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Volumn 238, Issue 6, 2009, Pages 1526-1534

Molecular mechanisms of mechanosensing in muscle development

Author keywords

Integrin; Muscle development; Sarcomere; Z disk; Zasp

Indexed keywords

INTEGRIN; TALIN;

EID: 66349097466     PISSN: 10588388     EISSN: 10970177     Source Type: Journal    
DOI: 10.1002/dvdy.21972     Document Type: Review
Times cited : (17)

References (99)
  • 1
    • 33846246384 scopus 로고    scopus 로고
    • Force as a Facilitator of Integrin Conformational Changes during Leukocyte Arrest on Blood Vessels and Antigen-Presenting Cells
    • DOI 10.1016/j.immuni.2007.01.002, PII S1074761307001021
    • Alon R, Dustin ML. 2007. Force as a facilitator of integrin conformational changes during leukocyte arrest on blood vessels and antigen-presenting cells. Immunity 26:17-27. (Pubitemid 46109349)
    • (2007) Immunity , vol.26 , Issue.1 , pp. 17-27
    • Alon, R.1    Dustin, M.L.2
  • 2
    • 0028073676 scopus 로고
    • Muscle LIM protein, a novel essential regulator of myogenesis, promotes myogenic differentiation
    • DOI 10.1016/0092-8674(94)90192-9
    • Arber S, Halder G, Caroni P. 1994. Muscle LIM protein, a novel essential regulator of myogenesis, promotes myogenic differentiation. Cell 79:221-231. (Pubitemid 24324913)
    • (1994) Cell , vol.79 , Issue.2 , pp. 221-231
    • Arber, S.1    Halder, G.2    Caroni, P.3
  • 4
    • 11144358221 scopus 로고    scopus 로고
    • Solution structure of ZASP PDZ domain: Implications for sarcomere ultrastructure and enigma family redundancy
    • DOI 10.1016/j.str.2004.02.019, PII S0969212604000619
    • Au Y, Atkinson RA, Guerrini R, Kelly G, Joseph C, Martin SR, Muskett FW, Pallavicini A, Faulkner G, Pastore A. 2004. Solution structure of ZASP PDZ domain; implications for sarcomere ultrastructure and enigma family redundancy. Structure 12:611-622. (Pubitemid 38447164)
    • (2004) Structure , vol.12 , Issue.4 , pp. 611-622
    • Au, Y.1    Atkinson, R.A.2    Guerrini, R.3    Kelly, G.4    Joseph, C.5    Martin, S.R.6    Muskett, F.W.7    Pallavicini, A.8    Faulkner, G.9    Pastore, A.10
  • 6
    • 0022458171 scopus 로고
    • Localization of talin in skeletal and cardiac muscles
    • DOI 10.1016/0014-5793(86)80505-1
    • Belkin AM, Zhidkova NI, Koteliansky VE. 1986. Localization of talin in skeletal and cardiac muscles. FEBS Lett 200:32-36. (Pubitemid 16067862)
    • (1986) FEBS Letters , vol.200 , Issue.1 , pp. 32-36
    • Belkin, A.M.1    Zhidkova, N.I.2    Koteliansky, V.E.3
  • 8
    • 33748309166 scopus 로고    scopus 로고
    • Adhesion-mediated mechanosensitivity: A time to experiment, and a time to theorize
    • DOI 10.1016/j.ceb.2006.08.012, PII S0955067406001232
    • Bershadsky A, Kozlov M, Geiger B. 2006. Adhesion-mediated mechanosensitivity: a time to experiment, and a time to theorize. Curr Opin Cell Biol 18:472-481. (Pubitemid 44332917)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.5 , pp. 472-481
    • Bershadsky, A.1    Kozlov, M.2    Geiger, B.3
  • 9
    • 0031961418 scopus 로고    scopus 로고
    • Genetic analysis of the Drosophila alpha(PS2) integrin subunit reveals discrete adhesive, morphogenetic and sarcomeric functions
    • Bloor JW, Brown NH. 1998. Genetic analysis of the Drosophila alphaPS2 integrin subunit reveals discrete adhesive, morphogenetic and sarcomeric functions. Genetics 148:1127-1142. (Pubitemid 28169024)
    • (1998) Genetics , vol.148 , Issue.3 , pp. 1127-1142
    • Bloor, J.W.1    Brown, N.H.2
  • 10
    • 0023663872 scopus 로고
    • The Drosophila PS2 antigen is an invertebrate integrin that, like the fibronectin receptor, becomes localized to muscle attachments
    • Bogaert T, Brown N, Wilcox M. 1987. The Drosophila PS2 antigen is an invertebrate integrin that, like the fibronectin receptor, becomes localized to muscle attachments. Cell 51:929-940.
    • (1987) Cell , vol.51 , pp. 929-940
    • Bogaert, T.1    Brown, N.2    Wilcox, M.3
  • 11
    • 21744441321 scopus 로고    scopus 로고
    • Structural dynamics of alpha-actinin-vinculin interactions
    • Bois PRJ, Borgon RA, Vonrhein C, Izard T. 2005. Structural dynamics of alpha-actinin-vinculin interactions. Mol Cell Biol 25:6112-6122.
