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Volumn 1, Issue 1, 2011, Pages 32-38

Nanoscopy of cell architecture: The actin-membrane interface

Author keywords

Atomic force microscopy; Correlative light and electron microscopy; FCS; Filopodia and lamellipodia; Focal adhesions; FRET; Stress fibres; Supperresolution microscopy

Indexed keywords

ACTIN; CELL PROTEIN; F ACTIN; G ACTIN; GREEN FLUORESCENT PROTEIN;

EID: 84992268377     PISSN: 19490992     EISSN: 1949100X     Source Type: Journal    
DOI: 10.4161/bioa.1.1.14799     Document Type: Note
Times cited : (6)

References (72)
  • 1
    • 45349108739 scopus 로고    scopus 로고
    • The. F-techniques: advances in receptor protein studies
    • Liu P, Ahmed S, Wohland T. The F-techniques: advances in receptor protein studies. Trends Endocrinol Metab 2008; 19:181-90.
    • (2008) Trends Endocrinol Metab , vol.19 , pp. 181-190
    • Liu, P.1    Ahmed, S.2    Wohland, T.3
  • 2
    • 35748946937 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in living cells
    • Kim SA, Heinze KG, Schwille P. Fluorescence correlation spectroscopy in living cells. Nat Methods 2007; 4:963-73.
    • (2007) Nat Methods , vol.4 , pp. 963-973
    • Kim, S.A.1    Heinze, K.G.2    Schwille, P.3
  • 3
    • 34347237194 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: novel variations of an established technique
    • Haustein E, Schwille P. Fluorescence correlation spectroscopy: novel variations of an established technique. Annu Rev Biophys Biomol Struct 2007; 36:151-69.
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 151-169
    • Haustein, E.1    Schwille, P.2
  • 5
    • 77954995399 scopus 로고    scopus 로고
    • A guide to super-resolution fluorescence microscopy
    • Schermelleh L, Heintzmann R, Leonhardt H. A guide to super-resolution fluorescence microscopy. J Cell Biol 2010; 190:165-75.
    • (2010) J Cell Biol , vol.190 , pp. 165-175
    • Schermelleh, L.1    Heintzmann, R.2    Leonhardt, H.3
  • 6
    • 78650512639 scopus 로고    scopus 로고
    • Breaking the diffraction barrier: super-resolution imaging of cells
    • Huang B, Babcock H, Zhuang X. Breaking the diffraction barrier: super-resolution imaging of cells. Cell 2010; 143:1047-58.
    • (2010) Cell , vol.143 , pp. 1047-1058
    • Huang, B.1    Babcock, H.2    Zhuang, X.3
  • 7
    • 65449162388 scopus 로고    scopus 로고
    • Correlative cryo-light microscopy and cryo-electron tomography: from cellular territories to molecular landscapes
    • Plitzko JM, Rigort A, Leis A. Correlative cryo-light microscopy and cryo-electron tomography: from cellular territories to molecular landscapes. Curr Opin Biotechnol 2009; 20:83-9.
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 83-89
    • Plitzko, J.M.1    Rigort, A.2    Leis, A.3
  • 8
    • 59249092115 scopus 로고    scopus 로고
    • Correlative light and electron microscopy
    • Razi M, Tooze SA. Correlative light and electron microscopy. Methods Enzymol 2009; 452:261-75.
    • (2009) Methods Enzymol , vol.452 , pp. 261-275
    • Razi, M.1    Tooze, S.A.2
  • 9
    • 69249159143 scopus 로고    scopus 로고
    • Correlative fluorescence and electron microscopy in tissues: immunocytochemistry
    • Robinson JM, Takizawa T. Correlative fluorescence and electron microscopy in tissues: immunocytochemistry. J Microsc 2009; 235:259-72.
    • (2009) J Microsc , vol.235 , pp. 259-272
    • Robinson, J.M.1    Takizawa, T.2
  • 10
    • 77952411039 scopus 로고    scopus 로고
    • Nanoscale optical imaging by atomic force infrared microscopy
    • Rice JH. Nanoscale optical imaging by atomic force infrared microscopy. Nanoscale 2010; 2:660-7.
