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Volumn 1, Issue 5, 2011, Pages 754-766

Non-muscle myosin II induces disassembly of actin stress fibres independently of myosin light chain dephosphorylation

Author keywords

Actin; Cell shortening; Mechanobiology; Non muscle myosin II; Stress fibres

Indexed keywords


EID: 81255178418     PISSN: 20428898     EISSN: 20428901     Source Type: Journal    
DOI: 10.1098/rsfs.2011.0031     Document Type: Article
Times cited : (33)

References (68)
  • 1
    • 36248969983 scopus 로고    scopus 로고
    • Actin stress fibres
    • (doi:10.1242/jcs.018473)
    • Pellegrin, S. & Mellor, H. 2007 Actin stress fibres. J. Cell Sci. 120, 3491-3499. (doi:10.1242/jcs.018473)
    • (2007) J. Cell Sci. , vol.120 , pp. 3491-3499
    • Pellegrin, S.1    Mellor, H.2
  • 3
    • 0030864069 scopus 로고    scopus 로고
    • Identification of novel graded polarity actin filament bundles in locomoting heart fibroblasts: Implications for the generation of motile force
    • (doi:10.1083/jcb.136.6.1287)
    • Cramer, L. P., Siebert, M. & Mitchison, T. J. 1997 Identification of novel graded polarity actin filament bundles in locomoting heart fibroblasts: implications for the generation of motile force. J. Cell Biol. 136, 1287-1305. (doi:10.1083/jcb.136.6.1287)
    • (1997) J. Cell Biol. , vol.136 , pp. 1287-1305
    • Cramer, L.P.1    Siebert, M.2    Mitchison, T.J.3
  • 4
    • 0033573912 scopus 로고    scopus 로고
    • Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch
    • (doi:10.1073/pnas.96.4.1351)
    • Krammer, A., Lu, H., Isralewitz, B., Schulten, K. & Vogel, V. 1999 Forced unfolding of the fibronectin type III module reveals a tensile molecular recognition switch. Proc. Natl Acad. Sci. USA 96, 1351-1356. (doi:10.1073/pnas.96.4.1351)
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1351-1356
    • Krammer, A.1    Lu, H.2    Isralewitz, B.3    Schulten, K.4    Vogel, V.5
  • 5
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • (doi:10.1083/jcb.141.2.539)
    • Zhong, C., Chrzanowska-Wodnicka, M., Brown, J., Shaub, A., Belkin, A. & Burridge, K. 1998 Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 141, 539-551. (doi:10.1083/jcb.141.2.539)
    • (1998) J. Cell Biol. , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.5    Burridge, K.6
  • 6
    • 0029995797 scopus 로고    scopus 로고
    • Rhostimulated contractility drives the formation of stress fibers and focal adhesions
    • (doi:10.1083/jcb.133.6.1403)
    • Chrzanowska-Wodnicka, M. & Burridge, K. 1996 Rhostimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133, 1403-1415. (doi:10.1083/jcb.133.6.1403)
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 7
    • 67650541328 scopus 로고    scopus 로고
    • Mechanosensing in actin stress fibers revealed by a close correlation between force and protein localization
    • (doi:10. 1242/jcs.042986)
    • Colombelli, J. et al. 2009 Mechanosensing in actin stress fibers revealed by a close correlation between force and protein localization. J. Cell Sci. 122, 1665-1679. (doi:10. 1242/jcs.042986)
    • (2009) J. Cell Sci. , vol.122 , pp. 1665-1679
    • Colombelli, J.1
  • 8
    • 30944452186 scopus 로고    scopus 로고
    • Focal adhesion size controls tensiondependent recruitment of alpha-smooth muscle actin to stress fibers
    • (doi:10.1083/jcb. 200506179)
    • Goffin, J. M., Pittet, P., Csucs, G., Lussi, J.W., Meister, J. J. & Hinz, B. 2006 Focal adhesion size controls tensiondependent recruitment of alpha-smooth muscle actin to stress fibers. J. Cell Biol. 172, 259-268. (doi:10.1083/jcb. 200506179)
    • (2006) J. Cell Biol. , vol.172 , pp. 259-268
    • Goffin, J.M.1    Pittet, P.2    Csucs, G.3    Lussi, J.W.4    Meister, J.J.5    Hinz, B.6
  • 9
    • 53349090308 scopus 로고    scopus 로고
    • Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner
    • (doi:10.1242/jcs.030320)
    • Hirata, H., Tatsumi, H. & Sokabe, M. 2008 Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner. J. Cell Sci. 121, 2795-2804. (doi:10.1242/jcs.030320)
    • (2008) J. Cell Sci. , vol.121 , pp. 2795-2804
    • Hirata, H.1    Tatsumi, H.2    Sokabe, M.3
  • 10
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCKindependent mechanism
    • (doi:10.1083/jcb.153.6.1175)
    • Riveline, D., Zamir, E., Balaban, N. Q., Schwarz, U. S., Ishizaki, T., Narumiya, S., Kam, Z., Geiger, B. & Bershadsky, A. D. 2001 Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCKindependent mechanism. J. Cell Biol. 153, 1175-1186. (doi:10.1083/jcb.153.6.1175)
    • (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
  • 11
    • 34548432555 scopus 로고    scopus 로고
    • Dynamics of cell orientation
    • (doi:10.1038/nphys680)
    • De, R., Zemel, A. & Safran, S. A. 2007 Dynamics of cell orientation. Nat. Phys. 3, 655-659. (doi:10.1038/nphys680)
    • (2007) Nat. Phys. , vol.3 , pp. 655-659
    • de, R.1    Zemel, A.2    Safran, S.A.3
  • 12
    • 0035425939 scopus 로고    scopus 로고
    • Dynamic reorientation of cultured cells and stress fibers under mechanical stress from periodic stretching
    • (doi:10.1006/excr.2001.5270)
    • Hayakawa, K., Sato, N. & Obinata, T. 2001 Dynamic reorientation of cultured cells and stress fibers under mechanical stress from periodic stretching. Exp. Cell Res. 268, 104-114. (doi:10.1006/excr.2001.5270)
    • (2001) Exp. Cell Res. , vol.268 , pp. 104-114
    • Hayakawa, K.1    Sato, N.2    Obinata, T.3
  • 13
    • 27644497978 scopus 로고    scopus 로고
    • Cooperative effects of Rho and mechanical stretch on stress fiber organization
    • (doi:10.1073/pnas.0506041102)
    • Kaunas, R., Nguyen, P., Usami, S. & Chien, S. 2005 Cooperative effects of Rho and mechanical stretch on stress fiber organization. Proc. Natl Acad. Sci. USA 102, 15 895-15 900. (doi:10.1073/pnas.0506041102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 15895-15900
    • Kaunas, R.1    Nguyen, P.2    Usami, S.3    Chien, S.4
  • 14
    • 60449089873 scopus 로고    scopus 로고
    • A kinematic model of stretchinduced stress fiber turnover and reorientation
    • (doi:10.1016/j.jtbi.2008.11.024)
    • Kaunas, R. & Hsu, H. J. 2009 A kinematic model of stretchinduced stress fiber turnover and reorientation. J. Theor. Biol. 257, 320-330. (doi:10.1016/j.jtbi.2008.11.024)
    • (2009) J. Theor. Biol. , vol.257 , pp. 320-330
    • Kaunas, R.1    Hsu, H.J.2
  • 15
    • 79952663509 scopus 로고    scopus 로고
    • Sarcomeric model of stretch-induced stress fiber reorganization
    • (doi:10.2147/CHC.S14984)
    • Kaunas, R., Hsu, H. J. & Deguchi, S. 2011 Sarcomeric model of stretch-induced stress fiber reorganization. Cell Health Cytoskeleton 3, 13-22. (doi:10.2147/CHC.S14984)
    • (2011) Cell Health Cytoskeleton , vol.3 , pp. 13-22
    • Kaunas, R.1    Hsu, H.J.2    Deguchi, S.3
  • 16
    • 77958153094 scopus 로고    scopus 로고
    • Cyclic stretch-induced stress fiber dynamics: Dependence on strain rate, Rho-kinase and MLCK
    • (doi:10.1016/j.bbrc.2010.09.046)
    • Lee, C. F., Haase, C., Deguchi, S. & Kaunas, R. 2010 Cyclic stretch-induced stress fiber dynamics: dependence on strain rate, Rho-kinase and MLCK. Biochem. Biophys. Res. Commun. 401, 344-349. (doi:10.1016/j.bbrc.2010.09.046)
    • (2010) Biochem. Biophys. Res. Commun. , vol.401 , pp. 344-349
    • Lee, C.F.1    Haase, C.2    Deguchi, S.3    Kaunas, R.4
  • 17
    • 33746676272 scopus 로고    scopus 로고
    • Involvement of SA channels in orienting response of cultured endothelial cells to cyclic stretch
    • Naruse, K., Yamada, T. & Sokabe, M. 1998 Involvement of SA channels in orienting response of cultured endothelial cells to cyclic stretch. Am. J. Physiol. 274, H1532-H1538.