    • (2005) Mol Cell Biol , vol.25 , pp. 6112-6122
    • Bois, P.R.J.1    Borgon, R.A.2    Vonrhein, C.3    Izard, T.4
  • 12
    • 44449148944 scopus 로고    scopus 로고
    • The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate beta 1 and beta 3 integrins
    • Bouaouina M, Lad Y, Calderwood DA. 2008. The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate beta 1 and beta 3 integrins. J Biol Chem 283:6118-6125.
    • (2008) J Biol Chem , vol.283 , pp. 6118-6125
    • Bouaouina, M.1    Lad, Y.2    Calderwood, D.A.3
  • 13
    • 0028173625 scopus 로고
    • Null mutations in the alpha(PS2) and beta(PS) integrin subunit genes have distinct phenotypes
    • Brown NH. 1994. Null mutations in the alphaPS2 and betaPS integrin subunit genes have distinct phenotypes. Development 120:1221-1231. (Pubitemid 24150047)
    • (1994) Development , vol.120 , Issue.5 , pp. 1221-1231
    • Brown, N.H.1
  • 16
    • 0346656820 scopus 로고    scopus 로고
    • N-RAP scaffolds I-Z-I assembly during myofibrillogenesis in cultured chick cardiomyocytes
    • DOI 10.1242/jcs.00847
    • Carroll S, Lu SJ, Herrera AH, Horowits R. 2004. N-RAP scaffolds I-Z-I assembly during myofibrillogenesis in cultured chick cardiomyocytes. J Cell Sci 117:105-114. (Pubitemid 38072125)
    • (2004) Journal of Cell Science , vol.117 , Issue.1 , pp. 105-114
    • Carroll, S.1    Lu, S.2    Herrera, A.H.3    Horowits, R.4
  • 18
    • 0038409304 scopus 로고    scopus 로고
    • Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes
    • DOI 10.1242/dev.00492
    • Clark KA, McGrail M, Beckerle MC. 2003. Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes. Development 130:2611-2621. (Pubitemid 37069578)
    • (2003) Development , vol.130 , Issue.12 , pp. 2611-2621
    • Clark, K.A.1    McGrail, M.2    Beckerle, M.C.3
  • 19
    • 34347328247 scopus 로고    scopus 로고
    • The Drosophila muscle LIM protein, Mlp84B, cooperates with D-titin to maintain muscle structural integrity
    • DOI 10.1242/jcs.000695
    • Clark KA, Bland JM, Beckerle MC. 2007. The Drosophila muscle LIM protein, Mlp84B, cooperates with D-titin to maintain muscle structural integrity. J Cell Sci 120:2066-2077. (Pubitemid 47010002)
    • (2007) Journal of Cell Science , vol.120 , Issue.12 , pp. 2066-2077
    • Clark, K.A.1    Bland, J.M.2    Beckerle, M.C.3
  • 20
    • 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 FJ, Felder A, Monkley S, Schwander M, Wood MR, Lieber R, Critchley D, Mueller 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    Mueller, U.8
  • 22
    • 0026739841 scopus 로고
    • Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes
    • Danowski BA, Imanaka-Yoshida K, Sanger JM, Sanger JW. 1992. Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes. J Cell Biol 118:1411-1420.
    • (1992) J Cell Biol , vol.118 , pp. 1411-1420
    • Danowski, B.A.1    Imanaka-Yoshida, K.2    Sanger, J.M.3    Sanger, J.W.4
  • 24
    • 33846309701 scopus 로고    scopus 로고
    • Integrins and the actin cytoskeleton
    • DOI 10.1016/j.ceb.2006.12.013, PII S0955067406001943
    • Delon I, Brown NH. 2007. Integrins and the actin cytoskeleton. Curr Opin Cell Biol 19:43-50. (Pubitemid 46123977)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.1 , pp. 43-50
    • Delon, I.1    Brown, N.H.2
  • 25
    • 44349162202 scopus 로고    scopus 로고
    • Cardiac myofibrillogenesis inside intact embryonic hearts
    • Du A, Sanger JM, Sanger JW. 2008. Cardiac myofibrillogenesis inside intact embryonic hearts. Dev Biol 318:236-246.
    • (2008) Dev Biol , vol.318 , pp. 236-246
    • Du, A.1    Sanger, J.M.2    Sanger, J.W.3
  • 26
    • 45249084352 scopus 로고    scopus 로고
    • Bending of z-lines by mechanical stimuli: An input signal for integrin dependent modulation of ion channels?
    • Dyachenko V, Christ A, Gubanov R, Isenberg G. 2008. Bending of z-lines by mechanical stimuli: an input signal for integrin dependent modulation of ion channels? Prog Biophys Mol Biol 97:196-216.
