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Volumn 24, Issue 7, 2016, Pages 1031-1043

Actin Organization in Cells Responding to a Perforated Surface, Revealed by Live Imaging and Cryo-Electron Tomography

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ACTIN RELATED PROTEIN 2-3 COMPLEX; METHENAMINE; MYOSIN II; PROTOZOAL PROTEIN;

EID: 84978175178     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2016.05.004     Document Type: Article
Times cited : (47)

References (60)
  • 2
    • 15444366581 scopus 로고    scopus 로고
    • Cutting artefacts and cutting process in vitreous sections for cryo-electron microscopy
    • Al-Amoudi, A., Studer, D., Dubochet, J., Cutting artefacts and cutting process in vitreous sections for cryo-electron microscopy. J. Struct. Biol. 150 (2005), 109–121.
    • (2005) J. Struct. Biol. , vol.150 , pp. 109-121
    • Al-Amoudi, A.1    Studer, D.2    Dubochet, J.3
  • 3
    • 0035910096 scopus 로고    scopus 로고
    • Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy
    • Amann, K.J., Pollard, T.D., Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy. Proc. Natl. Acad. Sci. USA 98 (2001), 15009–15013.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15009-15013
    • Amann, K.J.1    Pollard, T.D.2
  • 4
    • 77955445443 scopus 로고    scopus 로고
    • Self-organization of the phosphatidylinositol lipids signaling system for random cell migration
    • Arai, Y., Shibata, T., Matsuoka, S., Sato, M.J., Yanagida, T., Ueda, M., Self-organization of the phosphatidylinositol lipids signaling system for random cell migration. Proc. Natl. Acad. Sci. USA 107 (2010), 12399–12404.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12399-12404
    • Arai, Y.1    Shibata, T.2    Matsuoka, S.3    Sato, M.J.4    Yanagida, T.5    Ueda, M.6
  • 13
    • 0035941075 scopus 로고    scopus 로고
    • Taking cell-matrix adhesions to the third dimension
    • Cukierman, E., Pankov, R., Stevens, D.R., Yamada, K.M., Taking cell-matrix adhesions to the third dimension. Science 294 (2001), 1708–1712.
    • (2001) Science , vol.294 , pp. 1708-1712
    • Cukierman, E.1    Pankov, R.2    Stevens, D.R.3    Yamada, K.M.4
  • 14
    • 0023250545 scopus 로고
    • Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination
    • DeLozanne, A., Spudich, J., Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science 236 (1987), 1086–1091.
    • (1987) Science , vol.236 , pp. 1086-1091
    • DeLozanne, A.1    Spudich, J.2
  • 17
    • 84899462468 scopus 로고    scopus 로고
    • Cellular contact guidance through dynamic sensing of nanotopography
    • Driscoll, M.K., Sun, X., Guven, C., Fourkas, J.T., Losert, W., Cellular contact guidance through dynamic sensing of nanotopography. ACS Nano 8 (2014), 3546–3555.
    • (2014) ACS Nano , vol.8 , pp. 3546-3555
    • Driscoll, M.K.1    Sun, X.2    Guven, C.3    Fourkas, J.T.4    Losert, W.5
  • 18
    • 7544220540 scopus 로고    scopus 로고
    • A brilliant monomeric red fluorescent protein to visualize cytoskeleton dynamics in Dictyostelium
    • Fischer, M., Haase, I., Simmeth, E., Gerisch, G., Müller-Taubenberger, A., A brilliant monomeric red fluorescent protein to visualize cytoskeleton dynamics in Dictyostelium. FEBS Lett. 577 (2004), 227–232.
    • (2004) FEBS Lett. , vol.577 , pp. 227-232
    • Fischer, M.1    Haase, I.2    Simmeth, E.3    Gerisch, G.4    Müller-Taubenberger, A.5
  • 19
    • 0031004852 scopus 로고    scopus 로고
    • Amoeboid movement anchored by eupodia, new actin-rich knobby feet in Dictyostelium
    • Fukui, Y., Inoue, S., Amoeboid movement anchored by eupodia, new actin-rich knobby feet in Dictyostelium. Cell Motil. Cytoskeleton 36 (1997), 339–354.
