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Volumn 5, Issue 6, 2012, Pages 572-577

Mechano-sensing by actin filaments and focal adhesion proteins

Author keywords

Actins; ADF cofilin; Focal adhesions; Mechanosensing; Stress fibers; Tension

Indexed keywords


EID: 84869828156     PISSN: 19420889     EISSN: 19420889     Source Type: Journal    
DOI: 10.4161/cib.21891     Document Type: Article
Times cited : (35)

References (56)
  • 1
    • 0027460103 scopus 로고
    • Involvement of stretch-activated ion channels in Ca2+ mobilization to mechanical stretch in endothelial cells
    • Naruse K, Sokabe M. Involvement of stretch-activated ion channels in Ca2+ mobilization to mechanical stretch in endothelial cells. Am J Physiol 1993; 264:C1037-44.
    • (1993) Am J Physiol , vol.264
    • Naruse, K.1    Sokabe, M.2
  • 2
    • 0023760164 scopus 로고
    • Cytoplasmic calcium response to fluid shear stress in cultured vascular endothelial cells
    • Ando J, Komatsuda T, Kamiya A. Cytoplasmic calcium response to fluid shear stress in cultured vascular endothelial cells. In Vitro Cell Dev Biol 1988; 24:871-7; http://dx.doi.org/10.1007/ BF02623896.
    • (1988) In Vitro Cell Dev Biol , vol.24 , pp. 871-877
    • Ando, J.1    Komatsuda, T.2    Kamiya, A.3
  • 3
    • 0037135988 scopus 로고    scopus 로고
    • Evidence for a role of platelet endothelial cell adhesion molecule-1 in endothelial cell mechanosignal transduction: is it a mechanoresponsive molecule?
    • Osawa M, Masuda M, Kusano K, Fujiwara K. Evidence for a role of platelet endothelial cell adhesion molecule-1 in endothelial cell mechanosignal transduction: is it a mechanoresponsive molecule? J Cell Biol 2002; 158:773-85; http://dx.doi. org/10.1083/jcb.200205049.
    • (2002) J Cell Biol , vol.158 , pp. 773-785
    • Osawa, M.1    Masuda, M.2    Kusano, K.3    Fujiwara, K.4
  • 4
    • 0030002941 scopus 로고    scopus 로고
    • Mechanical strain induces pp60src activation and translocation to cytoskeleton in fetal rat lung cells
    • Liu M, Qin Y, Liu J, Tanswell AK, Post M. Mechanical strain induces pp60src activation and translocation to cytoskeleton in fetal rat lung cells. J Biol Chem 1996; 271:7066-71; http://dx.doi. org/10.1074/jbc.271.12.7066.
    • (1996) J Biol Chem , vol.271 , pp. 7066-7071
    • Liu, M.1    Qin, Y.2    Liu, J.3    Tanswell, A.K.4    Post, M.5
  • 5
    • 0033018894 scopus 로고    scopus 로고
    • Activation of pp60(src) is critical for stretch-induced orienting response in fibroblasts
    • Sai X, Naruse K, Sokabe M. Activation of pp60(src) is critical for stretch-induced orienting response in fibroblasts. J Cell Sci 1999; 112:1365-73.
    • (1999) J Cell Sci , vol.112 , pp. 1365-1373
    • Sai, X.1    Naruse, K.2    Sokabe, M.3
  • 7
    • 0035425939 scopus 로고    scopus 로고
    • Dynamic reorientation of cultured cells and stress fibers under mechanical stress from periodic stretching
    • Hayakawa K, Sato N, Obinata T. Dynamic reorientation of cultured cells and stress fibers under mechanical stress from periodic stretching. Exp Cell Res 2001; 268:104-14; http://dx.doi. org/10.1006/excr.2001.5270.
    • (2001) Exp Cell Res , vol.268 , pp. 104-114
    • Hayakawa, K.1    Sato, N.2    Obinata, T.3
  • 8
    • 0028951747 scopus 로고
    • Molecular mechanism of cardiac cellular hypertrophy by mechanical stress
    • Yamazaki T, Komuro I, Yazaki Y. Molecular mechanism of cardiac cellular hypertrophy by mechanical stress. J Mol Cell Cardiol 1995; 27:133-40; http://dx.doi.org/10.1016/S0022-2828(08)80013-2.
