, D.J.2    Horwitz, A.F.3
  • 37
    • 37549029679 scopus 로고    scopus 로고
    • Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo
    • Nieswandt, B., Moser, M., Pleines, I., Varga-Szabo, D., Monkley, S., Critchley, D. and Fassler, R. (2007). Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo. J. Exp. Med. 204, 3113-3118.
    • (2007) J. Exp. Med , vol.204 , pp. 3113-3118
    • Nieswandt, B.1    Moser, M.2    Pleines, I.3    Varga-Szabo, D.4    Monkley, S.5    Critchley, D.6    Fassler, R.7
  • 38
    • 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
  • 41
    • 0032563558 scopus 로고    scopus 로고
    • Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated embryonic stem cells
    • Priddle, H., Hemmings, L., Monkley, S., Woods, A., Patel, B., Sutton, D., Dunn, G. A., Zicha, D. and Critchley, D. R. (1998). Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated embryonic stem cells. J. Cell Biol. 142, 1121-1133.
    • (1998) J. Cell Biol , vol.142 , pp. 1121-1133
    • Priddle, H.1    Hemmings, L.2    Monkley, S.3    Woods, A.4    Patel, B.5    Sutton, D.6    Dunn, G.A.7    Zicha, D.8    Critchley, D.R.9
  • 42
    • 67749101848 scopus 로고    scopus 로고
    • Focal Adhesion Kinase Signaling Regulates the Expression of Caveolin 3 and beta1 Integrin, Genes Essential for Normal Myoblast Fusion
    • Quach, N. L., Biressi, S., Reichardt, L. F., Keller, C. and Rando, T. A. (2009). Focal Adhesion Kinase Signaling Regulates the Expression of Caveolin 3 and beta1 Integrin, Genes Essential for Normal Myoblast Fusion. Mol. Biol. Cell 20, 3422-3435.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3422-3435
    • Quach, N.L.1    Biressi, S.2    Reichardt, L.F.3    Keller, C.4    Rando, T.A.5
  • 43
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism
    • Riveline, D., Zamir, E., Balaban, N. Q., 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 mDia1-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
  • 45
    • 0016829688 scopus 로고
    • Segmental fiber breakdown and defects of the plasmalemma in diseased human muscles
    • Schmalbruch, H. (1975). Segmental fiber breakdown and defects of the plasmalemma in diseased human muscles. Acta Neuropathol. 33, 129-141.
    • (1975) Acta Neuropathol , vol.33 , pp. 129-141
    • Schmalbruch, H.1
  • 47
    • 0029566108 scopus 로고
    • A cre-transgenic mouse strain for the ubiquitous deletion of loxP-flanked gene segments including deletion in germ cells
    • Schwenk, F., Baron, U. and Rajewsky, K. (1995). A cre-transgenic mouse strain for the ubiquitous deletion of loxP-flanked gene segments including deletion in germ cells. Nucleic Acids Res. 23, 5080-5081.
    • (1995) Nucleic Acids Res , vol.23 , pp. 5080-5081
    • Schwenk, F.1    Baron, U.2    Rajewsky, K.3
  • 48
    • 28244491001 scopus 로고    scopus 로고
    • Gene duplication and functional divergence during evolution of the cytoskeletal linker protein talin
    • Senetar, M. A. and McCann, R. O. (2005). Gene duplication and functional divergence during evolution of the cytoskeletal linker protein talin. Gene 362, 141-152.
    • (2005) Gene , vol.362 , pp. 141-152
    • Senetar, M.A.1    McCann, R.O.2
  • 49
    • 10644221869 scopus 로고    scopus 로고
    • Intrasteric inhibition mediates the interaction of the I/LWEQ module proteins Talin1, Talin2, Hip1, and Hip12 with actin
    • Senetar, M. A., Foster, S. J. and McCann, R. O. (2004). Intrasteric inhibition mediates the interaction of the I/LWEQ module proteins Talin1, Talin2, Hip1, and Hip12 with actin. Biochemistry 43, 15418-15428.
    • (2004) Biochemistry , vol.43 , pp. 15418-15428
    • Senetar, M.A.1    Foster, S.J.2    McCann, R.O.3
  • 50
    • 33847217997 scopus 로고    scopus 로고
    • Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle
    • Senetar, M. A., Moncman, C. L. and McCann, R. O. (2007). Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle. Cell Motil. Cytoskeleton 64, 157-173.