    • (1997) Cell Motil. Cytoskeleton , vol.36 , pp. 339-354
    • Fukui, Y.1    Inoue, S.2
  • 20
    • 0033602721 scopus 로고    scopus 로고
    • Architectural dynamics of F-actin in eupodia suggests their role in invasive locomotion in Dictyostelium
    • Fukui, Y., de Hostos, E., Yumura, S., Kitanishi-Yumura, T., Inoue, S., Architectural dynamics of F-actin in eupodia suggests their role in invasive locomotion in Dictyostelium. Exp. Cell Res. 249 (1999), 33–45.
    • (1999) Exp. Cell Res. , vol.249 , pp. 33-45
    • Fukui, Y.1    de Hostos, E.2    Yumura, S.3    Kitanishi-Yumura, T.4    Inoue, S.5
  • 21
    • 84914134485 scopus 로고    scopus 로고
    • Actin and PIP3 waves in giant cells reveal the inherent length scale of an excited state
    • Gerhardt, M., Ecke, M., Walz, M., Stengl, A., Beta, C., Gerisch, G., Actin and PIP3 waves in giant cells reveal the inherent length scale of an excited state. J. Cell Sci. 127 (2014), 4507–4517.
    • (2014) J. Cell Sci. , vol.127 , pp. 4507-4517
    • Gerhardt, M.1    Ecke, M.2    Walz, M.3    Stengl, A.4    Beta, C.5    Gerisch, G.6
  • 24
    • 80053523626 scopus 로고    scopus 로고
    • Different modes of state transitions determine pattern in the phosphatidylinositide-actin system
    • Gerisch, G., Ecke, M., Wischnewski, D., Schroth-Diez, B., Different modes of state transitions determine pattern in the phosphatidylinositide-actin system. BMC Cell Biol., 12, 2011, 42.
    • (2011) BMC Cell Biol. , vol.12 , pp. 42
    • Gerisch, G.1    Ecke, M.2    Wischnewski, D.3    Schroth-Diez, B.4
  • 26
    • 84959570276 scopus 로고    scopus 로고
    • Quantitative analysis of filament branch orientation in Listeria actin comet tails
    • Jasnin, M., Crevenna, A.H., Quantitative analysis of filament branch orientation in Listeria actin comet tails. Biophys. J. 110 (2015), 817–826.
    • (2015) Biophys. J. , vol.110 , pp. 817-826
    • Jasnin, M.1    Crevenna, A.H.2
  • 27
    • 6944220067 scopus 로고    scopus 로고
    • Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces
    • Kovar, D.R., Pollard, T.D., Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces. Proc. Natl. Acad. Sci. USA 101 (2004), 14725–14730.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14725-14730
    • Kovar, D.R.1    Pollard, T.D.2
  • 28
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer, J.R., Mastronarde, D.N., McIntosh, J.R., Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116 (1996), 71–76.
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 29
    • 84938359661 scopus 로고    scopus 로고
    • Functional hierarchy of redundant actin assembly factors revealed by fine-grained registration of intrinsic image fluctuations
    • Lee, K., Elliott, H.L., Oak, Y., Zee, C.T., Groisman, A., Tytell, J.D., Danuser, G., Functional hierarchy of redundant actin assembly factors revealed by fine-grained registration of intrinsic image fluctuations. Cell Syst. 1 (2015), 37–50.
    • (2015) Cell Syst. , vol.1 , pp. 37-50
    • Lee, K.1    Elliott, H.L.2    Oak, Y.3    Zee, C.T.4    Groisman, A.5    Tytell, J.D.6    Danuser, G.7
  • 30
    • 84925229596 scopus 로고    scopus 로고
    • Tools of the trade: podosomes as multipurpose organelles of monocytic cells
    • Linder, S., Wiesner, C., Tools of the trade: podosomes as multipurpose organelles of monocytic cells. Cell Mol. Life Sci. 72 (2015), 121–135.
