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Volumn 8, Issue 6, 2012, Pages

Sarcomeric pattern formation by actin cluster coalescence

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; MUSCLE; ONE DIMENSIONAL;

EID: 84864048492     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1002544     Document Type: Article
Times cited : (26)

References (53)
  • 1
    • 34547149149 scopus 로고
    • Interpretation of muscle striation: Evidence from visible light microscopy
    • Huxley AF, (1956) Interpretation of muscle striation: Evidence from visible light microscopy. Brit Med Bull 12: 167-70.
    • (1956) Brit Med Bull , vol.12 , pp. 167-170
    • Huxley, A.F.1
  • 3
    • 3042723158 scopus 로고    scopus 로고
    • Simultaneous stretching and contraction of stress fibers in vivo
    • Peterson LJ, Rajfur Z, Maddox AS, Freel CD, Chen Y, et al. (2004) Simultaneous stretching and contraction of stress fibers in vivo. Mol Biol Cell 15: 3497-3508.
    • (2004) Mol Biol Cell , vol.15 , pp. 3497-3508
    • Peterson, L.J.1    Rajfur, Z.2    Maddox, A.S.3    Freel, C.D.4    Chen, Y.5
  • 4
    • 33646386142 scopus 로고    scopus 로고
    • Stress fibers are generated by two distinct actin assembly mechaisms in motile cells
    • Hotulainen P, Lappalainen P, (2006) Stress fibers are generated by two distinct actin assembly mechaisms in motile cells. J Cell Biol 173: 383-394.
    • (2006) J Cell Biol , vol.173 , pp. 383-394
    • Hotulainen, P.1    Lappalainen, P.2
  • 5
    • 0022980637 scopus 로고
    • Formation and alignment of Z lines in living chick myotubes microinjected with rhodamine-labeled alpha-actinin
    • McKenna NM, Johnson CS, Wang YL, (1986) Formation and alignment of Z lines in living chick myotubes microinjected with rhodamine-labeled alpha-actinin. J Cell Biol 103: 2163-71.
    • (1986) J Cell Biol , vol.103 , pp. 2163-2171
    • McKenna, N.M.1    Johnson, C.S.2    Wang, Y.L.3
  • 7
    • 33646043789 scopus 로고    scopus 로고
    • Focal adhesion kinase is essential for costamerogenesis in cultured skeletal muscle cells
    • Quach NL, Rando TA, (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
  • 10
    • 79954604476 scopus 로고    scopus 로고
    • Dynamic and structural signatures of lamellar actomyosin force generation
    • Aratyn-Schaus Y, Oakes PW, Gardel ML, (2011) Dynamic and structural signatures of lamellar actomyosin force generation. Mol Biol Cell 22: 1330-9.
    • (2011) Mol Biol Cell , vol.22 , pp. 1330-1339
    • Aratyn-Schaus, Y.1    Oakes, P.W.2    Gardel, M.L.3
  • 11
    • 35748954875 scopus 로고    scopus 로고
    • Polymer-induced bundling of F actin and the depletion force
    • Hosek M, Tang J, (2004) Polymer-induced bundling of F actin and the depletion force. Phys Rev E 69: 1-9.
    • (2004) Phys Rev E , vol.69 , pp. 1-9
    • Hosek, M.1    Tang, J.2
  • 13
    • 77952355776 scopus 로고    scopus 로고
    • A mechanical model of actin stress fiber formation and substrate elasticity sensing in adherent cells
    • Walcott S, Sun SX, (2010) A mechanical model of actin stress fiber formation and substrate elasticity sensing in adherent cells. Proc Natl Acad Sci U S A 107: 7757-62.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 7757-7762
    • Walcott, S.1    Sun, S.X.2
  • 16
    • 48849105558 scopus 로고    scopus 로고
    • Packing defects and the width of biopolymer bundles
    • Gov NS, (2008) Packing defects and the width of biopolymer bundles. Phys Rev E 78: 1-5.
    • (2008) Phys Rev E , vol.78 , pp. 1-5
    • Gov, N.S.1
  • 18
    • 33748058496 scopus 로고    scopus 로고
    • Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo
    • Witt CC, Burkart C, Labeit D, McNabb M, Wu Y, et al. (2006) Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo. EMBO J 25: 3843-55.