    • (2008) Prog Biophys Mol Biol , vol.97 , pp. 196-216
    • Dyachenko, V.1    Christ, A.2    Gubanov, R.3    Isenberg, G.4
  • 27
    • 0028028999 scopus 로고
    • Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin
    • Erickson HP. 1994. Reversible unfolding of fibronectin type-III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin. Proc Natl Acad Sci USA 91:10114-10118. (Pubitemid 24985043)
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , Issue.21 , pp. 10114-10118
    • Erickson, H.P.1
  • 28
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls alpha5beta1 function
    • Friedland JC, Lee MH, Boettiger D. 2009. Mechanically activated integrin switch controls alpha5beta1 function. Science 323:642-644.
    • (2009) Science , vol.323 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 29
    • 0032434538 scopus 로고    scopus 로고
    • Characterization of lethal Drosophila melanogaster alpha-actinin mutants
    • DOI 10.1023/A:1018789227987
    • Fyrberg C, Ketchum A, Ball E, Fyrberg E. 1998. Characterization of lethal Drosophila melanogaster alpha-actinin mutants. Biochem Genet 36:299-310. (Pubitemid 29048355)
    • (1998) Biochemical Genetics , vol.36 , Issue.9-10 , pp. 299-310
    • Fyrberg, C.1    Ketchum, A.2    Ball, E.3    Fyrberg, E.4
  • 30
    • 0025325694 scopus 로고
    • Molecular genetics of Drosophila alpha-actinin: Mutant alleles disrupt Z disc integrity and muscle insertions
    • DOI 10.1083/jcb.110.6.1999
    • Fyrberg E, Kelly M, Ball E, Fyrberg C, Reedy MC. 1990. Molecular genetics of Drosophila alpha-actinin: mutant alleles disrupt Z disc integrity and muscle insertions. J Cell Biol 110:1999-2011. (Pubitemid 20183158)
    • (1990) Journal of Cell Biology , vol.110 , Issue.6 , pp. 1999-2011
    • Fyrberg, E.1    Kelly, M.2    Ball, E.3    Fyrberg, C.4    Reedy, M.C.5
  • 31
    • 38349004559 scopus 로고    scopus 로고
    • Deletion of integrin-linked kinase from skeletal muscles of mice resembles muscular dystrophy due to alpha 7 beta 1-integrin deficiency
    • Gheyara AL, Vallejo-Illarramendi A, Zang K, Mei L, St-Arnaud R, Dedhar S, Reichardt LF. 2007. Deletion of integrin-linked kinase from skeletal muscles of mice resembles muscular dystrophy due to alpha 7 beta 1-integrin deficiency. Am J Pathol 171:1966-1977.
    • (2007) Am J Pathol , vol.171 , pp. 1966-1977
    • Gheyara, A.L.1    Vallejo-Illarramendi, A.2    Zang, K.3    Mei, L.4    St-Arnaud, R.5    Dedhar, S.6    Reichardt, L.F.7
  • 32
    • 0025868336 scopus 로고
    • Studies of the alpha-actinin/actin interaction in the Z-disk by using calpain
    • Goll DE, Dayton WR, Singh I, Robson RM. 1991. Studies of the alpha-actinin actin interaction in the Z-Disk by using calpain. J Biol Chem 266:8501-8510. (Pubitemid 21906538)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.13 , pp. 8501-8510
    • Goll, D.E.1    Dayton, W.R.2    Singh, I.3    Robson, R.M.4
  • 34
    • 0028030002 scopus 로고
    • Increased protein kinase C and isozyme redistribution in pressure-overload cardiac hypertrophy in the rat
    • Gu X, Bishop SP. 1994. Increased Protein-Kinase-C and isozyme redistribution in pressure-overload cardiac-hypetrophy in the rat. Circ Res 75:926-931. (Pubitemid 24323527)
    • (1994) Circulation Research , vol.75 , Issue.5 , pp. 926-931
    • Gu, X.1    Bishop, S.P.2
  • 35
    • 0034484456 scopus 로고    scopus 로고
    • Translocation of PKC isoforms in bovine aortic smooth muscle cells exposed to strain
    • Han O, Takei T, Basson M, Sumpio BE. 2001. Translocation of PKC isoforms in bovine aortic smooth muscle cells exposed to strain. J Cell Biochem 80:367-372.
    • (2001) J Cell Biochem , vol.80 , pp. 367-372
    • Han, O.1    Takei, T.2    Basson, M.3    Sumpio, B.E.4
  • 38
    • 0026683672 scopus 로고
    • The role of beta 1 integrin in spreading and myofibrillogenesis in neonatal rat cardiomyocytes in vitro
    • Hilenski LL, Ma XH, Vinson N, Terracio L, Borg TK. 1992. The role of beta 1 integrin in spreading and myofibrillogenesis in neonatal rat cardiomyocytes in vitro. Cell Motil Cytoskeleton 21:87-100.