    • (2010) Nanoscale , vol.2 , pp. 660-667
    • Rice, J.H.1
  • 11
  • 12
    • 48649106769 scopus 로고    scopus 로고
    • AFM: a nanotool in membrane biology
    • Muller DJ. AFM: a nanotool in membrane biology. Biochemistry 2008; 47:7986-98.
    • (2008) Biochemistry , vol.47 , pp. 7986-7998
    • Muller, D.J.1
  • 16
    • 35748968807 scopus 로고    scopus 로고
    • Spatial regulation of Fus3 MAP kinase activity through a reaction-diffusion mechanism in yeast pheromone signalling
    • Maeder CI, Hink MA, Kinkhabwala A, Mayr R, Bastiaens PI, Knop M. Spatial regulation of Fus3 MAP kinase activity through a reaction-diffusion mechanism in yeast pheromone signalling. Nat Cell Biol 2007; 9:1319-26.
    • (2007) Nat Cell Biol , vol.9 , pp. 1319-1326
    • Maeder, C.I.1    Hink, M.A.2    Kinkhabwala, A.3    Mayr, R.4    Bastiaens, P.I.5    Knop, M.6
  • 17
    • 67649392701 scopus 로고    scopus 로고
    • Determination of in vivo dissociation constant, Kd, of Cdc42-effector complexes in live mammalian cells using single wavelength fluorescence cross-correlation spectroscopy
    • Sudhaharan T, Liu P, Foo YH, Bu W, Lim KB, Wohland T, Ahmed S. Determination of in vivo dissociation constant, Kd, of Cdc42-effector complexes in live mammalian cells using single wavelength fluorescence cross-correlation spectroscopy. J Biol Chem 2009; 284:13602-9.
    • (2009) J Biol Chem , vol.284 , pp. 13602-13609
    • Sudhaharan, T.1    Liu, P.2    Foo, Y.H.3    Bu, W.4    Lim, K.B.5    Wohland, T.6    Ahmed, S.7
  • 18
    • 68949136866 scopus 로고    scopus 로고
    • Determination of dissociation constants in living zebrafish embryos with single wavelength fluorescence cross-correlation spectroscopy
    • Shi X, Foo YH, Sudhaharan T, Chong SW, Korzh V, Ahmed S, et al. Determination of dissociation constants in living zebrafish embryos with single wavelength fluorescence cross-correlation spectroscopy. Biophys J 2009; 97:678-86.
    • (2009) Biophys J , vol.97 , pp. 678-686
    • Shi, X.1    Foo, Y.H.2    Sudhaharan, T.3    Chong, S.W.4    Korzh, V.5    Ahmed, S.6
  • 20
    • 0034028826 scopus 로고    scopus 로고
    • Surpassing the lateral resolution limit by a factor of two using structured illumination microscopy
    • Gustafsson MG. Surpassing the lateral resolution limit by a factor of two using structured illumination microscopy. J Microscopy 2000; 198:82-7.
    • (2000) J Microscopy , vol.198 , pp. 82-87
    • Gustafsson, M.G.1
  • 21
    • 0141792843 scopus 로고    scopus 로고
    • Saturated patterned excitation microscopy with two-dimensional excitation patterns
    • Heintzmann R. Saturated patterned excitation microscopy with two-dimensional excitation patterns. Micron 2003; 34:283-91.
    • (2003) Micron , vol.34 , pp. 283-291
    • Heintzmann, R.1
  • 22
    • 65449189726 scopus 로고    scopus 로고
    • Super-resolution video microscopy of live cells by structured illumination
    • Kner P, Chhun BB, Griffis ER, Winoto L, Gustafsson MG. Super-resolution video microscopy of live cells by structured illumination. Nat Methods 2009; 6:339-42.