    • (2006) EMBO J , vol.25 , pp. 3843-3855
    • Witt, C.C.1    Burkart, C.2    Labeit, D.3    McNabb, M.4    Wu, Y.5
  • 19
    • 77953141955 scopus 로고    scopus 로고
    • Nebulin regulates actin filament lengths by a stabilization mechanism
    • Pappas CT, Krieg Pa, Gregorio CC, (2010) Nebulin regulates actin filament lengths by a stabilization mechanism. J Cell Biol 189: 859-70.
    • (2010) J Cell Biol , vol.189 , pp. 859-870
    • Pappas, C.T.1    Krieg, P.A.2    Gregorio, C.C.3
  • 21
    • 0346656820 scopus 로고    scopus 로고
    • N-RAP scaffolds I-Z-I assembly during myofibrillogenesis in cultured chick cardiomyocytes
    • Carroll S, Lu S, Herrera AH, Horowits R, (2004) N-RAP scaffolds I-Z-I assembly during myofibrillogenesis in cultured chick cardiomyocytes. J Cell Sci 117: 105-14.
    • (2004) J Cell Sci , vol.117 , pp. 105-114
    • Carroll, S.1    Lu, S.2    Herrera, A.H.3    Horowits, R.4
  • 22
    • 78650149624 scopus 로고    scopus 로고
    • Nebulin and N-WASP cooperate to cause IGF-1 induced sarcomeric actin filament formation
    • Takano K, Watanabe-Takano H, Suetsugu S, Kurita S, Tsujita K, et al. (2010) Nebulin and N-WASP cooperate to cause IGF-1 induced sarcomeric actin filament formation. Science 330: 1536-1540.
    • (2010) Science , vol.330 , pp. 1536-1540
    • Takano, K.1    Watanabe-Takano, H.2    Suetsugu, S.3    Kurita, S.4    Tsujita, K.5
  • 23
    • 77958521897 scopus 로고    scopus 로고
    • Dynamic regulation of sarcomeric actin filaments in striated muscle
    • Ono S, (2010) Dynamic regulation of sarcomeric actin filaments in striated muscle. Cytoskeleton 67: 677-92.
    • (2010) Cytoskeleton , vol.67 , pp. 677-692
    • Ono, S.1
  • 24
    • 0142136092 scopus 로고    scopus 로고
    • Formin Leaky Cap Allows Elongation in the Presence of Tight Capping Proteins
    • Zigmond SH, Evangelista M, Boone C, Yang C, Dar AC, et al. (2003) Formin Leaky Cap Allows Elongation in the Presence of Tight Capping Proteins. J Cell Biol 13: 1820-1823.
    • (2003) J Cell Biol , vol.13 , pp. 1820-1823
    • Zigmond, S.H.1    Evangelista, M.2    Boone, C.3    Yang, C.4    Dar, A.C.5
  • 25
    • 0033594081 scopus 로고    scopus 로고
    • Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes
    • Laurent V, Loisel TP, Harbeck B, Wehman A, Gröbe L, et al. (1999) Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes. J Cell Biol 144: 1245-58.
    • (1999) J Cell Biol , vol.144 , pp. 1245-1258
    • Laurent, V.1    Loisel, T.P.2    Harbeck, B.3    Wehman, A.4    Gröbe, L.5
  • 26
    • 0344759163 scopus 로고    scopus 로고
    • Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy
    • Salmikangas P, Mykkänen OM, Grönholm M, Heiska L, Kere J, et al. (1999) Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy. Hum Mol Genet 8: 1329-36.
    • (1999) Hum Mol Genet , vol.8 , pp. 1329-1336
    • Salmikangas, P.1    Mykkänen, O.M.2    Grönholm, M.3    Heiska, L.4    Kere, J.5
  • 27
    • 43249104243 scopus 로고    scopus 로고
    • Tracking changes in Z-band organization during myofibrillogenesis with FRET imaging
    • Stout AL, Wang J, Sanger JM, Sanger JW, (2008) Tracking changes in Z-band organization during myofibrillogenesis with FRET imaging. Cell Motil Cytoskeleton 65: 353-67.
    • (2008) Cell Motil Cytoskeleton , vol.65 , pp. 353-367
    • Stout, A.L.1    Wang, J.2    Sanger, J.M.3    Sanger, J.W.4
  • 28
    • 78649708350 scopus 로고    scopus 로고
    • Sarcomere Formation Occurs by the Assembly of Multiple Latent Protein Complexes
    • Rui Y, Bai J, Perrimon N, (2010) Sarcomere Formation Occurs by the Assembly of Multiple Latent Protein Complexes. PLoS Genetics 6: e1001208.