    • (1992) Cell Motil Cytoskeleton , vol.21 , pp. 87-100
    • Hilenski, L.L.1    Ma, X.H.2    Vinson, N.3    Terracio, L.4    Borg, T.K.5
  • 39
    • 40149107045 scopus 로고    scopus 로고
    • How force might activate talin's vinculin binding sites: SMD reveals a structural mechanism
    • Hytonen VP, Vogel V. 2008. How force might activate talin's vinculin binding sites: SMD reveals a structural mechanism. PLoS Comput Biol 4.
    • (2008) PLoS Comput Biol , pp. 4
    • Hytonen, V.P.1    Vogel, V.2
  • 40
    • 0033040088 scopus 로고    scopus 로고
    • Vinculin, talin, integrin alpha 6 beta 1 and laminin can serve as components of attachment complex mediating contraction force transmission from cardiomyocytes to extracellular matrix
    • DOI 10.1002/(SICI)1097-0169(1999)42:1<1::AID-CM1>3.0.CO;2-0
    • Imanaka-Yoshida K, Enomoto-Iwamoto M, Yoshida T, Sakakura T. 1999. Vinculin, talin, integrin alpha 6 beta 1 and laminin can serve as components of attachment complex mediating contraction force transmission from cardiomyocytes to extracellular matrix. Cell Motil Cytoskeleton 42:1-11. (Pubitemid 29144319)
    • (1999) Cell Motility and the Cytoskeleton , vol.42 , Issue.1 , pp. 1-11
    • Imanaka-Yoshida, K.1    Enomoto-Iwamoto, M.2    Yoshida, T.3    Sakakura, T.4
  • 41
    • 38049040363 scopus 로고    scopus 로고
    • Zasp is required for the assembly of functional integrin adhesion sites
    • Jani K, Schöck F. 2007. Zasp is required for the assembly of functional integrin adhesion sites. J Cell Biol 179:1583-1597.
    • (2007) J Cell Biol , vol.179 , pp. 1583-1597
    • Jani, K.1    Schöck, F.2
  • 42
    • 9944231967 scopus 로고    scopus 로고
    • Conversion between three conformational states of integrin I domains with a C-terminal pull spring studied with molecular dynamics
    • DOI 10.1016/j.str.2004.10.005, PII S0969212604003739
    • Jin M, Andricioaei L, Springer TA. 2004. Conversion between three conformational states of integrin I domains with a C-terminal pull spring studied with molecular dynamics. Structure 12:2137-2147. (Pubitemid 39593193)
    • (2004) Structure , vol.12 , Issue.12 , pp. 2137-2147
    • Jin, M.1    Andricioaei, I.2    Springer, T.A.3
  • 43
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson RP, Craig SW. 1994. An intramolecular association between the head and tail domains of vinculin modulates talin binding. J Biol Chem 269:12611-12619. (Pubitemid 24202049)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.17 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 44
    • 33644815614 scopus 로고    scopus 로고
    • Force-induced unfolding of the focal adhesion targeting domain and the influence of Paxillin binding
    • Kaazempur-Mofrad MR, Golgi J, Abdula Rahim NA, Kamm RD. 2004. Force-induced unfolding of the focal adhesion targeting domain and the influence of Paxillin binding. Mech Chem Biosyst 1:253-265.
    • (2004) Mech Chem Biosyst , vol.1 , pp. 253-265
    • Kaazempur-Mofrad, M.R.1    Golgi, J.2    Abdula Rahim, N.A.3    Kamm, R.D.4
  • 45
    • 20444465227 scopus 로고    scopus 로고
    • Integrin activation and matrix binding mediate cellular responses to mechanical stretch
    • DOI 10.1074/jbc.C400455200
    • Katsumi A, Naoe T, Matsushita T, Kaibuchi K, Schwartz MA. 2005. Integrin activation and matrix binding mediate cellular responses to mechanical stretch. J Biol Chem 280:16546-16549. (Pubitemid 41389109)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 16546-16549
    • Katsumi, A.1    Naoe, T.2    Matsushita, T.3    Kaibuchi, K.4    Schwartz, M.A.5
  • 46
    • 13844253573 scopus 로고    scopus 로고
    • Identification of the beta1-integrin binding site on alpha-actinin by cryoelectron microscopy
    • DOI 10.1016/j.jsb.2004.11.010
    • Kelly DF, Taylor KA. 2005. Identification of the beta1-integrin binding site on alpha-actinin by cryoelectron microscopy. J Struct Biol 149:290-302. (Pubitemid 40250063)
    • (2005) Journal of Structural Biology , vol.149 , Issue.3 , pp. 290-302
    • Kelly, D.F.1    Taylor, K.A.2
  • 47
    • 2942735211 scopus 로고    scopus 로고
    • The ZASP-like motif in actinin-associated LIM protein is required for interaction with the alpha-actinin rod and for targeting to the muscle Z-line
    • DOI 10.1074/jbc.M401871200
    • Klaavuniemi T, Kelloniemi A, Ylänne J. 2004. The ZASP-like motif in actinin-associated LIM protein is required for interaction with the alpha-actinin rod and for targeting to the muscle Z-line. J Biol Chem 279:26402-26410. (Pubitemid 38798792)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.25 , pp. 26402-26410
    • Klaavuniemi, T.1    Kelloniemi, A.2    Ylanne, J.3
  • 50
    • 0035158546 scopus 로고    scopus 로고
    • Focal adhesion kinase and p130Cas mediate both sarcomeric organization and activation of genes associated with cardiac myocyte hypertrophy