    • (2015) Cell Mol. Life Sci. , vol.72 , pp. 121-135
    • Linder, S.1    Wiesner, C.2
  • 31
    • 33745384269 scopus 로고    scopus 로고
    • Distinct roles of PI(3,4,5)P3 during chemoattractant signaling in Dictyostelium: a quantitative in vivo analysis by inhibition of PI3-kinase
    • Loovers, H.M., Postma, M., Keizer-Gunnink, I., Huang, Y.E., Devreotes, P.N., van Haastert, P.J., Distinct roles of PI(3,4,5)P3 during chemoattractant signaling in Dictyostelium: a quantitative in vivo analysis by inhibition of PI3-kinase. Mol. Biol. Cell 17 (2006), 1503–1513.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1503-1513
    • Loovers, H.M.1    Postma, M.2    Keizer-Gunnink, I.3    Huang, Y.E.4    Devreotes, P.N.5    van Haastert, P.J.6
  • 32
    • 14844330221 scopus 로고    scopus 로고
    • Structural studies by electron tomography: from cells to molecules
    • Lucic, V., Förster, F., Baumeister, W., Structural studies by electron tomography: from cells to molecules. Annu. Rev. Biochem. 74 (2005), 833–865.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 833-865
    • Lucic, V.1    Förster, F.2    Baumeister, W.3
  • 33
    • 33847685630 scopus 로고    scopus 로고
    • Focused-ion-beam thinning of frozen-hydrated biological specimens for cryo-electron microscopy
    • Marko, M., Hsieh, C., Schalek, R., Frank, J., Mannella, C., Focused-ion-beam thinning of frozen-hydrated biological specimens for cryo-electron microscopy. Nat. Methods 4 (2007), 215–217.
    • (2007) Nat. Methods , vol.4 , pp. 215-217
    • Marko, M.1    Hsieh, C.2    Schalek, R.3    Frank, J.4    Mannella, C.5
  • 34
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D.N., Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152 (2005), 36–51.
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 35
    • 0029775654 scopus 로고    scopus 로고
    • Cell motility driven by actin polymerization
    • Mogilner, A., Oster, G., Cell motility driven by actin polymerization. Biophys. J. 71 (1996), 3030–3045.
    • (1996) Biophys. J. , vol.71 , pp. 3030-3045
    • Mogilner, A.1    Oster, G.2
  • 37
  • 38
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins, R.D., Heuser, J.A., Pollard, T.D., The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA 95 (1998), 6181–6186.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 39
    • 34648834682 scopus 로고    scopus 로고
    • The third dimension bridges the gap between cell culture and live tissue
    • Pampaloni, F., Reynaud, E.G., Stelzer, E.H., The third dimension bridges the gap between cell culture and live tissue. Nat. Rev. Mol. Cell Biol. 8 (2007), 839–845.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 839-845
    • Pampaloni, F.1    Reynaud, E.G.2    Stelzer, E.H.3
  • 40
    • 84964344223 scopus 로고    scopus 로고
    • Regulation of invadopodia by mechanical signaling
    • Parekh, A., Weaver, A.M., Regulation of invadopodia by mechanical signaling. Exp. Cell Res. 343 (2015), 89–95.
    • (2015) Exp. Cell Res. , vol.343 , pp. 89-95
    • Parekh, A.1    Weaver, A.M.2
  • 41
    • 0024436810 scopus 로고
    • Capping of surface receptors and concomitant cortical tension are generated by conventional myosin
    • Pasternak, C., Spudich, J.A., Elson, E.L., Capping of surface receptors and concomitant cortical tension are generated by conventional myosin. Nature 341 (1989), 549–551.
    • (1989) Nature , vol.341 , pp. 549-551
    • Pasternak, C.1    Spudich, J.A.2    Elson, E.L.3
  • 42
    • 80052066186 scopus 로고    scopus 로고
    • Perspectives on electron cryo-tomography of vitreous cryo-sections
    • Pierson, J., Vos, M., McIntosh, J.R., Peters, P.J., Perspectives on electron cryo-tomography of vitreous cryo-sections. J. Electron Microsc. (Tokyo) 60:Suppl 1 (2011), S93–S100.
    • (2011) J. Electron Microsc. (Tokyo) , vol.60 , pp. S93-S100
    • Pierson, J.1    Vos, M.2    McIntosh, J.R.3    Peters, P.J.4
  • 43
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • Pollard, T.D., Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 36 (2007), 451–477.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 47
    • 84864386261 scopus 로고    scopus 로고
    • Integrative approaches for cellular cryo-electron tomography: correlative imaging and focused ion beam micromachining
    • Rigort, A., Villa, E., Bäuerlein, F.J., Engel, B.D., Plitzko, J.M., Integrative approaches for cellular cryo-electron tomography: correlative imaging and focused ion beam micromachining. Methods Cell Biol. 111 (2012), 259–281.