    • (2010) PLoS Genetics , vol.6
    • Rui, Y.1    Bai, J.2    Perrimon, N.3
  • 30
  • 31
    • 54049157485 scopus 로고    scopus 로고
    • Expansion and Polarity Sorting in Microtubule-Dynein Bundles
    • Zemel A, Mogilner A, (2008) Expansion and Polarity Sorting in Microtubule-Dynein Bundles. Prog Theoret Phys Suppl 173: 17.
    • (2008) Prog Theoret Phys , Issue.SUPPL. 173 , pp. 17
    • Zemel, A.1    Mogilner, A.2
  • 32
    • 68849091348 scopus 로고    scopus 로고
    • Motor-induced sliding of microtubule and actin bundles
    • Zemel A, Mogilner A, (2009) Motor-induced sliding of microtubule and actin bundles. Phys Chem Chem Phys 11: 4821-4833.
    • (2009) Phys Chem Chem Phys , vol.11 , pp. 4821-4833
    • Zemel, A.1    Mogilner, A.2
  • 33
    • 80052538625 scopus 로고    scopus 로고
    • The emergence of sarcomeric, graded-polarity and spindle-like patterns in bundles of short cytoskeletal polymers
    • Craig E, Dey S, Mogilner A, (2011) The emergence of sarcomeric, graded-polarity and spindle-like patterns in bundles of short cytoskeletal polymers. J Phys: Condens Matter 23: 374102 (10pp).
    • (2011) J Phys: Condens Matter , vol.23 , pp. 10
    • Craig, E.1    Dey, S.2    Mogilner, A.3
  • 34
    • 0027993176 scopus 로고
    • Porcine myosin-VI: characterization of a new mammalian unconventional myosin
    • Hasson T, Mooseker MS, (1994) Porcine myosin-VI: characterization of a new mammalian unconventional myosin. J Cell Biol 127: 425-40.
    • (1994) J Cell Biol , vol.127 , pp. 425-440
    • Hasson, T.1    Mooseker, M.S.2
  • 39
    • 0030864069 scopus 로고    scopus 로고
    • Identification of novel graded polarity actin filament bundles in locomoting heart fibroblasts: implications for the generation of motile force
    • Cramer LP, Siebert M, Mitchison TJ, (1997) Identification of novel graded polarity actin filament bundles in locomoting heart fibroblasts: implications for the generation of motile force. J Cell Biol 136: 1287-305.
    • (1997) J Cell Biol , vol.136 , pp. 1287-1305
    • Cramer, L.P.1    Siebert, M.2    Mitchison, T.J.3
  • 40
    • 0027194759 scopus 로고
    • Cellular motions and thermal uctuations: the Brownian ratchet
    • Peskin CS, Odell GM, Oster GF, (1993) Cellular motions and thermal uctuations: the Brownian ratchet. Biophys J 65: 316-24.
    • (1993) Biophys J , vol.65 , pp. 316-324
    • Peskin, C.S.1    Odell, G.M.2    Oster, G.F.3
  • 41
    • 1642322799 scopus 로고    scopus 로고
    • An actin molecular treadmill and myosins maintain stereocilia functional architecture and self-renewal
    • Rzadzinska AK, Schneider ME, Davies C, Riordan GP, Kachar B, (2004) An actin molecular treadmill and myosins maintain stereocilia functional architecture and self-renewal. J Cell Biol 164: 887-97.
    • (2004) J Cell Biol , vol.164 , pp. 887-897
    • Rzadzinska, A.K.1    Schneider, M.E.2    Davies, C.3    Riordan, G.P.4    Kachar, B.5
  • 42
    • 33847773123 scopus 로고    scopus 로고
    • Direct measurement of force generation by actin filament polymerization using an optical trap
    • Footer MJ, Kerssemakers JWJ, Theriot JA, Dogterom M, (2007) Direct measurement of force generation by actin filament polymerization using an optical trap. Proc Natl Acad Sci U S A 104: 2181-2186.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 2181-2186
    • Footer, M.J.1    Kerssemakers, J.W.J.2    Theriot, J.A.3    Dogterom, M.4
  • 44
    • 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. Nature Rev Mol Cell Biol 10: 293-8.
    • (2009) Nature Rev Mol Cell Biol , vol.10 , pp. 293-298
    • Sparrow, J.C.1    Schöck, F.2
  • 45
    • 0031006187 scopus 로고    scopus 로고
    • Independent Assembly of 1. 6 Angstrom Long Bipolar MHC Filaments and I-Z-I Bodies
    • Holtzer H, Hijikata T, Lin ZX, Holtzer S, Protasi F, et al. (1997) Independent Assembly of 1. 6 Angstrom Long Bipolar MHC Filaments and I-Z-I Bodies. Cell Struct Funct 93: 83-93.