    • (1998) Am. J. Physiol. , vol.274
    • Naruse, K.1    Yamada, T.2    Sokabe, M.3
  • 18
    • 0032911020 scopus 로고    scopus 로고
    • Bidirectional signaling between the cytoskeleton and integrins
    • (doi:10.1016/S0955-0674(99)80037-4)
    • Schoenwaelder, S. M. & Burridge, K. 1999 Bidirectional signaling between the cytoskeleton and integrins. Curr. Opin. Cell Biol. 11, 274-286. (doi:10.1016/S0955-0674(99)80037-4)
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 274-286
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 19
    • 22144472976 scopus 로고    scopus 로고
    • Quantitative evaluation of threshold fiber strain that induces reorganization of cytoskeletal actin fiber structure in osteoblastic cells
    • (doi:10. 1016/j.jbiomech.2004.08.012)
    • Sato, K., Adachi, T., Matsuo, M. & Tomita, Y. 2005 Quantitative evaluation of threshold fiber strain that induces reorganization of cytoskeletal actin fiber structure in osteoblastic cells. J. Biomech. 38, 1895-1901. (doi:10. 1016/j.jbiomech.2004.08.012)
    • (2005) J. Biomech. , vol.38 , pp. 1895-1901
    • Sato, K.1    Adachi, T.2    Matsuo, M.3    Tomita, Y.4
  • 20
    • 33744472484 scopus 로고    scopus 로고
    • Intracellular stress transmission through actin stress fiber network in adherent vascular cells
    • Deguchi, S., Ohashi, T. & Sato, M. 2005 Intracellular stress transmission through actin stress fiber network in adherent vascular cells. Mol. Cell Biomech. 2, 205-216.
    • (2005) Mol. Cell Biomech. , vol.2 , pp. 205-216
    • Deguchi, S.1    Ohashi, T.2    Sato, M.3
  • 21
    • 35048857084 scopus 로고    scopus 로고
    • Local disassembly of actin stress fibers induced by selected release of intracellular tension in osteoblastic cell
    • (doi:10.1299/jbse.1.204)
    • Sato, K., Adachi, T., Shirai, Y., Saito, N. & Tomita, Y. 2006 Local disassembly of actin stress fibers induced by selected release of intracellular tension in osteoblastic cell. J. Biomech. Sci. Eng. 1, 204-214. (doi:10.1299/jbse.1.204)
    • (2006) J. Biomech. Sci. Eng. , vol.1 , pp. 204-214
    • Sato, K.1    Adachi, T.2    Shirai, Y.3    Saito, N.4    Tomita, Y.5
  • 22
    • 77957084444 scopus 로고    scopus 로고
    • Cellular ATP
    • Cell chemistry and physiology, In, part 2 (eds E. E. Bittar & N. Bittar), ch. 1, New York, NY: Elsevier Science
    • Harris, D. A. 1996 Cellular ATP. In Principles of medical biology, vol. 4 part 2 (eds E. E. Bittar & N. Bittar), ch. 1, pp. 1-47, Cell chemistry and physiology. New York, NY: Elsevier Science.
    • (1996) Principles of medical biology , vol.4 , pp. 1-47
    • Harris, D.A.1
  • 23
    • 77951880862 scopus 로고    scopus 로고
    • Actin stress fibers are at a tipping point between conventional shortening and rapid disassembly at physiological levels of MgATP
    • (doi:10.1016/j.bbrc.2010.03.150)
    • Matsui, T. S., Ito, K., Kaunas, R., Sato, M. & Deguchi, S. 2010 Actin stress fibers are at a tipping point between conventional shortening and rapid disassembly at physiological levels of MgATP. Biochem. Biophys. Res. Commun. 395, 301-306. (doi:10.1016/j.bbrc.2010.03.150)
    • (2010) Biochem. Biophys. Res. Commun. , vol.395 , pp. 301-306
    • Matsui, T.S.1    Ito, K.2    Kaunas, R.3    Sato, M.4    Deguchi, S.5
  • 24
    • 33749077090 scopus 로고    scopus 로고
    • Tensile properties of single stress fibers isolated from cultured vascular smooth muscle cells
    • (doi:10.1016/j.jbiomech.2005.08.026)
    • Deguchi, S., Ohashi, T. & Sato, M. 2006 Tensile properties of single stress fibers isolated from cultured vascular smooth muscle cells. J. Biomech. 39, 2603-2610. (doi:10.1016/j.jbiomech.2005.08.026)
    • (2006) J. Biomech. , vol.39 , pp. 2603-2610
    • Deguchi, S.1    Ohashi, T.2    Sato, M.3
  • 26
    • 0023919181 scopus 로고
    • Force measurements by micromanipulation of a single actin filament by glass needles
    • (doi:10.1038/334074a0)
    • Kishino, A. & Yanagida, T. 1988 Force measurements by micromanipulation of a single actin filament by glass needles. Nature 334, 74-76. (doi:10.1038/334074a0)
    • (1988) Nature , vol.334 , pp. 74-76
    • Kishino, A.1    Yanagida, T.2
  • 27
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato, A. & Fabiato, F. 1979 Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J. Physiol. Paris 75, 463-505.