    • (2007) Cell Motil. Cytoskeleton , vol.64 , pp. 157-173
    • Senetar, M.A.1    Moncman, C.L.2    McCann, R.O.3
  • 51
    • 0030051130 scopus 로고    scopus 로고
    • Tenascin-C expression in dystrophin-related muscular dystrophy
    • Settles, D. L., Cihak, R. A. and Erickson, H. P. (1996). Tenascin-C expression in dystrophin-related muscular dystrophy. Muscle Nerve 19, 147-154.
    • (1996) Muscle Nerve , vol.19 , pp. 147-154
    • Settles, D.L.1    Cihak, R.A.2    Erickson, H.P.3
  • 52
    • 33747854588 scopus 로고    scopus 로고
    • Cytoplasmic gamma-actin is not required for skeletal muscle development but its absence leads to a progressive myopathy
    • Sonnemann, K. J., Fitzsimons, D. P., Patel, J. R., Liu, Y., Schneider, M. F., Moss, R. L. and Ervasti, J. M. (2006). Cytoplasmic gamma-actin is not required for skeletal muscle development but its absence leads to a progressive myopathy. Dev. Cell 11, 387-397.
    • (2006) Dev. Cell , vol.11 , pp. 387-397
    • Sonnemann, K.J.1    Fitzsimons, D.P.2    Patel, J.R.3    Liu, Y.4    Schneider, M.F.5    Moss, R.L.6    Ervasti, J.M.7
  • 54
    • 0030783172 scopus 로고    scopus 로고
    • Animal models for muscular dystrophy show different patterns of sarcolemmal disruption
    • Straub, V., Rafael, J. A., Chamberlain, J. S. and Campbell, K. P. (1997). Animal models for muscular dystrophy show different patterns of sarcolemmal disruption. J. Cell Biol. 139, 375-385.
    • (1997) J. Cell Biol , vol.139 , pp. 375-385
    • Straub, V.1    Rafael, J.A.2    Chamberlain, J.S.3    Campbell, K.P.4
  • 57
    • 0032476651 scopus 로고    scopus 로고
    • Taverna, D., Disatnik, M. H., Rayburn, H., Bronson, R. T., Yang, J., Rando, T. A. and Hynes, R. O. (1998). Dystrophic muscle in mice chimeric for expression of alpha5 integrin. J. Cell Biol. 143, 849-859.
    • Taverna, D., Disatnik, M. H., Rayburn, H., Bronson, R. T., Yang, J., Rando, T. A. and Hynes, R. O. (1998). Dystrophic muscle in mice chimeric for expression of alpha5 integrin. J. Cell Biol. 143, 849-859.
  • 59
    • 0020520291 scopus 로고
    • A comparison of the contractile properties of the human gastrocnemius and soleus muscles
    • Vandervoort, A. A. and McComas, A. J. (1983). A comparison of the contractile properties of the human gastrocnemius and soleus muscles. Eur. J. Appl. Physiol. Occup. Physiol. 51, 435-440.
    • (1983) Eur. J. Appl. Physiol. Occup. Physiol , vol.51 , pp. 435-440
    • Vandervoort, A.A.1    McComas, A.J.2
  • 61
    • 0025662048 scopus 로고
    • Dystrophin-deficient mdx muscle fibers are preferentially vulnerable to necrosis induced by experimental lengthening contractions
    • Weller, B., Karpati, G. and Carpenter, S. (1990). Dystrophin-deficient mdx muscle fibers are preferentially vulnerable to necrosis induced by experimental lengthening contractions. J. Neurol. Sci. 100, 9-13.
    • (1990) J. Neurol. Sci , vol.100 , pp. 9-13
    • Weller, B.1    Karpati, G.2    Carpenter, S.3
  • 62
    • 51049100594 scopus 로고    scopus 로고
    • Talin depletion reveals independence of initial cell spreading from integrin activation and traction
    • Zhang, X., Jiang, G., Cai, Y., Monkley, S. J., Critchley, D. R. and Sheetz, M. P. (2008). Talin depletion reveals independence of initial cell spreading from integrin activation and traction. Nat. Cell Biol. 10, 1062-1068.
    • (2008) Nat. Cell Biol , vol.10 , pp. 1062-1068
    • Zhang, X.1    Jiang, G.2    Cai, Y.3    Monkley, S.J.4    Critchley, D.R.5    Sheetz, M.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.