    • (2009) Nat Methods , vol.6 , pp. 339-342
    • Kner, P.1    Chhun, B.B.2    Griffis, E.R.3    Winoto, L.4    Gustafsson, M.G.5
  • 24
    • 38049110263 scopus 로고    scopus 로고
    • Dual-color superresolution imaging of genetically expressed probes within individual adhesion complexes
    • Shroff H, Galbraith CG, Galbraith JA, White H, Gillette J, Olenych S, et al. Dual-color superresolution imaging of genetically expressed probes within individual adhesion complexes. Proc Natl Acad Sci USA 2007; 104:20308-13.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20308-20313
    • Shroff, H.1    Galbraith, C.G.2    Galbraith, J.A.3    White, H.4    Gillette, J.5    Olenych, S.6
  • 25
    • 42949083695 scopus 로고    scopus 로고
    • Livecell photoactivated localization microscopy of nanoscale adhesion dynamics
    • Shroff H, Galbraith CG, Galbraith JA, Betzig E. Livecell photoactivated localization microscopy of nanoscale adhesion dynamics. Nat Methods 2008; 5:417-23.
    • (2008) Nat Methods , vol.5 , pp. 417-423
    • Shroff, H.1    Galbraith, C.G.2    Galbraith, J.A.3    Betzig, E.4
  • 26
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust MJ, Bates M, Zhuang X. Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat Methods 2006; 3:793-5.
    • (2006) Nat Methods , vol.3 , pp. 793-795
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 27
    • 34648826792 scopus 로고    scopus 로고
    • Multicolor super-resolution imaging with photo-switchable fluorescent probes
    • Bates M, Huang B, Dempsey GT, Zhuang X. Multicolor super-resolution imaging with photo-switchable fluorescent probes. Science 2007; 317:1749-53.
    • (2007) Science , vol.317 , pp. 1749-1753
    • Bates, M.1    Huang, B.2    Dempsey, G.T.3    Zhuang, X.4
  • 31
    • 0028460042 scopus 로고
    • Breaking the diffraction resolution limit by stimulated emission: stimulated-emissiondepletion fluorescence microscopy
    • Hell SW, Wichmann J. Breaking the diffraction resolution limit by stimulated emission: stimulated-emissiondepletion fluorescence microscopy. Opt Lett 1994; 19:780-2.
    • (1994) Opt Lett , vol.19 , pp. 780-782
    • Hell, S.W.1    Wichmann, J.2
  • 32
    • 0032607671 scopus 로고    scopus 로고
    • Subdiffraction resolution in far-field fluorescence microscopy
    • Klar TA, Hell SW. Subdiffraction resolution in far-field fluorescence microscopy. Opt Lett 1999; 24:954-6.
    • (1999) Opt Lett , vol.24 , pp. 954-956
    • Klar, T.A.1    Hell, S.W.2
  • 37
    • 42149143016 scopus 로고    scopus 로고
    • Three-dimensional resolution doubling in wide-field fluorescence microscopy by structured illumination
    • Gustafsson MG, Shao L, Carlton PM, Wang CJ, Golubovskaya IN, et al. Three-dimensional resolution doubling in wide-field fluorescence microscopy by structured illumination. Biophys J 2008; 94:4957-70.
    • (2008) Biophys J , vol.94 , pp. 4957-4970
    • Gustafsson, M.G.1    Shao, L.2    Carlton, P.M.3    Wang, C.J.4    Golubovskaya, I.N.5
  • 38
    • 45549091077 scopus 로고    scopus 로고
    • Subdiffraction multicolor imaging of the nuclear periphery with 3D structured illumination microscopy
    • Schermelleh L, Carlton PM, Haase S, Shao L, Winoto L, Kner P, et al. Subdiffraction multicolor imaging of the nuclear periphery with 3D structured illumination microscopy. Science 2008; 320:1332-6.
    • (2008) Science , vol.320 , pp. 1332-1336
    • Schermelleh, L.1    Carlton, P.M.2    Haase, S.3    Shao, L.4    Winoto, L.5    Kner, P.6
  • 42
    • 38949216802 scopus 로고    scopus 로고
    • Threedimensional super-resolution imaging by stochastic optical reconstruction microscopy
    • Huang B, Wang W, Bates M, Zhuang X. Threedimensional super-resolution imaging by stochastic optical reconstruction microscopy. Science 2008; 319:810-3.