    • (1979) J. Physiol. Paris , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 28
    • 4744345012 scopus 로고    scopus 로고
    • Dynamic change in the distribution of integrin on isolated ventral membrane: Effect of divalent cation species
    • (doi:10.1002/cm.20029)
    • Hirata, H., Ohki, K. & Miyata, H. 2004 Dynamic change in the distribution of integrin on isolated ventral membrane: effect of divalent cation species. Cell Motil. Cytoskeleton 59, 131-140. (doi:10.1002/cm.20029)
    • (2004) Cell Motil. Cytoskeleton , vol.59 , pp. 131-140
    • Hirata, H.1    Ohki, K.2    Miyata, H.3
  • 29
    • 19744371284 scopus 로고    scopus 로고
    • Mobility of integrin a5b1 measured on the isolated ventral membranes of human skin fibroblasts
    • Hirata, H., Ohki, K. & Miyata, H. 2005 Mobility of integrin a5b1 measured on the isolated ventral membranes of human skin fibroblasts. Biochim. Biophys. Acta 1723, 100-105.
    • (2005) Biochim. Biophys. Acta , vol.1723 , pp. 100-105
    • Hirata, H.1    Ohki, K.2    Miyata, H.3
  • 30
    • 72949084650 scopus 로고    scopus 로고
    • A versatile micro-mechanical tester for actin stress fibers isolated from cells
    • (doi:10.3233/BIR-2009-0551)
    • Matsui, T. S., Deguchi, S., Sakamoto, N., Ohashi, T. & Sato, M. 2009 A versatile micro-mechanical tester for actin stress fibers isolated from cells. Biorheology 46, 401-415. (doi:10.3233/BIR-2009-0551)
    • (2009) Biorheology , vol.46 , pp. 401-415
    • Matsui, T.S.1    Deguchi, S.2    Sakamoto, N.3    Ohashi, T.4    Sato, M.5
  • 31
    • 37349002468 scopus 로고    scopus 로고
    • Nonlinear force-length relationship in the ADPinduced contraction of skeletal myofibrils
    • (doi:10.1529/biophysj.107.110650)
    • Shimamoto, Y., Kono, F., Suzuki, M. & Ishiwata, S. 2007 Nonlinear force-length relationship in the ADPinduced contraction of skeletal myofibrils. Biophys. J. 93, 4330-4341. (doi:10.1529/biophysj.107.110650)
    • (2007) Biophys. J. , vol.93 , pp. 4330-4341
    • Shimamoto, Y.1    Kono, F.2    Suzuki, M.3    Ishiwata, S.4
  • 32
    • 33646205849 scopus 로고    scopus 로고
    • Half-sarcomere dynamics in myofibrils during activation and relaxation studied by tracking fluorescent markers
    • (doi:10.1529/biophysj.105.070334)
    • Telley, I. A., Denoth, J., Stüssi, E., Pfitzer, G. & Stehle, R. 2006 Half-sarcomere dynamics in myofibrils during activation and relaxation studied by tracking fluorescent markers. Biophys. J. 90, 514-530. (doi:10.1529/biophysj.105.070334)
    • (2006) Biophys. J. , vol.90 , pp. 514-530
    • Telley, I.A.1    Denoth, J.2    Stüssi, E.3    Pfitzer, G.4    Stehle, R.5
  • 33
    • 0035972212 scopus 로고    scopus 로고
    • Rho-kinase-mediated contraction of isolated stress fibers
    • (doi:10.1083/jcb.153.3.569)
    • Katoh, K., Kano, Y., Amano, M., Onishi, H., Kaibuchi, K. & Fujiwara, K. 2001 Rho-kinase-mediated contraction of isolated stress fibers. J. Cell Biol. 153, 569-584. (doi:10.1083/jcb.153.3.569)
    • (2001) J. Cell Biol. , vol.153 , pp. 569-584
    • Katoh, K.1    Kano, Y.2    Amano, M.3    Onishi, H.4    Kaibuchi, K.5    Fujiwara, K.6
  • 34
    • 0025104145 scopus 로고
    • Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay
    • (doi:10.1016/S0022-2836(05)80060-9)
    • Harada, Y., Sakurada, K., Aoki, T., Thomas, D. D. & Yanagida, T. 1990 Mechanochemical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol. Biol. 216, 49-68. (doi:10.1016/S0022-2836(05)80060-9)
    • (1990) J. Mol. Biol. , vol.216 , pp. 49-68
    • Harada, Y.1    Sakurada, K.2    Aoki, T.3    Thomas, D.D.4    Yanagida, T.5
  • 35
    • 0021261156 scopus 로고
    • Direct observation of motion of single F-actin filaments in the presence of myosin
    • (doi:10.1038/307058a0)
