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Volumn 10, Issue 9, 2008, Pages 1039-1050

Actin and α-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA ACTIN; GREEN FLUORESCENT PROTEIN; MYOSIN II; MYOSIN IIA; PAXILLIN; TALIN;

EID: 51049104617     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1763     Document Type: Article
Times cited : (637)

References (49)
  • 1
    • 1642586962 scopus 로고    scopus 로고
    • FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly
    • Webb, D. J. et al. FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly. Nature Cell Biol. 6, 154-161 (2004).
    • (2004) Nature Cell Biol , vol.6 , pp. 154-161
    • Webb, D.J.1
  • 2
    • 0344305784 scopus 로고    scopus 로고
    • Cell migration: Integrating signals from front to back
    • Ridley, A. J. et al. Cell migration: Integrating signals from front to back. Science 302, 1704-1709(2003).
    • (2003) Science , vol.302 , pp. 1704-1709
    • Ridley, A.J.1
  • 3
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D. A. & Horwitz, A. F. Cell migration: A physically integrated molecular process. Cell 84, 359-369 (1996).
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 4
    • 0036229694 scopus 로고    scopus 로고
    • Networks and crosstalk: Integrin signalling spreads
    • Schwartz, M. A. & Ginsberg, M. H. Networks and crosstalk: Integrin signalling spreads. Nature Cell Biol. 4, E65-68 (2002).
    • (2002) Nature Cell Biol , vol.4
    • Schwartz, M.A.1    Ginsberg, M.H.2
  • 5
    • 0035858878 scopus 로고    scopus 로고
    • Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts
    • Beningo, K. A., Dembo, M., Kaverina, I., Small, J. V. & Wang, Y. L. Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts. J. Cell Biol. 153 881-888 (2001).
    • (2001) J. Cell Biol , vol.153 , pp. 881-888
    • Beningo, K.A.1    Dembo, M.2    Kaverina, I.3    Small, J.V.4    Wang, Y.L.5
  • 6
    • 33646776346 scopus 로고    scopus 로고
    • Paxillin phosphorylation at Ser 273 localizes a GIT1-PIX-PAK complex and regulates adhesion and protrusion dynamics
    • Nayal, A. et al. Paxillin phosphorylation at Ser 273 localizes a GIT1-PIX-PAK complex and regulates adhesion and protrusion dynamics. J. Cell Biol. 173, 587-589 (2006).
    • (2006) J. Cell Biol , vol.173 , pp. 587-589
    • Nayal, A.1
  • 8
    • 0036222784 scopus 로고    scopus 로고
    • Adhesion assembly, disassembly and tumover in migrating cells - over and over and over again
    • Webb, D. J., Parsons, J. T. & Horwitz, A. F. Adhesion assembly, disassembly and tumover in migrating cells - over and over and over again. Nature Cell Biol. 4, E97-E100 (2002).
    • (2002) Nature Cell Biol , vol.4
    • Webb, D.J.1    Parsons, J.T.2    Horwitz, A.F.3
  • 9
    • 4544309783 scopus 로고    scopus 로고
    • Two distinct actin networks drive the protrusion of migrating cells
    • Ponti, A., Machacek, M., Gupton, S. L., Waterman-Storer, C. M. & Danuser, G. Two distinct actin networks drive the protrusion of migrating cells. Science 305, 1782-1786 (2004).
    • (2004) Science , vol.305 , pp. 1782-1786
    • Ponti, A.1    Machacek, M.2    Gupton, S.L.3    Waterman-Storer, C.M.4    Danuser, G.5
  • 10
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina, T. M. & Borisy, G. G. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145, 1009-1026 (1999).
    • (1999) J. Cell Biol , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 11
    • 33745245989 scopus 로고    scopus 로고
    • Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration
    • Gupton, S. L. & Waterman-Storer, C. M. Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration. Cell 125, 1361-1374 (2006).