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 133-140
    • Yamazaki, T.1    Komuro, I.2    Yazaki, Y.3
  • 9
    • 0033134111 scopus 로고    scopus 로고
    • Release of mechanical tension triggers apoptosis of human fibroblasts in a model of regressing granulation tissue
    • Grinnell F, Zhu M, Carlson MA, Abrams JM. Release of mechanical tension triggers apoptosis of human fibroblasts in a model of regressing granulation tissue. Exp Cell Res 1999; 248:608-19; http://dx.doi.org/10.1006/excr.1999.4440.
    • (1999) Exp Cell Res , vol.248 , pp. 608-619
    • Grinnell, F.1    Zhu, M.2    Carlson, M.A.3    Abrams, J.M.4
  • 10
    • 34347372032 scopus 로고    scopus 로고
    • Soft substrate induces apoptosis by the disturbance of Ca2+ homeostasis in renal epithelial LLC-PK1 cells
    • Chiu WT, Wang YH, Tang MJ, Shen MR. Soft substrate induces apoptosis by the disturbance of Ca2+ homeostasis in renal epithelial LLC-PK1 cells. J Cell Physiol 2007; 212:401-10; http:// dx.doi.org/10.1002/jcp.21037.
    • (2007) J Cell Physiol , vol.212 , pp. 401-410
    • Chiu, W.T.1    Wang, Y.H.2    Tang, M.J.3    Shen, M.R.4
  • 11
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • Engler AJ, Sen S, Sweeney HL, Discher DE. Matrix elasticity directs stem cell lineage specification. Cell 2006; 126:677-89; http://dx.doi. org/10.1016/j.cell.2006.06.044.
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 12
    • 0025762570 scopus 로고
    • Mechanical transduction by membrane ion channels: a mini review
    • Sachs F. Mechanical transduction by membrane ion channels: a mini review. Mol Cell Biochem 1991; 104:57-60; http://dx.doi. org/10.1007/BF00229804.
    • (1991) Mol Cell Biochem , vol.104 , pp. 57-60
    • Sachs, F.1
  • 13
    • 0030901623 scopus 로고    scopus 로고
    • Mechanosensitive channels of Escherichia coli: the MscL gene, protein, and activities
    • Sukharev SI, Blount P, Martinac B, Kung C. Mechanosensitive channels of Escherichia coli: the MscL gene, protein, and activities. Annu Rev Physiol 1997; 59:633-57; http://dx.doi. org/10.1146/annurev.physiol.59.1.633.
    • (1997) Annu Rev Physiol , vol.59 , pp. 633-657
    • Sukharev, S.I.1    Blount, P.2    Martinac, B.3    Kung, C.4
  • 14
    • 0035855845 scopus 로고    scopus 로고
    • Molecular basis of mechanosensory transduction
    • Gillespie PG, Walker RG. Molecular basis of mechanosensory transduction. Nature 2001; 413:194-202; http://dx.doi. org/10.1038/35093011.
    • (2001) Nature , vol.413 , pp. 194-202
    • Gillespie, P.G.1    Walker, R.G.2
  • 15
    • 0035479910 scopus 로고    scopus 로고
    • Assembly and mechanosensory function of focal contacts
    • Geiger B, Bershadsky A. Assembly and mechanosensory function of focal contacts. Curr Opin Cell Biol 2001; 13:584-92; http://dx.doi. org/10.1016/S0955-0674(00)00255-6.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 584-592
    • Geiger, B.1    Bershadsky, A.2
  • 17
    • 1842530398 scopus 로고    scopus 로고
    • Integrins in mechanotransduction
    • Katsumi A, Orr AW, Tzima E, Schwartz MA. Integrins in mechanotransduction. J Biol Chem 2004; 279:12001-4; http://dx.doi. org/10.1074/jbc.R300038200.
    • (2004) J Biol Chem , vol.279 , pp. 12001-12004
    • Katsumi, A.1    Orr, A.W.2    Tzima, E.3    Schwartz, M.A.4
  • 18
    • 2942624012 scopus 로고    scopus 로고
    • Integrin-dependent signal cascades in chondrocyte mechanotransduction
    • Millward-Sadler SJ, Salter DM. Integrin-dependent signal cascades in chondrocyte mechanotransduction. Ann Biomed Eng 2004; 32:435-46; http://dx.doi.org/10.1023/ B:ABME.0000017538.72511.48.