    • Yanagida, T., Nakase, M., Nishiyama, K. & Oosawa, F. 1984 Direct observation of motion of single F-actin filaments in the presence of myosin. Nature 307, 58-60. (doi:10.1038/307058a0)
    • (1984) Nature , vol.307 , pp. 58-60
    • Yanagida, T.1    Nakase, M.2    Nishiyama, K.3    Oosawa, F.4
  • 36
    • 0021749672 scopus 로고
    • The relationship between stress fiber-like structures and nascent myofibrils in cultured cardiac myocytes
    • (doi:10.1083/jcb.99.6.2268)
    • Dlugosz, A. A., Antin, P. B., Nachmias, V. T. & Holtzer, H. 1984 The relationship between stress fiber-like structures and nascent myofibrils in cultured cardiac myocytes. J. Cell Biol. 99, 2268-2278. (doi:10.1083/jcb.99.6.2268)
    • (1984) J. Cell Biol. , vol.99 , pp. 2268-2278
    • Dlugosz, A.A.1    Antin, P.B.2    Nachmias, V.T.3    Holtzer, H.4
  • 37
    • 0027524780 scopus 로고
    • Non-sarcomeric mode of myosin II organization in the fibroblast lamellum
    • (doi:10.1083/jcb.123.3.637)
    • Verkhovsky, A. B. & Borisy, G. G. 1993 Non-sarcomeric mode of myosin II organization in the fibroblast lamellum. J. Cell Biol. 123, 637-652. (doi:10.1083/jcb.123.3.637)
    • (1993) J. Cell Biol. , vol.123 , pp. 637-652
    • Verkhovsky, A.B.1    Borisy, G.G.2
  • 38
    • 0028818253 scopus 로고
    • Myosin II filament assemblies in the active lamella of fibroblasts: Their morphogenesis and role in the formation of actin filament bundles
    • (doi:10.1083/jcb.131.4.989)
    • Verkhovsky, A. B., Svitkina, T. M. & Borisy, G. G. 1995 Myosin II filament assemblies in the active lamella of fibroblasts: their morphogenesis and role in the formation of actin filament bundles. J. Cell Biol. 131, 989-1002. (doi:10.1083/jcb.131.4.989)
    • (1995) J. Cell Biol. , vol.131 , pp. 989-1002
    • Verkhovsky, A.B.1    Svitkina, T.M.2    Borisy, G.G.3
  • 39
    • 0026045382 scopus 로고
    • Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament number without altering the filament length distribution
    • (doi:10.1083/jcb.115.3.677)
    • Cano, M. L., Lauffenburger, D. A. & Zigmond, S. H. 1991 Kinetic analysis of F-actin depolymerization in polymorphonuclear leukocyte lysates indicates that chemoattractant stimulation increases actin filament number without altering the filament length distribution. J. Cell Biol. 115, 3677-3687. (doi:10.1083/jcb.115.3.677)
    • (1991) J. Cell Biol. , vol.115 , pp. 3677-3687
    • Cano, M.L.1    Lauffenburger, D.A.2    Zigmond, S.H.3
  • 40
    • 0035965138 scopus 로고    scopus 로고
    • Kinetic mechanism of end-to-end annealing of actin filaments
    • (doi:10.1006/jmbi.2001.5005)
    • Andrianantoandro, E., Blanchoin, L., Sept, D., McCammon, J. A. & Pollard, T. D. 2001 Kinetic mechanism of end-to-end annealing of actin filaments. J. Mol. Biol. 312, 721-730. (doi:10.1006/jmbi.2001.5005)
    • (2001) J. Mol. Biol. , vol.312 , pp. 721-730
    • Andrianantoandro, E.1    Blanchoin, L.2    Sept, D.3    McCammon, J.A.4    Pollard, T.D.5
  • 41
    • 33846815057 scopus 로고    scopus 로고
    • Regulation of myosin II dynamics by phosphorylation and dephosphorylation of its light chain in epithelial cells
    • (doi:10.1091/mbc.E06-07-0590)
    • Watanabe, T., Hosoya, H. & Yonemura, S. 2007 Regulation of myosin II dynamics by phosphorylation and dephosphorylation of its light chain in epithelial cells. Mol. Biol. Cell. 18, 605-616. (doi:10.1091/mbc.E06-07-0590)
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 605-616
    • Watanabe, T.1    Hosoya, H.2    Yonemura, S.3
  • 42
    • 0028277783 scopus 로고
    • Stress relaxation of fibroblasts activates a cyclic AMP signaling pathway
    • (doi:10.1083/jcb.126.2.457)
    • He, Y. & Grinnell, F. 1994 Stress relaxation of fibroblasts activates a cyclic AMP signaling pathway. J. Cell Biol. 126, 457-464. (doi:10.1083/jcb.126.2.457)
    • (1994) J. Cell Biol. , vol.126 , pp. 457-464