    • Kovacic-Milivojevic B, Roediger F, Almeida EAC, Damsky CH, Gardner DG, Ilic D. 2001. Focal adhesion kinase and p130Cas mediate both sarcomeric organization and activation of genes associated with cardiac myocyte hypertrophy. Mol Biol Cell 12:2290-2307. (Pubitemid 33051957)
    • (2001) Molecular Biology of the Cell , vol.12 , Issue.8 , pp. 2290-2307
    • Kovacic-Milivojevic, B.1    Roediger, F.2    Almeida, E.A.C.3    Damsky, C.H.4    Gardner, D.G.5    Ilic, D.6
  • 52
    • 0033548441 scopus 로고    scopus 로고
    • Identification of protein-disulfide isomerase activity in fibronectin
    • Langenbach KJ, Sottile J. 1999. Identification of protein-disulfide isomerase activity in fibronectin. J Biol Chem 274:7032-7038. (Pubitemid 129504987)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.2-11 , pp. 7032-7038
    • Langenbach, K.J.1    Sottile, J.2
  • 53
    • 61449220945 scopus 로고    scopus 로고
    • Genetic and cell biological analysis of integrin outside-in signaling
    • Legate KR, Wickstrom SA, Fässler R. 2009. Genetic and cell biological analysis of integrin outside-in signaling. Genes Dev 23:397-418.
    • (2009) Genes Dev , vol.23 , pp. 397-418
    • Legate, K.R.1    Wickstrom, S.A.2    Fässler, R.3
  • 54
    • 0024965992 scopus 로고
    • The function of PS integrins during Drosophila embryogenesis
    • Leptin M, Bogaert T, Lehmann R, Wilcox M. 1989. The function of PS integrins during Drosophila embryogenesis. Cell 56:401-408.
    • (1989) Cell , vol.56 , pp. 401-408
    • Leptin, M.1    Bogaert, T.2    Lehmann, R.3    Wilcox, M.4
  • 56
    • 0037009042 scopus 로고    scopus 로고
    • Integrin activation takes shape
    • DOI 10.1083/jcb.200206011
    • Liddington RC, Ginsberg MH. 2002. Integrin activation takes shape. J Cell Biol 158:833-839. (Pubitemid 35001074)
    • (2002) Journal of Cell Biology , vol.158 , Issue.5 , pp. 833-839
    • Liddington, R.C.1    Ginsberg, M.H.2
  • 57
    • 39749137483 scopus 로고    scopus 로고
    • Sense and stretchability: The role of titin and titin-associated proteins in myocardial stress-sensing and mechanical dysfunction
    • Linke WA. 2008. Sense and stretchability: the role of titin and titin-associated proteins in myocardial stress-sensing and mechanical dysfunction. Cardiovasc Res 77:637-648.
    • (2008) Cardiovasc Res , vol.77 , pp. 637-648
    • Linke, W.A.1
  • 60
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • DOI 10.1146/annurev.immunol.25.022106.141618
    • Luo BH, Carman CV, Springer TA. 2007. Structural basis of integrin regulation and signaling. Annu Rev Immunol 25:619-647. (Pubitemid 46697919)
    • (2007) Annual Review of Immunology , vol.25 , pp. 619-647
    • Luo, B.-H.1    Carman, C.V.2    Springer, T.A.3
  • 61
    • 1642263252 scopus 로고    scopus 로고
    • Restoration of Resting Sarcomere Length after Uniaxial Static Strain Is Regulated by Protein Kinase C epsilon and Focal Adhesion Kinase
    • DOI 10.1161/01.RES.0000121101.32286.C8
    • Mansour H, de Tombe PP, Samarel AM, Russell B. 2004. Restoration of resting sarcomere length after uniaxial static strain is regulated by protein kinase C epsilon and focal adhesion kinase. Circ Res 94:642-649. (Pubitemid 38387747)
    • (2004) Circulation Research , vol.94 , Issue.5 , pp. 642-649
    • Mansour, H.1    De Tombe, P.P.2    Samarel, A.M.3    Russell, B.4
  • 63
    • 0035115798 scopus 로고    scopus 로고
    • Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils
    • Minajeva A, Kulke M, Fernandez JM, Linke WA. 2001. Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils. Biophys J 80:1442-1451. (Pubitemid 32182167)
    • (2001) Biophysical Journal , vol.80 , Issue.3 , pp. 1442-1451
    • Minajeva, A.1    Kulke, M.2    Fernandez, J.M.3    Linke, W.A.4
  • 64
    • 24344442455 scopus 로고    scopus 로고
    • Focal adhesion kinase mediates MEF2 and c-Jun activation by stretch: Role in the activation of the cardiac hypertrophic genetic program
    • DOI 10.1016/j.cardiores.2005.05.011, PII S0008636305002531
    • Nadruz W, Corat MAF, Marin TM, Pereira GAG, Franchini KG. 2005. Focal adhesion kinase mediates MEF2 and c-Jun activation by stretch: role in the activation of the cardiac hypertrophic genetic program. Cardiovasc Res 68:87-97. (Pubitemid 41253559)
    • (2005) Cardiovascular Research , vol.68 , Issue.1 , pp. 87-97
    • Nadruz Jr., W.1    Corat, M.A.F.2    Marin, T.M.3    Guimaraes Pereira, G.A.4    Franchini, K.G.5
  • 65
    • 2442481067 scopus 로고    scopus 로고
    • alpha-actinin revisited: A fresh look at an old player
    • DOI 10.1002/cm.20007
    • Otey CA, Carpen O. 2004. Alpha-actinin revisited: a fresh look at an old player. Cell Motil Cytoskeleton 58:104-111. (Pubitemid 38697587)
    • (2004) Cell Motility and the Cytoskeleton , vol.58 , Issue.2 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 66
    • 0025291522 scopus 로고
    • An interaction between alpha-actinin and beta-1 integrin subunit in vitro
    • Otey CA, Pavalko FM, Burridge K. 1990. An interaction between alpha-actinin and beta-1 integrin subunit in vitro. J Cell Biol 111:721-729.