    • (2004) Ann Biomed Eng , vol.32 , pp. 435-446
    • Millward-Sadler, S.J.1    Salter, D.M.2
  • 19
    • 79952598024 scopus 로고    scopus 로고
    • Integrins and extracellular matrix in mechanotransduction
    • Schwartz MA. Integrins and extracellular matrix in mechanotransduction. Cold Spring Harb Perspect Biol 2010; 2:a005066; http://dx.doi. org/10.1101/cshperspect.a005066.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Schwartz, M.A.1
  • 20
    • 4544242249 scopus 로고    scopus 로고
    • Stretch of the vascular wall induces smooth muscle differentiation by promoting actin polymerization
    • Albinsson S, Nordström I, Hellstrand P. Stretch of the vascular wall induces smooth muscle differentiation by promoting actin polymerization. J Biol Chem 2004; 279:34849-55; http://dx.doi. org/10.1074/jbc.M403370200.
    • (2004) J Biol Chem , vol.279 , pp. 34849-34855
    • Albinsson, S.1    Nordström, I.2    Hellstrand, P.3
  • 21
    • 0030425905 scopus 로고    scopus 로고
    • Stimulus-dependent disorganization of actin filaments induced by overexpression of cofilin in C2 myoblasts
    • Ono S, Abe H, Obinata T. Stimulus-dependent disorganization of actin filaments induced by overexpression of cofilin in C2 myoblasts. Cell Struct Funct 1996; 21:491-9; http://dx.doi.org/10.1247/ csf.21.491.
    • (1996) Cell Struct Funct , vol.21 , pp. 491-499
    • Ono, S.1    Abe, H.2    Obinata, T.3
  • 22
    • 40949165235 scopus 로고    scopus 로고
    • Actin stress fibers transmit and focus force to activate mechanosensitive channels
    • Hayakawa K, Tatsumi H, Sokabe M. Actin stress fibers transmit and focus force to activate mechanosensitive channels. J Cell Sci 2008; 121:496-503; http://dx.doi.org/10.1242/ jcs.022053.
    • (2008) J Cell Sci , vol.121 , pp. 496-503
    • Hayakawa, K.1    Tatsumi, H.2    Sokabe, M.3
  • 23
    • 80054079832 scopus 로고    scopus 로고
    • Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament
    • Hayakawa K, Tatsumi H, Sokabe M. Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament. J Cell Biol 2011; 195:721-7; http://dx.doi. org/10.1083/jcb.201102039.
    • (2011) J Cell Biol , vol.195 , pp. 721-727
    • Hayakawa, K.1    Tatsumi, H.2    Sokabe, M.3
  • 24
    • 0031577459 scopus 로고    scopus 로고
    • Activation of JNK/SAPK and ERK by mechanical strain in vascular smooth muscle cells depends on extracellular matrix composition
    • Reusch HP, Chan G, Ives HE, Nemenoff RA. Activation of JNK/SAPK and ERK by mechanical strain in vascular smooth muscle cells depends on extracellular matrix composition. Biochem Biophys Res Commun 1997; 237:239-44; http:// dx.doi.org/10.1006/bbrc.1997.7121.
    • (1997) Biochem Biophys Res Commun , vol.237 , pp. 239-244
    • Reusch, H.P.1    Chan, G.2    Ives, H.E.3    Nemenoff, R.A.4
  • 25
    • 0033931172 scopus 로고    scopus 로고
    • Integrin and mechanosensitive ion channeldependent tyrosine phosphorylation of focal adhesion proteins and beta-catenin in human articular chondrocytes after mechanical stimulation
    • Lee HS, Millward-Sadler SJ, Wright MO, Nuki G, Salter DM. Integrin and mechanosensitive ion channeldependent tyrosine phosphorylation of focal adhesion proteins and beta-catenin in human articular chondrocytes after mechanical stimulation. J Bone Miner Res 2000; 15:1501-9; http://dx.doi. org/10.1359/jbmr.2000.15.8.1501.