    • He, Y.1    Grinnell, F.2
  • 43
    • 0141533044 scopus 로고    scopus 로고
    • Integrin signaling to the actin cytoskeleton
    • (doi:10.1016/S0955-0674(03) 00109-1)
    • DeMali, K. A., Wennerberg, K. & Burridge, K. 2003 Integrin signaling to the actin cytoskeleton. Curr. Opin. Cell. Biol. 15, 572-582. (doi:10.1016/S0955-0674(03) 00109-1)
    • (2003) Curr. Opin. Cell. Biol. , vol.15 , pp. 572-582
    • DeMali, K.A.1    Wennerberg, K.2    Burridge, K.3
  • 44
    • 52049092063 scopus 로고    scopus 로고
    • Motor proteins: Myosin mechanosensors
    • (doi:10. 1016/j.cub.2008.07.071)
    • Kee, Y. S. & Robinson, D. N. 2008 Motor proteins: myosin mechanosensors. Curr. Biol. 18, R860-R862. (doi:10. 1016/j.cub.2008.07.071)
    • (2008) Curr. Biol. , vol.18
    • Kee, Y.S.1    Robinson, D.N.2
  • 45
    • 34547158278 scopus 로고    scopus 로고
    • Load-dependent mechanism of nonmuscle myosin 2
    • (doi:10. 1073/pnas.0701181104)
    • Kovacs, M., Thirumurugan, K., Knight, P. J. & Sellers, J. R. 2007 Load-dependent mechanism of nonmuscle myosin 2. Proc. Natl Acad. Sci. USA 104, 9994-9999. (doi:10. 1073/pnas.0701181104)
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 9994-9999
    • Kovacs, M.1    Thirumurugan, K.2    Knight, P.J.3    Sellers, J.R.4
  • 46
    • 77954237525 scopus 로고    scopus 로고
    • Unconventional processive mechanics of non-muscle myosin IIB
    • (doi:10. 1074/jbc.M110.123851)
    • Norstrom, M. F., Smithback, P. A. & Rock, R. S. 2010 Unconventional processive mechanics of non-muscle myosin IIB. J. Biol. Chem. 285, 26326-26334. (doi:10. 1074/jbc.M110.123851)
    • (2010) J. Biol. Chem. , vol.285 , pp. 26326-26334
    • Norstrom, M.F.1    Smithback, P.A.2    Rock, R.S.3
  • 47
    • 13444263735 scopus 로고    scopus 로고
    • Adenosine diphosphate and strain sensitivity in myosin motors
    • (doi:10.1098/rstb.2004.1560)
    • Nyitrai, M. & Geeves, M. A. 2004 Adenosine diphosphate and strain sensitivity in myosin motors. Phil. Trans. R. Soc. Lond. B 359, 1867-1877. (doi:10.1098/rstb.2004.1560)
    • (2004) Phil. Trans. R. Soc. Lond. B , vol.359 , pp. 1867-1877
    • Nyitrai, M.1    Geeves, M.A.2
  • 48
    • 1642448472 scopus 로고    scopus 로고
    • Functional divergence of human cytoplasmic myosin II: Kinetic characterization of the non-muscle IIA isoform
    • (doi:10. 1074/jbc.M305453200)
    • Kovacs, M., Wang, F., Hu, A., Zhang, Y. & Sellers, J. R. 2003 Functional divergence of human cytoplasmic myosin II: kinetic characterization of the non-muscle IIA isoform. J. Biol. Chem. 278, 38 132-38 140. (doi:10. 1074/jbc.M305453200)
    • (2003) J. Biol. Chem. , vol.278 , pp. 38132-38140
    • Kovacs, M.1    Wang, F.2    Hu, A.3    Zhang, Y.4    Sellers, J.R.5
  • 49
    • 0042347443 scopus 로고    scopus 로고
    • Kinetic mechanism of non-muscle myosin IIB: Functional adaptations for tension generation and maintenance
    • (doi:10.1074/jbc.M302510200)
    • Wang, F., Kovacs, M., Hu, A., Limouze, J., Harvey, E. V. & Sellers, J. R. 2003 Kinetic mechanism of non-muscle myosin IIB: functional adaptations for tension generation and maintenance. J. Biol. Chem. 278, 27 439-27 448. (doi:10.1074/jbc.M302510200)
    • (2003) J. Biol. Chem. , vol.278 , pp. 27439-27448
    • Wang, F.1    Kovacs, M.2    Hu, A.3    Limouze, J.4    Harvey, E.V.5    Sellers, J.R.6
  • 50
    • 0035997133 scopus 로고    scopus 로고
    • Buckling of actin stress fibers: A new wrinkle in the cytoskeletal tapestry
    • (doi:10.1002/cm. 10056)
    • Costa, K., Hucker, W. J. & Yin, F. 2002 Buckling of actin stress fibers: a new wrinkle in the cytoskeletal tapestry. Cell Motil. Cytoskeleton 52, 266-274. (doi:10.1002/cm. 10056)
    • (2002) Cell Motil. Cytoskeleton , vol.52 , pp. 266-274
    • Costa, K.1    Hucker, W.J.2    Yin, F.3
  • 51