    • (2006) Cell , vol.125 , pp. 1361-1374
    • Gupton, S.L.1    Waterman-Storer, C.M.2
  • 12
    • 33846672361 scopus 로고    scopus 로고
    • Lamellipodial actin mechanically links myosin activity with adhesion-site formation
    • Giannone, G. et al. Lamellipodial actin mechanically links myosin activity with adhesion-site formation. Cell 128, 561-575 (2007).
    • (2007) Cell , vol.128 , pp. 561-575
    • Giannone, G.1
  • 13
    • 1542315352 scopus 로고    scopus 로고
    • Nanometer analysis of cell spreading on matrix-coated surfaces reveals two distinct cell states and STEPs
    • Dubin-Thaier, B. J., Giannone, G., Dobereiner, H. G. & Sheetz, M. P. Nanometer analysis of cell spreading on matrix-coated surfaces reveals two distinct cell states and STEPs. Biophys. J. 86, 1794-1806 (2004).
    • (2004) Biophys. J , vol.86 , pp. 1794-1806
    • Dubin-Thaier, B.J.1    Giannone, G.2    Dobereiner, H.G.3    Sheetz, M.P.4
  • 14
    • 33847354235 scopus 로고    scopus 로고
    • Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells
    • Vicente-Manzanares, M., Zareno, J., Whitmore, L., Choi, C. K. & Horwitz, A. F. Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells. J. Cell Biol. 176, 573-580 (2007).
    • (2007) J. Cell Biol , vol.176 , pp. 573-580
    • Vicente-Manzanares, M.1    Zareno, J.2    Whitmore, L.3    Choi, C.K.4    Horwitz, A.F.5
  • 15
    • 33748309166 scopus 로고    scopus 로고
    • Adhesion-mediated mechanosensitivity: A time to experiment, and a time to theorize
    • Bershadsky, A., Kozlov, M. & Geiger, B. Adhesion-mediated mechanosensitivity: A time to experiment, and a time to theorize. Curr. Opin. Cell Biol. 18, 472-481 (2006).
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 472-481
    • Bershadsky, A.1    Kozlov, M.2    Geiger, B.3
  • 16
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith, C. G., Yamada, K. M. & Sheetz, M. P. The relationship between force and focal complex development. J. Cell Biol. 159, 695-705 (2002).
    • (2002) J. Cell Biol , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 17
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDial-dependent and ROCK-independent mechanism
    • Riveline, D. et al. Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDial-dependent and ROCK-independent mechanism. J. Cell Biol. 153, 1175-1186 (2001).
    • (2001) J. Cell Biol , vol.153 , pp. 1175-1186
    • Riveline, D.1
  • 18
    • 0037043341 scopus 로고    scopus 로고
    • Effects of cell tension on the small GTPase Rac
    • Katsumi, A. et al. Effects of cell tension on the small GTPase Rac. J. Cell Biol. 158, 153-164 (2002).
    • (2002) J. Cell Biol , vol.158 , pp. 153-164
    • Katsumi, A.1
  • 19
    • 0029786313 scopus 로고    scopus 로고
    • Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase)
    • Amano, M. et al. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J. Biol. Chem. 271, 20246-20249 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 20246-20249
    • Amano, M.1
  • 20
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M. & Burridge, K. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133, 1403-1415 (1996).
    • (1996) J. Cell Biol , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 21
    • 33846781373 scopus 로고    scopus 로고
    • A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
    • Zaidel-Bar, R., Milo, R., Kam, Z. & Geiger, B. A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J. Cell Sci. 120, 137-148 (2007).
    • (2007) J. Cell Sci , vol.120 , pp. 137-148
    • Zaidel-Bar, R.1    Milo, R.2    Kam, Z.3    Geiger, B.4
  • 22
    • 0344465841 scopus 로고    scopus 로고
    • Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells
    • Zaidel-Bar, R., Ballestrem, C., Kam, Z. & Geiger, B. Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells, J. Cell Sci. 116, 4605-4613 (2003).