    • (2000) J Bone Miner Res , vol.15 , pp. 1501-1509
    • Lee, H.S.1    Millward-Sadler, S.J.2    Wright, M.O.3    Nuki, G.4    Salter, D.M.5
  • 26
    • 0035949694 scopus 로고    scopus 로고
    • Focal adhesion kinase is involved in mechanosensing during fibroblast migration
    • Wang HB, Dembo M, Hanks SK, Wang Y. Focal adhesion kinase is involved in mechanosensing during fibroblast migration. Proc Natl Acad Sci U S A 2001; 98:11295-300; http://dx.doi. org/10.1073/pnas.201201198.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11295-11300
    • Wang, H.B.1    Dembo, M.2    Hanks, S.K.3    Wang, Y.4
  • 27
    • 3042820402 scopus 로고    scopus 로고
    • Mechanical stimuli regulate rapamycin-sensitive signalling by a phosphoinositide 3-kinase-, protein kinase B- and growth factorindependent mechanism
    • Hornberger TA, Stuppard R, Conley KE, Fedele MJ, Fiorotto ML, Chin ER, et al. Mechanical stimuli regulate rapamycin-sensitive signalling by a phosphoinositide 3-kinase-, protein kinase B- and growth factorindependent mechanism. Biochem J 2004; 380:795-804; http://dx.doi.org/10.1042/ BJ20040274.
    • (2004) Biochem J , vol.380 , pp. 795-804
    • Hornberger, T.A.1    Stuppard, R.2    Conley, K.E.3    Fedele, M.J.4    Fiorotto, M.L.5    Chin, E.R.6
  • 29
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
    • Sakai R, Iwamatsu A, Hirano N, Ogawa S, Tanaka T, Mano H, et al. A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J 1994; 13:3748-56.
    • (1994) EMBO J , vol.13 , pp. 3748-3756
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Mano, H.6
  • 30
    • 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 DH, Critchley DR, Sheetz MP. Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation. J Cell Biol 2003; 163:409-19; http://dx.doi.org/10.1083/ jcb.200302001.
    • (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
  • 31
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith CG, Yamada KM, Sheetz MP. The relationship between force and focal complex development. J Cell Biol 2002; 159:695-705; http://dx.doi.org/10.1083/jcb.200204153.
    • (2002) J Cell Biol , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 32
    • 0041461882 scopus 로고    scopus 로고
    • Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin
    • Jiang G, Giannone G, Critchley DR, Fukumoto E, Sheetz MP. Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 2003; 424:334-7; http://dx.doi. org/10.1038/nature01805.
    • (2003) Nature , vol.424 , pp. 334-337
    • Jiang, G.1    Giannone, G.2    Critchley, D.R.3    Fukumoto, E.4    Sheetz, M.P.5
  • 33
    • 0035074552 scopus 로고    scopus 로고
    • Rap1 is involved in cell stretching modulation of p38 but not ERK or JNK MAP kinase
    • Sawada Y, Nakamura K, Doi K, Takeda K, Tobiume K, Saitoh M, et al. Rap1 is involved in cell stretching modulation of p38 but not ERK or JNK MAP kinase. J Cell Sci 2001; 114:1221-7.
    • (2001) J Cell Sci , vol.114 , pp. 1221-1227
    • Sawada, Y.1    Nakamura, K.2    Doi, K.3    Takeda, K.4    Tobiume, K.5    Saitoh, M.6
  • 34
    • 33751335857 scopus 로고    scopus 로고
    • Force sensing by mechanical extension of the Src family kinase substrate p130Cas
    • Sawada Y, Tamada M, Dubin-Thaler BJ, Cherniavskaya O, Sakai R, Tanaka S, et al. Force sensing by mechanical extension of the Src family kinase substrate p130Cas. Cell 2006; 127:1015-26; http:// dx.doi.org/10.1016/j.cell.2006.09.044.
    • (2006) Cell , vol.127 , pp. 1015-1026
    • Sawada, Y.1    Tamada, M.2    Dubin-Thaler, B.J.3    Cherniavskaya, O.4    Sakai, R.5    Tanaka, S.6
  • 36
    • 20644440418 scopus 로고    scopus 로고
    • The kinase domain of titin controls muscle gene expression and protein turnover
    • Lange S, Xiang F, Yakovenko A, Vihola A, Hackman P, Rostkova E, et al. The kinase domain of titin controls muscle gene expression and protein turnover. Science 2005; 308:1599-603; http://dx.doi. org/10.1126/science.1110463.
    • (2005) Science , vol.308 , pp. 1599-1603
    • Lange, S.1    Xiang, F.2    Yakovenko, A.3    Vihola, A.4    Hackman, P.5    Rostkova, E.6
  • 37
    • 0037117522 scopus 로고    scopus 로고
    • Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension
    • Baneyx G, Baugh L, Vogel V. Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension. Proc Natl Acad Sci U S A 2002; 99:5139-43; http://dx.doi. org/10.1073/pnas.072650799.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 5139-5143
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 38
    • 0028364087 scopus 로고
    • Fibronectin's III-1 module contains a conformationdependent binding site for the amino-terminal region of fibronectin
    • Hocking DC, Sottile J, McKeown-Longo PJ. Fibronectin's III-1 module contains a conformationdependent binding site for the amino-terminal region of fibronectin. J Biol Chem 1994; 269:19183-7.