    • 33646179573 scopus 로고    scopus 로고
    • Viscoelastic retraction of single living stress fibers and its impact on cell shape, cytoskeletal organization, and extracellular matrix mechanics
    • (doi:10.1529/biophysj.105.071506)
    • Kumar, S., Maxwell, I. Z., Heisterkamp, A., Polte, T. R., Lele, T. P., Salanga, M., Mazur, E. & Ingber, D. E. 2006 Viscoelastic retraction of single living stress fibers and its impact on cell shape, cytoskeletal organization, and extracellular matrix mechanics. Biophys. J. 90, 3762-3773. (doi:10.1529/biophysj.105.071506)
    • (2006) Biophys. J. , vol.90 , pp. 3762-3773
    • Kumar, S.1    Maxwell, I.Z.2    Heisterkamp, A.3    Polte, T.R.4    Lele, T.P.5    Salanga, M.6    Mazur, E.7    Ingber, D.E.8
  • 52
    • 33646386142 scopus 로고    scopus 로고
    • Stress fibers are generated by two distinct actin assembly mechanisms in motile cells
    • (doi:10.1083/jcb. 200511093)
    • Hotulainen, P. & Lappalainen, P. 2006 Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J. Cell Biol. 173, 383-394. (doi:10.1083/jcb. 200511093)
    • (2006) J. Cell Biol. , vol.173 , pp. 383-394
    • Hotulainen, P.1    Lappalainen, P.2
  • 54
    • 70350454867 scopus 로고    scopus 로고
    • Non-muscle myosin II takes centre stage in cell adhesion and migration
    • (doi:10.1038/nrm2786)
    • Vicente-Manzanares, M., Ma, X., Adelstein, R. S. & Horwitz, A. R. 2009 Non-muscle myosin II takes centre stage in cell adhesion and migration. Nat. Rev. Mol. Cell Biol. 10, 778-790. (doi:10.1038/nrm2786)
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 778-790
    • Vicente-Manzanares, M.1    Ma, X.2    Adelstein, R.S.3    Horwitz, A.R.4
  • 55
    • 0030773824 scopus 로고    scopus 로고
    • Molecular motors: Structural adaptations to cellular functions
    • (doi:10.1038/39247)
    • Howard, J. 1997 Molecular motors: structural adaptations to cellular functions. Nature 389, 561-567. (doi:10.1038/39247)
    • (1997) Nature , vol.389 , pp. 561-567
    • Howard, J.1
  • 56
    • 0142148230 scopus 로고    scopus 로고
    • Polarized actin bundles formed by human fascin-1: Their sliding and disassembly on myosin II and myosin V in vitro
    • (doi:10.1046/j.1471-4159.2003.02058.x)
    • Ishikawa, R., Sakamoto, T., Ando, T., Fujime, S. & Kohama, K. 2003 Polarized actin bundles formed by human fascin-1: their sliding and disassembly on myosin II and myosin V in vitro. J. Neurochem. 87, 676-685. (doi:10.1046/j.1471-4159.2003.02058.x)
    • (2003) J. Neurochem. , vol.87 , pp. 676-685
    • Ishikawa, R.1    Sakamoto, T.2    Ando, T.3    Fujime, S.4    Kohama, K.5
  • 57
    • 33644775671 scopus 로고    scopus 로고
    • Myosin II functions in actin-bundle turnover in neuronal growth cones
    • (doi:10.1038/ncb1367)
    • Medeiros, N. A., Burnette, D. T. & Forscher, P. 2006 Myosin II functions in actin-bundle turnover in neuronal growth cones. Nat. Cell Biol. 8, 216-226. (doi:10.1038/ncb1367)
    • (2006) Nat. Cell Biol. , vol.8 , pp. 216-226
    • Medeiros, N.A.1    Burnette, D.T.2    Forscher, P.3
  • 58
    • 36549035377 scopus 로고    scopus 로고
    • A cytoskeletal demolition worker: Myosin II acts as an actin depolymerization agent
    • (doi:10.1016/j.jmb.2007.09.066)
    • Haviv, L., Gillo, D., Backouche, F. & Bernheim-Groswasser, A. 2008 A cytoskeletal demolition worker: myosin II acts as an actin depolymerization agent. J. Mol. Biol. 375, 325-330. (doi:10.1016/j.jmb.2007.09.066)
    • (2008) J. Mol. Biol. , vol.375 , pp. 325-330
    • Haviv, L.1    Gillo, D.2    Backouche, F.3    Bernheim-Groswasser, A.4
  • 59
    • 77952687450 scopus 로고    scopus 로고
    • Myosin II contributes to cell-scale actin network treadmilling through network disassembly
    • (doi:10.1038/nature08994)