    • (2003) J. Cell Sci , vol.116 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 23
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D. & Halt, A. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53-62 (1995).
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Halt, A.2
  • 24
    • 0033577975 scopus 로고    scopus 로고
    • Interplay between Rac and Rho in the control of substrate contact dynamics
    • Rottner, K., Hall, A. & Small, J. V. Interplay between Rac and Rho in the control of substrate contact dynamics. Curr. Biol. 9, 640-649 (1999).
    • (1999) Curr. Biol , vol.9 , pp. 640-649
    • Rottner, K.1    Hall, A.2    Small, J.V.3
  • 25
    • 0037039770 scopus 로고    scopus 로고
    • Single-molecule speckle analysis of actin filament turnover in lamellipodia
    • Watanabe, N. & Mitchison, T. J. Single-molecule speckle analysis of actin filament turnover in lamellipodia. Science 295, 1083-1086 (2002).
    • (2002) Science , vol.295 , pp. 1083-1086
    • Watanabe, N.1    Mitchison, T.J.2
  • 26
    • 2442481067 scopus 로고    scopus 로고
    • α-actinin revisited: A fresh look at an old player
    • Otey, C. & Carpen, O. α-actinin revisited: A fresh look at an old player. Cell Motil. Cytoskeleton 58, 104-111 (2004).
    • (2004) Cell Motil. Cytoskeleton , vol.58 , pp. 104-111
    • Otey, C.1    Carpen, O.2
  • 27
    • 20744438782 scopus 로고    scopus 로고
    • Disease-associated mutations and alternative splicing alter the enzymatic and motile activity of nonmuscle myosins II-B and II
    • Kim, K. Y., Kovacs, M., Kawamoto, S., Sellers, J. R. & Adelstein, R. S. Disease-associated mutations and alternative splicing alter the enzymatic and motile activity of nonmuscle myosins II-B and II.-C. J. Biol. Chem. 280, 22769-22775 (2005).
    • (2005) C. J. Biol. Chem , vol.280 , pp. 22769-22775
    • Kim, K.Y.1    Kovacs, M.2    Kawamoto, S.3    Sellers, J.R.4    Adelstein, R.S.5
  • 28
    • 0037195954 scopus 로고    scopus 로고
    • Mutations in human nonmuscle myosin IIA found in patients with May-Hegglin anomaly and Fechtner syndrome result in impaired enzymatic function
    • Hu, A., Wang, F. & Sellers, J. R. Mutations in human nonmuscle myosin IIA found in patients with May-Hegglin anomaly and Fechtner syndrome result in impaired enzymatic function. J. Biol. Chem. 277, 46512-46517 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 46512-46517
    • Hu, A.1    Wang, F.2    Sellers, J.R.3
  • 29
    • 33751091524 scopus 로고    scopus 로고
    • Disruption of α-actinin-integrin interactions at focal adhesions renders osteoblasts susceptible to apoptosis
    • Triplett, J. W. & Pavalko, F. M. Disruption of α-actinin-integrin interactions at focal adhesions renders osteoblasts susceptible to apoptosis. Am. J. Physiol. Cell. Physiol. 291, C909-C921 (2006).
    • (2006) Am. J. Physiol. Cell. Physiol , vol.291
    • Triplett, J.W.1    Pavalko, F.M.2
  • 30
    • 1542380678 scopus 로고    scopus 로고
    • Periodic lamellipodial contractions correlate with rearward actin waves
    • Giannone, G. et al. Periodic lamellipodial contractions correlate with rearward actin waves. Cell 116, 431-443 (2004).