    • (2008) Science , vol.319 , pp. 810-813
    • Huang, B.1    Wang, W.2    Bates, M.3    Zhuang, X.4
  • 43
    • 57049139281 scopus 로고    scopus 로고
    • Wholecell 3D STORM reveals interactions between cellular structures with nanometer-scale resolution
    • Huang B, Jones SA, Brandenburg B, Zhuang X. Wholecell 3D STORM reveals interactions between cellular structures with nanometer-scale resolution. Nat Methods 2008; 5:1047-52.
    • (2008) Nat Methods , vol.5 , pp. 1047-1052
    • Huang, B.1    Jones, S.A.2    Brandenburg, B.3    Zhuang, X.4
  • 45
    • 56149101340 scopus 로고    scopus 로고
    • Correlative light-electron microscopy (CLEM) combining live-cell imaging and immunolabeling of ultrathin cryosections
    • van Rijnsoever C, Oorschot V, Klumperman J. Correlative light-electron microscopy (CLEM) combining live-cell imaging and immunolabeling of ultrathin cryosections. Nat Methods 2008; 5:973-80.
    • (2008) Nat Methods , vol.5 , pp. 973-980
    • van Rijnsoever, C.1    Oorschot, V.2    Klumperman, J.3
  • 48
    • 77955172060 scopus 로고    scopus 로고
    • Fast, high-contrast imaging of animal development with scanned light sheet-based structuredillumination microscopy
    • Keller PJ, Schmidt AD, Santella A, Khairy K, Bao Z, Wittbrodt J, et al. Fast, high-contrast imaging of animal development with scanned light sheet-based structuredillumination microscopy. Nat Methods 2010; 7:637-42.
    • (2010) Nat Methods , vol.7 , pp. 637-642
    • Keller, P.J.1    Schmidt, A.D.2    Santella, A.3    Khairy, K.4    Bao, Z.5    Wittbrodt, J.6
  • 49
    • 79952114325 scopus 로고    scopus 로고
    • High resolution imaging of actin filaments in living cells under physiologically relevant conditions using apertureless near-field microscopy
    • Wang JJ, Kirkham J, Donegan J, Smith DA. High resolution imaging of actin filaments in living cells under physiologically relevant conditions using apertureless near-field microscopy. J Nanosci Nanotechnol 2010; 10:7489-93.
    • (2010) J Nanosci Nanotechnol , vol.10 , pp. 7489-7493
    • Wang, J.J.1    Kirkham, J.2    Donegan, J.3    Smith, D.A.4
  • 53
    • 41649110901 scopus 로고    scopus 로고
    • Paxillin dynamics measured during adhesion assembly and disassembly by correlation spectroscopy
    • Digman MA, Brown CM, Horwitz AR, Mantulin WW, Gratton E. Paxillin dynamics measured during adhesion assembly and disassembly by correlation spectroscopy. Biophys J 2008; 94:2819-31.
    • (2008) Biophys J , vol.94 , pp. 2819-2831
    • Digman, M.A.1    Brown, C.M.2    Horwitz, A.R.3    Mantulin, W.W.4    Gratton, E.5
  • 54
    • 44049105523 scopus 로고    scopus 로고
    • Mapping the number of molecules and brightness in the laser scanning microscope
    • Digman MA, Dalal R, Horwitz AF, Gratton E. Mapping the number of molecules and brightness in the laser scanning microscope. Biophys J 2008; 94:2320-32.
    • (2008) Biophys J , vol.94 , pp. 2320-2332
    • Digman, M.A.1    Dalal, R.2    Horwitz, A.F.3    Gratton, E.4
  • 56
    • 29244433026 scopus 로고    scopus 로고
    • Analyzing focal adhesion structure by atomic force microscopy
    • Franz CM, Muller DJ. Analyzing focal adhesion structure by atomic force microscopy. J Cell Sci 2005; 118:5315-23.
    • (2005) J Cell Sci , vol.118 , pp. 5315-5323
    • Franz, C.M.1    Muller, D.J.2
  • 57
    • 77950594066 scopus 로고    scopus 로고
    • I-BAR domains IRSp53 and filopodium formation Semin
    • Ahmed S, Goh WI, Bu W. I-BAR domains, IRSp53 and filopodium formation Semin. Cell Dev Biol 2010; 21:350-6.