    • (1990) J Cell Biol , vol.111 , pp. 721-729
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 67
    • 11144269771 scopus 로고    scopus 로고
    • PKC mediates cyclic stretch-induced cardiac hypertrophy through Rho family GTPases and mitogen-activated protein kinases in cardiomyocytes
    • DOI 10.1002/jcp.20151
    • Pan J, Singh US, Takahashi T, Oka Y, Palm-Leis A, Herbelin BS, Baker KM. 2005. PKC mediates cyclic stretch-induced cardiac hypertrophy through Rho family GTPases and mitogen-activated protein kinases in cardiomyocytes. J Cell Physiol 202:536-553. (Pubitemid 40041325)
    • (2005) Journal of Cellular Physiology , vol.202 , Issue.2 , pp. 536-553
    • Pan, J.1    Singh, U.S.2    Takahashi, T.3    Oka, Y.4    Palm-Leis, A.5    Herbelin, B.S.6    Baker, K.M.7
  • 68
    • 0010935732 scopus 로고
    • A vinculin-containing cortical lattice in skeletal muscle: Transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma
    • Pardo JV, Siliciano JD, Craig SW. 1983. A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma. Proc Natl Acad Sci USA 80:1008-1012.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 1008-1012
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 69
    • 0035033212 scopus 로고    scopus 로고
    • Adult mice deficient in actinin-associated LIM-domain protein reveal a developmental pathway for right ventricular cardiomyopathy
    • DOI 10.1038/87920
    • Pashmforoush M, Pomies P, Peterson KL, Kubalak S, Ross J Jr, Hefti A, Aebi U, Beckerle MC, Chien KR. 2001. Adult mice deficient in actinin-associated LIM-domain protein reveal a developmental pathway for right ventricular cardiomyopathy. Nat Med 7:591-597. (Pubitemid 32448327)
    • (2001) Nature Medicine , vol.7 , Issue.5 , pp. 591-597
    • Pashmforoush, M.1    Pomies, P.2    Peterson, K.L.3    Kubalak, S.4    Ross Jr., J.5    Hefti, A.6    Aebi, U.7    Beckerle, M.C.8    Chien, K.R.9
  • 70
    • 0032832968 scopus 로고    scopus 로고
    • Purification and characterization of an alpha-actinin-binding PDZ-LIM protein that is up-regulated during muscle differentiation
    • DOI 10.1074/jbc.274.41.29242
    • Pomies P, Macalma T, Beckerle MC. 1999. Purification and characterization of an alpha-actinin-binding PDZ-LIM protein that is up-regulated during muscle differentiation. J Biol Chem 274:29242-29250. (Pubitemid 29477090)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.41 , pp. 29242-29250
    • Pomies, P.1    Macalma, T.2    Beckerle, M.C.3
  • 71
    • 43449130018 scopus 로고    scopus 로고
    • Zebrafish integrin-linked kinase is required in skeletal muscles for strengthening the integrin-ECM adhesion complex
    • Postel R, Vakeel P, Topczewski J, Knöll R, Bakkers J. 2008. Zebrafish integrin-linked kinase is required in skeletal muscles for strengthening the integrin-ECM adhesion complex. Dev Biol 318:92-101.