    • (2012) Methods Cell Biol. , vol.111 , pp. 259-281
    • Rigort, A.1    Villa, E.2    Bäuerlein, F.J.3    Engel, B.D.4    Plitzko, J.M.5
  • 48
    • 72049090358 scopus 로고    scopus 로고
    • Identification and characterization of a small molecule inhibitor of formin-mediated actin assembly
    • Rizvi, S.A., Neidt, E.M., Cui, J., Feiger, Z., Skau, C.T., Gardel, M.L., Kozmin, S.A., Kovar, D.R., Identification and characterization of a small molecule inhibitor of formin-mediated actin assembly. Chem. Biol. 16 (2009), 1158–1168.
    • (2009) Chem. Biol. , vol.16 , pp. 1158-1168
    • Rizvi, S.A.1    Neidt, E.M.2    Cui, J.3    Feiger, Z.4    Skau, C.T.5    Gardel, M.L.6    Kozmin, S.A.7    Kovar, D.R.8
  • 50
    • 20444426470 scopus 로고    scopus 로고
    • The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia
    • Schirenbeck, A., Bretschneider, T., Arasada, R., Schleicher, M., Faix, J., The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia. Nat. Cell Biol. 7 (2005), 619–625.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 619-625
    • Schirenbeck, A.1    Bretschneider, T.2    Arasada, R.3    Schleicher, M.4    Faix, J.5
  • 51
    • 0037484174 scopus 로고    scopus 로고
    • Modeling tissue-specific signaling and organ function in three dimensions
    • Schmeichel, K.L., Bissell, M.J., Modeling tissue-specific signaling and organ function in three dimensions. J. Cell Sci. 116 (2003), 2377–2388.
    • (2003) J. Cell Sci. , vol.116 , pp. 2377-2388
    • Schmeichel, K.L.1    Bissell, M.J.2
  • 53
    • 84882878737 scopus 로고    scopus 로고
    • Amira: A Highly Interactive System for Visual Data Analysis
    • Elsevier, Butterwoth-Heinemann
    • Stalling, D., Westerhoff, M., Hege, H.-C., Amira: A Highly Interactive System for Visual Data Analysis. 2005, Elsevier, Butterwoth-Heinemann, 749–767.
    • (2005) , pp. 749-767
    • Stalling, D.1    Westerhoff, M.2    Hege, H.-C.3
  • 54
    • 0032510323 scopus 로고    scopus 로고
    • Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells
    • Stauffer, T.P., Ahn, S., Meyer, T., Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells. Curr. Biol. 8 (1998), 343–346.
    • (1998) Curr. Biol. , vol.8 , pp. 343-346
    • Stauffer, T.P.1    Ahn, S.2    Meyer, T.3
  • 55
    • 84885847209 scopus 로고    scopus 로고
    • Opening windows into the cell: focused-ion-beam milling for cryo-electron tomography
    • Villa, E., Schaffer, M., Plitzko, J.M., Baumeister, W., Opening windows into the cell: focused-ion-beam milling for cryo-electron tomography. Curr. Opin. Struct. Biol. 23 (2013), 771–777.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 771-777
    • Villa, E.1    Schaffer, M.2    Plitzko, J.M.3    Baumeister, W.4
  • 56
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos, C.J., Matter, W.F., Hui, K.Y., Brown, R.F., A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 269 (1994), 5241–5248.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 57
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch, M.D., Iwamatsu, A., Mitchison, T.J., Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385 (1997), 265–269.
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 58
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • Welch, M.D., Rosenblatt, J., Skoble, J., Portnoy, D.A., Mitchison, T.J., Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281 (1998), 105–108.
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 59
    • 84885871508 scopus 로고    scopus 로고
    • Correlative cryo-electron tomography and optical microscopy of cells
    • Zhang, P., Correlative cryo-electron tomography and optical microscopy of cells. Curr. Opin. Struct. Biol. 23 (2013), 763–770.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 763-770
    • Zhang, P.1


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