    • (1997) Cell Struct Funct , vol.93 , pp. 83-93
    • Holtzer, H.1    Hijikata, T.2    Lin, Z.X.3    Holtzer, S.4    Protasi, F.5
  • 46
    • 78751645685 scopus 로고    scopus 로고
    • Filament turnover stabilizes contractile cytoskeletal structures
    • Guthardt Torres P, Doubrovinski K, Kruse K, (2010) Filament turnover stabilizes contractile cytoskeletal structures. Eur Phys Lett 91: 68003.
    • (2010) Eur Phys Lett , vol.91 , pp. 68003
    • Guthardt Torres, P.1    Doubrovinski, K.2    Kruse, K.3
  • 47
    • 31944448495 scopus 로고    scopus 로고
    • Inter-filament attractions narrow the length distribution of actin filaments
    • Biron D, Moses E, Borukhov I, Safran SA, (2006) Inter-filament attractions narrow the length distribution of actin filaments. Europhys Lett 73: 464-470.
    • (2006) Europhys Lett , vol.73 , pp. 464-470
    • Biron, D.1    Moses, E.2    Borukhov, I.3    Safran, S.A.4
  • 48
    • 44049093878 scopus 로고    scopus 로고
    • Stochastic severing of actin filaments by actin depolymerizing factor/cofilin controls the emergence of a steady dynamical regime
    • Roland J, Berro J, Michelot A, Blanchoin L, Martiel JL, (2008) Stochastic severing of actin filaments by actin depolymerizing factor/cofilin controls the emergence of a steady dynamical regime. Biophys J 94: 2082-94.
    • (2008) Biophys J , vol.94 , pp. 2082-2094
    • Roland, J.1    Berro, J.2    Michelot, A.3    Blanchoin, L.4    Martiel, J.L.5
  • 49
    • 79051469596 scopus 로고    scopus 로고
    • Theory of the length distribution of tread-milling actin filaments inside bundles
    • Gov NS, (2007) Theory of the length distribution of tread-milling actin filaments inside bundles. Eur Phys Lett 77: 68005.
    • (2007) Eur Phys Lett , vol.77 , pp. 68005
    • Gov, N.S.1
  • 50
    • 0035480846 scopus 로고    scopus 로고
    • A model for actin-filament length distribution in a lamellipod
    • Edelstein-Keshet L, Ermentrout GB, (2001) A model for actin-filament length distribution in a lamellipod. J Math Biol 355: 325-355.
    • (2001) J Math Biol , vol.355 , pp. 325-355
    • Edelstein-Keshet, L.1    Ermentrout, G.B.2
  • 51
    • 0033013812 scopus 로고    scopus 로고
    • Myofibrillogenesis in the developing chicken heart: assembly of Z-disk, M-line and the thick filaments
    • Ehler E, Rothen BM, Hämmerle SP, Komiyama M, Perriard JC, (1999) Myofibrillogenesis in the developing chicken heart: assembly of Z-disk, M-line and the thick filaments. J Cell Sci 112: 1529-39.
    • (1999) J Cell Sci , vol.112 , pp. 1529-1539
    • Ehler, E.1    Rothen, B.M.2    Hämmerle, S.P.3    Komiyama, M.4    Perriard, J.C.5
  • 52
    • 79960307611 scopus 로고    scopus 로고
    • Striated acto-myosin fibers can reorganize and register in response to elastic interactions with the matrix
    • Friedrich BM, Buxboim A, Discher DE, Safran SA, (2011) Striated acto-myosin fibers can reorganize and register in response to elastic interactions with the matrix. Biophys J 100: 2706-2715.
    • (2011) Biophys J , vol.100 , pp. 2706-2715
    • Friedrich, B.M.1    Buxboim, A.2    Discher, D.E.3    Safran, S.A.4
  • 53
    • 79960299436 scopus 로고    scopus 로고
    • Reconstitution of contractile actomyosin bundles
    • Thoresen T, Lenz M, Gardel ML, (2011) Reconstitution of contractile actomyosin bundles. Biophys J 100: 2698-705.
    • (2011) Biophys J , vol.100 , pp. 2698-2705
    • Thoresen, T.1    Lenz, M.2    Gardel, M.L.3


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