    • (2008) Dev Biol , vol.318 , pp. 92-101
    • Postel, R.1    Vakeel, P.2    Topczewski, J.3    Knöll, R.4    Bakkers, J.5
  • 72
    • 0030042104 scopus 로고    scopus 로고
    • Identification and localization of an actin-binding motif that is unique to the epsilon isoform of protein kinase C and participates in the regulation of synaptic function
    • Prekeris R, Mayhew MW, Cooper JB, Terrian DM. 1996. Identification and localization of an actin-binding motif that is unique to the epsilon isoform of protein kinase C and participates in the regulation of synaptic function. J Cell Biol 132:77-90. (Pubitemid 26035076)
    • (1996) Journal of Cell Biology , vol.132 , Issue.1-2 , pp. 77-90
    • Prekeris, R.1    Mayhew, M.W.2    Cooper, J.B.3    Terrian, D.M.4
  • 73
    • 0032500583 scopus 로고    scopus 로고
    • Molecular analysis of the interactions between protein kinase C-epsilon and filamentous actin
    • DOI 10.1074/jbc.273.41.26790
    • Prekeris R, Hernandez RM, Mayhew MW, White MK, Terrian DM. 1998. Molecular analysis of the interactions between protein kinase C-epsilon and filamentous actin. J Biol Chem 273:26790-26798. (Pubitemid 28471696)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26790-26798
    • Prekeris, R.1    Hernandez, R.M.2    Mayhew, M.W.3    White, M.K.4    Terrian, D.M.5
  • 75
    • 1242320058 scopus 로고    scopus 로고
    • At the Crossroads of Myocardial Signaling: The Role of Z-Discs in Intracellular Signaling and Cardiac Function
    • DOI 10.1161/01.RES.0000116143.74830.A9
    • Pyle WG, Solaro RJ. 2004. At the cross-roads of myocardial signaling: the role of Z-discs in intracellular signaling and cardiac function. Circ Res 94:296-305. (Pubitemid 38240720)
    • (2004) Circulation Research , vol.94 , Issue.3 , pp. 296-305
    • Pyle, W.G.1    Solaro, R.J.2
  • 76
  • 77
    • 0035042676 scopus 로고    scopus 로고
    • Localization and kinetics of protein kinase C-epsilon anchoring in cardiac myocytes
    • Robia SL, Ghanta J, Robu VG, Walker JW. 2001. Localization and kinetics of protein kinase C-epsilon anchoring in cardiac myocytes. Biophys J 80:2140-2151. (Pubitemid 32401980)
    • (2001) Biophysical Journal , vol.80 , Issue.5 , pp. 2140-2151
    • Robia, S.L.1    Ghanta, J.2    Robu, V.G.3    Walker, J.W.4
  • 79
    • 0028158867 scopus 로고
    • Protein kinase C isoform expression and regulation in the developing rat heart
    • Rybin VO, Steinberg SF. 1994. Protein-Kinase-C isoform expression and regulation in the developing rat-heart. Circ Res 74:299-309. (Pubitemid 24029162)
    • (1994) Circulation Research , vol.74 , Issue.2 , pp. 299-309
    • Rybin, V.O.1    Steinberg, S.F.2
  • 80
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125(FAK), directs SH2 dependent binding of pp60(SRC)
    • Schaller MD, Hildebrand JD, Shannon JD, Fox JW, Vines RR, Parsons JT. 1994. Autophosphorylation of the focal adhesion kinase, pp125(FAK), directs SH2 dependent binding of pp60(SRC). Mol Cell Biol 14:1680-1688.
    • (1994) Mol Cell Biol , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5    Parsons, J.T.6
  • 84
    • 62849125813 scopus 로고    scopus 로고
    • The initial steps of myofibril assembly: Integrins pave the way
    • Sparrow JC, Schöck F. 2009. The initial steps of myofibril assembly: integrins pave the way. Nat Rev Mol Cell Biol 10:293-298.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 293-298
    • Sparrow, J.C.1    Schöck, F.2
  • 85
    • 55949109631 scopus 로고    scopus 로고
    • Structural basis of protein kinase C isoform function
    • Steinberg SF. 2008. Structural basis of protein kinase C isoform function. Physiol Rev 88:1341-1378.
    • (2008) Physiol Rev , vol.88 , pp. 1341-1378
    • Steinberg, S.F.1
  • 87
    • 33744829519 scopus 로고    scopus 로고
    • An interaction between integrin and the talin FERM domain mediates integrin activation but not linkage to the cytoskeleton
    • DOI 10.1038/ncb1411, PII N1411
    • Tanentzapf G, Brown NH. 2006. An interaction between integrin and the talin FERM domain mediates integrin activation but not linkage to the cytoskeleton. Nat Cell Biol 8:601-606. (Pubitemid 43827353)
    • (2006) Nature Cell Biology , vol.8 , Issue.6 , pp. 601-606
    • Tanentzapf, G.1    Brown, N.H.2
  • 88
    • 0242322488 scopus 로고    scopus 로고
    • Molecular Basis of Passive Stress Relaxation in Human Soleus Fibers: Assessment of the Role of Immunoglobulin-like Domain Unfolding
    • Trombitas K, Wu Y, McNabb M, Greaser M, Kellermayer MS, Labeit S, Granzier H. 2003. Molecular basis of passive stress relaxation in human soleus fibers: assessment of the role of immunoglobulin-like domain unfolding. Biophys J 85:3142-3153. (Pubitemid 37345801)
    • (2003) Biophysical Journal , vol.85 , Issue.5 , pp. 3142-3153
    • Trombitas, K.1    Wu, Y.2    McNabb, M.3    Greaser, M.4    Kellermayer, M.S.Z.5    Labeit, S.6    Granzier, H.L.7
  • 90
    • 0033918680 scopus 로고    scopus 로고
    • Beta(1)-integrin and PI 3-kinase regulate RhoA-dependent activation of skeletal alpha-actin promoter in myoblasts
    • Wei L, Zhou W, Wang L, Schwartz RJ. 2000. beta(1)-integrin and PI 3-kinase regulate RhoA-dependent activation of skeletal alpha-actin promoter in myoblasts. Am J Physiol Heart Circ Physiol 278:H1736-H1743.