    • (1994) J Biol Chem , vol.269 , pp. 19183-19187
    • Hocking, D.C.1    Sottile, J.2    McKeown-Longo, P.J.3
  • 39
    • 48649102251 scopus 로고    scopus 로고
    • Fibronectin unfolding revisited: modeling cell traction-mediated unfolding of the tenth type-III repeat
    • Gee EP, Ingber DE, Stultz CM. Fibronectin unfolding revisited: modeling cell traction-mediated unfolding of the tenth type-III repeat. PLoS One 2008; 3:e2373; http://dx.doi.org/10.1371/journal. pone.0002373.
    • (2008) PLoS One , vol.3
    • Gee, E.P.1    Ingber, D.E.2    Stultz, C.M.3
  • 40
    • 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. Identification of novel graded polarity actin filament bundles in locomoting heart fibroblasts: implications for the generation of motile force. J Cell Biol 1997; 136:1287-305; http://dx.doi.org/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
  • 41
    • 0035002155 scopus 로고    scopus 로고
    • Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates
    • Balaban NQ, Schwarz US, Riveline D, Goichberg P, Tzur G, Sabanay I, et al. Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates. Nat Cell Biol 2001; 3:466-72; http://dx.doi. org/10.1038/35074532.
    • (2001) Nat Cell Biol , vol.3 , pp. 466-472
    • Balaban, N.Q.1    Schwarz, U.S.2    Riveline, D.3    Goichberg, P.4    Tzur, G.5    Sabanay, I.6
  • 42
    • 0032516848 scopus 로고    scopus 로고
    • Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins Comparison of plant and human ADFs and effect of phosphorylation
    • Ressad F, Didry D, Xia GX, Hong Y, Chua NH, Pantaloni D, et al. Kinetic analysis of the interaction of actin-depolymerizing factor (ADF)/cofilin with G- and F-actins. Comparison of plant and human ADFs and effect of phosphorylation. J Biol Chem 1998; 273:20894-902; http://dx.doi. org/10.1074/jbc.273.33.20894.
    • (1998) J Biol Chem , vol.273 , pp. 20894-20902
    • Ressad, F.1    Didry, D.2    Xia, G.X.3    Hong, Y.4    Chua, N.H.5    Pantaloni, D.6
  • 43
    • 77952196594 scopus 로고    scopus 로고
    • The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament
    • De La Cruz EM, Sept D. The kinetics of cooperative cofilin binding reveals two states of the cofilin-actin filament. Biophys J 2010; 98:1893-901; http://dx.doi.org/10.1016/j. bpj.2010.01.023.
    • (2010) Biophys J , vol.98 , pp. 1893-1901
    • De La Cruz, E.M.1    Sept, D.2
  • 44
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function
    • McGough A, Pope B, Chiu W, Weeds A. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J Cell Biol 1997; 138:771-81; http://dx.doi. org/10.1083/jcb.138.4.771.
    • (1997) J Cell Biol , vol.138 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 45
    • 0035795407 scopus 로고    scopus 로고
    • Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits
    • Galkin VE, Orlova A, Lukoyanova N, Wriggers W, Egelman EH. Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J Cell Biol 2001; 153:75-86; http://dx.doi.org/10.1083/ jcb.153.1.75.
    • (2001) J Cell Biol , vol.153 , pp. 75-86
    • Galkin, V.E.1    Orlova, A.2    Lukoyanova, N.3    Wriggers, W.4    Egelman, E.H.5
  • 46
    • 80053311771 scopus 로고    scopus 로고
    • The interaction of cofilin with the actin filament
    • Wong DY, Sept D. The interaction of cofilin with the actin filament. J Mol Biol 2011; 413:97-105; http://dx.doi.org/10.1016/j. jmb.2011.08.039.
    • (2011) J Mol Biol , vol.413 , pp. 97-105
    • Wong, D.Y.1    Sept, D.2
  • 47
    • 84856991361 scopus 로고    scopus 로고
    • Actin filaments as tension sensors
    • Galkin VE, Orlova A, Egelman EH. Actin filaments as tension sensors. Curr Biol 2012; 22:R96-101; http://dx.doi.org/10.1016/j. cub.2011.12.010.