    • Wilson, C. A. et al. 2010 Myosin II contributes to cell-scale actin network treadmilling through network disassembly. Nature 465, 373-377. (doi:10.1038/nature08994)
    • (2010) Nature , vol.465 , pp. 373-377
    • Wilson, C.A.1
  • 60
    • 41549108457 scopus 로고    scopus 로고
    • Building the actin cytoskeleton: Filopodia contribute to the construction of contractile bundles in the lamella
    • (doi:10.1083/jcb.200709134)
    • Nemethova, M., Auinger, S. & Small, J. V. 2008 Building the actin cytoskeleton: filopodia contribute to the construction of contractile bundles in the lamella. J. Cell Biol. 180, 1233-1244. (doi:10.1083/jcb.200709134)
    • (2008) J. Cell Biol. , vol.180 , pp. 1233-1244
    • Nemethova, M.1    Auinger, S.2    Small, J.V.3
  • 61
    • 0034698841 scopus 로고    scopus 로고
    • Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts
    • (doi:10.1083/jcb.150.4.797)
    • Totsukawa, G., Yamakita, Y., Yamashiro, S., Hartshorne, D. J., Sasaki, Y. & Matsumura, F. 2000 Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J. Cell Biol. 150, 797-806. (doi:10.1083/jcb.150.4.797)
    • (2000) J. Cell Biol. , vol.150 , pp. 797-806
    • Totsukawa, G.1    Yamakita, Y.2    Yamashiro, S.3    Hartshorne, D.J.4    Sasaki, Y.5    Matsumura, F.6
  • 62
    • 0019843141 scopus 로고
    • Non-muscle aactinins are calcium-sensitive actin-binding proteins
    • (doi:10.1038/294565a0)
    • Burridge, K. & Feramisco, J. R. 1981 Non-muscle aactinins are calcium-sensitive actin-binding proteins. Nature 294, 565-567. (doi:10.1038/294565a0)
    • (1981) Nature , vol.294 , pp. 565-567
    • Burridge, K.1    Feramisco, J.R.2
  • 63
    • 3042540132 scopus 로고
    • Actin-binding proteins
    • (doi:10.1016/0968-0004(82)90153-0)
    • Craig, S. W. & Pollard, T. D. 1982 Actin-binding proteins. Trends Biochem. Sci. 7, 88-92. (doi:10.1016/0968-0004(82)90153-0)
    • (1982) Trends Biochem. Sci. , vol.7 , pp. 88-92
    • Craig, S.W.1    Pollard, T.D.2
  • 64
    • 0030802568 scopus 로고    scopus 로고
    • The structure, function, and assembly of actin filament bundle
    • (doi:10.1016/S0074-7696(08) 62125-7)
    • Furukawa, R. & Fechheimer, M. 1997 The structure, function, and assembly of actin filament bundle. Int. Rev. Cytol. 175, 29-90. (doi:10.1016/S0074-7696(08) 62125-7)
    • (1997) Int. Rev. Cytol. , vol.175 , pp. 29-90
    • Furukawa, R.1    Fechheimer, M.2
  • 65
    • 0023760164 scopus 로고
    • Cytoplasmic calcium response to fluid shear stress in cultured vascular endothelial cells
    • (doi:10.1007/BF02623896)
    • Ando, J., Komatsuda, T. & Kamiya, A. 1988 Cytoplasmic calcium response to fluid shear stress in cultured vascular endothelial cells. In vitro Cell Dev. Biol. 24, 871-877. (doi:10.1007/BF02623896)
    • (1988) In vitro Cell Dev. Biol. , vol.24 , pp. 871-877
    • Ando, J.1    Komatsuda, T.2    Kamiya, A.3
  • 66
    • 0026695285 scopus 로고
    • Flow-induced calcium transients in single endothelial cells: Spatial and temporal analysis
    • Geiger, R.V., Berk, B. C., Alexander, R.W. &Nerem, R. M. 1992 Flow-induced calcium transients in single endothelial cells: spatial and temporal analysis. Am. J. Physiol. 262, C1411-C1417.
    • (1992) Am. J. Physiol. , vol.262
    • Geiger, R.V.1    Berk, B.C.2    Alexander, R.W.3    Nerem, R.M.4
  • 68
    • 0027516325 scopus 로고
    • Morphological and biochemical analyses of contractile proteins (actin, myosin, caldesmon and tropomyosin) in normal and transformed cells
    • Tanaka, J., Watanabe, T., Nakamura, N. & Sobue, K. 1993 Morphological and biochemical analyses of contractile proteins (actin, myosin, caldesmon and tropomyosin) in normal and transformed cells. J. Cell Sci. 104, 595-606.
    • (1993) J. Cell Sci. , vol.104 , pp. 595-606
    • Tanaka, J.1    Watanabe, T.2    Nakamura, N.3    Sobue, K.4


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