    • (2000) Am J Physiol Heart Circ Physiol , vol.278
    • Wei, L.1    Zhou, W.2    Wang, L.3    Schwartz, R.J.4
  • 91
    • 0030827949 scopus 로고    scopus 로고
    • Actinin-associated LIM protein: Identification of a domain interaction between PDZ and spectrin-like repeat motifs
    • DOI 10.1083/jcb.139.2.507
    • Xia H, Winokur ST, Kuo WL, Altherr MR, Bredt DS. 1997. Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs. J Cell Biol 139:507-515. (Pubitemid 27459321)
    • (1997) Journal of Cell Biology , vol.139 , Issue.2 , pp. 507-515
    • Xia, H.1    Winokur, S.T.2    Kuo, W.-L.3    Altherr, M.R.4    Bredt, D.S.5
  • 93
    • 0032536770 scopus 로고    scopus 로고
    • Molecular structure of the sarcomeric Z-disk: Two types of titin interactions lead to an asymmetrical sorting of alpha-actinin
    • DOI 10.1093/emboj/17.6.1614
    • Young P, Ferguson C, Banuelos S, Gautel M. 1998. Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin. EMBO J 17:1614-1624. (Pubitemid 28119115)
    • (1998) EMBO Journal , vol.17 , Issue.6 , pp. 1614-1624
    • Young, P.1    Ferguson, C.2    Banuelos, S.3    Gautel, M.4
  • 94
    • 0035809918 scopus 로고    scopus 로고
    • Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane
    • DOI 10.1083/jcb.152.5.1007
    • Zervas CG, Gregory SL, Brown NH. 2001. Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane. J Cell Biol 152:1007-1018. (Pubitemid 34286076)
    • (2001) Journal of Cell Biology , vol.152 , Issue.5 , pp. 1007-1018
    • Zervas, C.G.1    Gregory, S.L.2    Brown, N.H.3
  • 95
    • 33645808902 scopus 로고    scopus 로고
    • Dynamic association between alpha-actinin and betaintegrin regulates contraction of canine tracheal smooth muscle
    • Zhang W, Gunst SJ. 2006. Dynamic association between alpha-actinin and betaintegrin regulates contraction of canine tracheal smooth muscle. J Physiol 572:659-676.
    • (2006) J Physiol , vol.572 , pp. 659-676
    • Zhang, W.1    Gunst, S.J.2
  • 96
    • 0037115611 scopus 로고    scopus 로고
    • Assembly fo the PINCH-IL-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
    • DOI 10.1242/jcs.00166
    • Zhang YJ, Chen K, Tu YZ, Velyvis A, Yang YW, Qin J, Wu CY. 2002. Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites. J Cell Sci 115:4777-4786. (Pubitemid 36054631)
    • (2002) Journal of Cell Science , vol.115 , Issue.24 , pp. 4777-4786
    • Zhang, Y.1    Chen, K.2    Tu, Y.3    Velyvis, A.4    Yang, Y.5    Qin, J.6    Wu, C.7
  • 97
    • 0033538565 scopus 로고    scopus 로고
    • Cypher, a Striated Muscle-restricted PDZ and LIM Domain-containing Protein, Binds to alpha-Actinin-2 and Protein Kinase C
    • Zhou Q, Ruiz-Lozano P, Martone ME, Chen J. 1999. Cypher, a striated muscle-restricted PDZ and LIM domain-containing protein, binds to alpha-actinin-2 and protein kinase C. J Biol Chem 274:19807-19813. (Pubitemid 129519430)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.28 , pp. 19807-19813
    • Zhou, Q.1    Ruiz-Lozano, P.2    Martone, M.E.3    Chen, J.4
  • 99
    • 57749116060 scopus 로고    scopus 로고
    • Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces
    • Zhu J, Luo BH, Xiao T, Zhang C, Nishida N, Springer TA. 2008. Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol Cell 32:849-861.
    • (2008) Mol Cell , vol.32 , pp. 849-861
    • Zhu, J.1    Luo, B.H.2    Xiao, T.3    Zhang, C.4    Nishida, N.5    Springer, T.A.6


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