    • (2012) Curr Biol , vol.22
    • Galkin, V.E.1    Orlova, A.2    Egelman, E.H.3
  • 48
    • 84855875234 scopus 로고    scopus 로고
    • Force- and Ca2+-dependent internalization of integrins in cultured endothelial cells
    • Kiyoshima D, Kawakami K, Hayakawa K, Tatsumi H, Sokabe M. Force- and Ca2+-dependent internalization of integrins in cultured endothelial cells. J Cell Sci 2011; 124:3859-70; http://dx.doi. org/10.1242/jcs.088559.
    • (2011) J Cell Sci , vol.124 , pp. 3859-3870
    • Kiyoshima, D.1    Kawakami, K.2    Hayakawa, K.3    Tatsumi, H.4    Sokabe, M.5
  • 50
    • 12844279136 scopus 로고    scopus 로고
    • Cyclic changes in keratocyte speed and traction stress arise from Ca2+-dependent regulation of cell adhesiveness
    • Doyle AD, Lee J. Cyclic changes in keratocyte speed and traction stress arise from Ca2+-dependent regulation of cell adhesiveness. J Cell Sci 2005; 118:369-79; http://dx.doi.org/10.1242/ jcs.01590.
    • (2005) J Cell Sci , vol.118 , pp. 369-379
    • Doyle, A.D.1    Lee, J.2
  • 51
    • 33646386142 scopus 로고    scopus 로고
    • Stress fibers are generated by two distinct actin assembly mechanisms in motile cells
    • Hotulainen P, Lappalainen P. Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J Cell Biol 2006; 173:383-94; http://dx.doi.org/10.1083/jcb.200511093.
    • (2006) J Cell Biol , vol.173 , pp. 383-394
    • Hotulainen, P.1    Lappalainen, P.2
  • 52
    • 80054710650 scopus 로고    scopus 로고
    • LIM kinase has a dual role in regulating lamellipodium extension by decelerating the rate of actin retrograde flow and the rate of actin polymerization
    • Ohashi K, Fujiwara S, Watanabe T, Kondo H, Kiuchi T, Sato M, et al. LIM kinase has a dual role in regulating lamellipodium extension by decelerating the rate of actin retrograde flow and the rate of actin polymerization. J Biol Chem 2011; 286:36340-51; http://dx.doi.org/10.1074/jbc. M111.259135.
    • (2011) J Biol Chem , vol.286 , pp. 36340-36351
    • Ohashi, K.1    Fujiwara, S.2    Watanabe, T.3    Kondo, H.4    Kiuchi, T.5    Sato, M.6
  • 53
    • 77954486800 scopus 로고    scopus 로고
    • Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics
    • Grashoff C, Hoffman BD, Brenner MD, Zhou R, Parsons M, Yang MT, et al. Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics. Nature 2010; 466:263-6; http://dx.doi.org/10.1038/nature09198.
    • (2010) Nature , vol.466 , pp. 263-266
    • Grashoff, C.1    Hoffman, B.D.2    Brenner, M.D.3    Zhou, R.4    Parsons, M.5    Yang, M.T.6
  • 54
    • 0017639363 scopus 로고
    • Phalloidin-induced actin polymerization in the cytoplasm of cultured cells interferes with cell locomotion and growth
    • Wehland J, Osborn M, Weber K. Phalloidin-induced actin polymerization in the cytoplasm of cultured cells interferes with cell locomotion and growth. Proc Natl Acad Sci U S A 1977; 74:5613-7; http://dx.doi.org/10.1073/pnas.74.12.5613.
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 5613-5617
    • Wehland, J.1    Osborn, M.2    Weber, K.3
  • 55
    • 36248969983 scopus 로고    scopus 로고
    • Actin stress fibres
    • Pellegrin S, Mellor H. Actin stress fibres. J Cell Sci 2007; 120:3491-9; http://dx.doi. org/10.1242/jcs.018473.
    • (2007) J Cell Sci , vol.120 , pp. 3491-3499
    • Pellegrin, S.1    Mellor, H.2
  • 56
    • 79951909900 scopus 로고    scopus 로고
    • Cancer cell invasion is enhanced by applied mechanical stimulation
    • Menon S, Beningo KA. Cancer cell invasion is enhanced by applied mechanical stimulation. PLoS One 2011; 6:e17277; http://dx.doi. org/10.1371/journal.pone.0017277.
    • (2011) PLoS One , vol.6
    • Menon, S.1    Beningo, K.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.