    • (2004) Cell , vol.116 , pp. 431-443
    • Giannone, G.1
  • 31
    • 0037049555 scopus 로고    scopus 로고
    • Recruitment of the Arp2/3 complex to vinculin: Coupling membrane protrusion to matrix adhesion
    • DeMali, K. A., Barlow, C. A. & Burridge, K. Recruitment of the Arp2/3 complex to vinculin: Coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159, 881-891 (2002).
    • (2002) J. Cell Biol , vol.159 , pp. 881-891
    • DeMali, K.A.1    Barlow, C.A.2    Burridge, K.3
  • 32
    • 34548316989 scopus 로고    scopus 로고
    • Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex
    • Serrels, B. et al. Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex. Nature Cell Biol. 9, 1046-1056 (2007).
    • (2007) Nature Cell Biol , vol.9 , pp. 1046-1056
    • Serrels, B.1
  • 33
    • 0034597092 scopus 로고    scopus 로고
    • Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/ 3 complex
    • Weed, S. A. et al. Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/ 3 complex. J. Cell. Biol. 151, 29-40 (2000).
    • (2000) J. Cell. Biol , vol.151 , pp. 29-40
    • Weed, S.A.1
  • 34
    • 33847159264 scopus 로고    scopus 로고
    • Polymerizing actin fibers position integrins primed to probe for adhesion sites
    • Galbraith, C. G., Yamada, K. M. & Galbraith, J. A. Polymerizing actin fibers position integrins primed to probe for adhesion sites. Science 315, 992-995 (2007).
    • (2007) Science , vol.315 , pp. 992-995
    • Galbraith, C.G.1    Yamada, K.M.2    Galbraith, J.A.3
  • 35
    • 24644441368 scopus 로고    scopus 로고
    • The comings and goings of actin: Coupling protrusion and retraction in cell motility
    • Small, J. V. & Resch, G. P. The comings and goings of actin: Coupling protrusion and retraction in cell motility. Curr. Opin. Cell Biol. 17, 517-523 (2005)
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 517-523
    • Small, J.V.1    Resch, G.P.2
  • 36
    • 0021627104 scopus 로고
    • Spreading of non-transformed and transformed cells
    • Vasiliev, J. M. Spreading of non-transformed and transformed cells. Biochim. Biophys. Acta 780, 21-65 (1985).
    • (1985) Biochim. Biophys. Acta , vol.780 , pp. 21-65
    • Vasiliev, J.M.1
  • 37
    • 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. 173, 383-394 (2006).
    • (2006) J. Cell Biol , vol.173 , pp. 383-394
    • Hotulainen, P.1    Lappalainen, P.2
  • 38
    • 0035954424 scopus 로고    scopus 로고
    • Differential dynamics of α5 integrin, paxillin, and α-actinin during formation and disassembly of adhesions in migrating cells
    • Laukaitis, C. M., Webb, D. J., Donais, K. & Horwitz, A. F. Differential dynamics of α5 integrin, paxillin, and α-actinin during formation and disassembly of adhesions in migrating cells. J. Cell Biol. 153 1427-1440 (2006).
    • (2006) J. Cell Biol , vol.153 , pp. 1427-1440
    • Laukaitis, C.M.1    Webb, D.J.2    Donais, K.3    Horwitz, A.F.4
  • 39
    • 1542314212 scopus 로고    scopus 로고
    • Nonmuscle myosin IIb is involved in the guidance of fibroblast migration
    • Lo, C. M. et al. Nonmuscle myosin IIb is involved in the guidance of fibroblast migration. Mol. Biol. Cell 15, 982-989 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 982-989
    • Lo, C.M.1
  • 40
    • 33751225683 scopus 로고    scopus 로고
    • Nonmuscle myoson IIA-dependent force inhibits cell spreading and drives F-actin flow
    • Cal, Y. et al. Nonmuscle myoson IIA-dependent force inhibits cell spreading and drives F-actin flow. Biophys. J. 91, 3907-3920 (2006).
    • (2006) Biophys. J , vol.91 , pp. 3907-3920
    • Cal, Y.1
  • 41
    • 0035313171 scopus 로고    scopus 로고
    • During multicellular migration, myosn II serves a structural role independent of its motor function
    • Xu, X. S. et al. During multicellular migration, myosn II serves a structural role independent of its motor function. Dev. Biol. 232, 255-264 (2001).
    • (2001) Dev. Biol , vol.232 , pp. 255-264
    • Xu, X.S.1
  • 42
    • 2542428351 scopus 로고    scopus 로고
    • A point mutation in the motor domain of nonmuscle myosin II-B impairs migration of distinct groups of neurons
    • Ma, X., Kawamoto, S., Hara, Y. & Adelstein, R. S. A point mutation in the motor domain of nonmuscle myosin II-B impairs migration of distinct groups of neurons. Mol. Biol. Cell 15, 2568-2579 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2568-2579
    • Ma, X.1    Kawamoto, S.2    Hara, Y.3    Adelstein, R.S.4
  • 44
    • 0033787392 scopus 로고    scopus 로고
    • Conditional expression of a truncated fragment of nonmuscle myosin II-A alters cell shape but not cytokinesis in HeLa cells
    • Wei, Q. & Adelstein, R. S. Conditional expression of a truncated fragment of nonmuscle myosin II-A alters cell shape but not cytokinesis in HeLa cells. Mol. Biol. Cell 11, 3617-3627 (2000).
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3617-3627
    • Wei, Q.1    Adelstein, R.S.2
  • 45
    • 4444339659 scopus 로고    scopus 로고
    • Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension
    • DesMarais, V., Macaluso, F., Condeelis, J. & Bailly, M. Synergistic interaction between the Arp2/3 complex and cofilin drives stimulated lamellipod extension. J. Cell Sci. 117, 3499-3510 (2004).
    • (2004) J. Cell Sci , vol.117 , pp. 3499-3510
    • DesMarais, V.1    Macaluso, F.2    Condeelis, J.3    Bailly, M.4
  • 46
    • 34547101979 scopus 로고    scopus 로고
    • Association of the tensin N-terminal protein-tyrosine phosphatase domain with the alpha isoform of protein phosphatase-1 in focal adhesions
    • Eto, M., Kirkbride, J., Elliott, E., Lo, S. H. & Brautigan, D. L. Association of the tensin N-terminal protein-tyrosine phosphatase domain with the alpha isoform of protein phosphatase-1 in focal adhesions. J. Biol. Chem. 282, 17806-17815 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 17806-17815
    • Eto, M.1    Kirkbride, J.2    Elliott, E.3    Lo, S.H.4    Brautigan, D.L.5
  • 47
    • 0035162704 scopus 로고    scopus 로고
    • Zyxin is not colocalized with vasodilator-stimutated phosphoprotein (VASP) at lamellipodial tips and exhibits different dynamics to vinculin, paxillin, and VASP in focal adhesions
    • Rottner, K., Krause, M., Gimona, M., Small, J. V. & Wehland, J. Zyxin is not colocalized with vasodilator-stimutated phosphoprotein (VASP) at lamellipodial tips and exhibits different dynamics to vinculin, paxillin, and VASP in focal adhesions. Mol. Biol. Cell 12, 3103-3113 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3103-3113
    • Rottner, K.1    Krause, M.2    Gimona, M.3    Small, J.V.4    Wehland, J.5
  • 48
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner, N. C. et al. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nature Biotechnol. 22, 1567-1572 (2004).
    • (2004) Nature Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1
  • 49
    • 0032576597 scopus 로고    scopus 로고
    • Visualization and molecular analysis of actin assembly in living cells
    • Schafer, D. A. et al. Visualization and molecular analysis of actin assembly in living cells. J. Cell Biol. 143, 1919-1930 (1998).
    • (1998) J. Cell Biol , vol.143 , pp. 1919-1930
    • Schafer, D.A.1


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