    • (2010) Cell Dev Biol , vol.21 , pp. 350-356
    • Ahmed, S.1    Goh, W.I.2    Bu, W.3
  • 58
    • 33646763140 scopus 로고    scopus 로고
    • Optimization of WAVE2 complexinduced actin polymerization by membrane-bound IRSp53 PIP(3) and Rac
    • Suetsugu S, Kurisu S, Oikawa T, Yamazaki D, Oda A, Takenawa T. Optimization of WAVE2 complexinduced actin polymerization by membrane-bound IRSp53, PIP(3) and Rac. J Cell Biol 2006; 173:571-85.
    • (2006) J Cell Biol , vol.173 , pp. 571-585
    • Suetsugu, S.1    Kurisu, S.2    Oikawa, T.3    Yamazaki, D.4    Oda, A.5    Takenawa, T.6
  • 59
    • 50649084583 scopus 로고    scopus 로고
    • The Cdc42 effector IRSp53 generates filopodia by coupling membrane protrusion with actin dynamics
    • Lim KB, Bu W, Goh WI, Koh E, Ong SH, Pawson T, et al. The Cdc42 effector IRSp53 generates filopodia by coupling membrane protrusion with actin dynamics. J Biol Chem 2008; 283:20454-72.
    • (2008) J Biol Chem , vol.283 , pp. 20454-20472
    • Lim, K.B.1    Bu, W.2    Goh, W.I.3    Koh, E.4    Ong, S.H.5    Pawson, T.6
  • 60
    • 77957916873 scopus 로고    scopus 로고
    • Cdc42 interaction with N-WASP and Toca-1 regulates membrane tubulation, vesicle formation and vesicle motility: implications for endocytosis
    • Bu W, Lim KB, Yu YH, Chou AM, Sudhaharan T, Ahmed S. Cdc42 interaction with N-WASP and Toca-1 regulates membrane tubulation, vesicle formation and vesicle motility: implications for endocytosis. PLoS One 2010; 5:12153.
    • (2010) PLoS One , vol.5 , pp. 12153
    • Bu, W.1    Lim, K.B.2    Yu, Y.H.3    Chou, A.M.4    Sudhaharan, T.5    Ahmed, S.6
  • 61
    • 66449088020 scopus 로고    scopus 로고
    • The Toca-1-N-WASP complex links filopodial formation to endocytosis
    • Bu W, Chou AM, Lim KB, Sudhaharan T, Ahmed S. The Toca-1-N-WASP complex links filopodial formation to endocytosis. J Biol Chem 2009; 284:11622-36.
    • (2009) J Biol Chem , vol.284 , pp. 11622-11636
    • Bu, W.1    Chou, A.M.2    Lim, K.B.3    Sudhaharan, T.4    Ahmed, S.5
  • 63
    • 4043115604 scopus 로고    scopus 로고
    • Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end
    • Mejillano MR, Kojima S, Applewhite DA, Gertler FB, Svitkina TM, Borisy GG. Lamellipodial versus filopodial mode of the actin nanomachinery: pivotal role of the filament barbed end. Cell 2004; 118:363-73.
    • (2004) Cell , vol.118 , pp. 363-373
    • Mejillano, M.R.1    Kojima, S.2    Applewhite, D.A.3    Gertler, F.B.4    Svitkina, T.M.5    Borisy, G.G.6
  • 64
    • 62649117848 scopus 로고    scopus 로고
    • Impact of actin rearrangement and degranulation on the membrane structure of primary mast cells: a combined atomic force and laser scanning confocal microscopy investigation
    • Deng Z, Zink T, Chen HY, Walters D, Liu FT, Liu GY. Impact of actin rearrangement and degranulation on the membrane structure of primary mast cells: a combined atomic force and laser scanning confocal microscopy investigation. Biophys J 2009; 96:1629-39.
    • (2009) Biophys J , vol.96 , pp. 1629-1639
    • Deng, Z.1    Zink, T.2    Chen, H.Y.3    Walters, D.4    Liu, F.T.5    Liu, G.Y.6
  • 65
    • 77952171377 scopus 로고    scopus 로고
    • Applications of atomic force microscopy in biophysical chemistry of cells
    • Deng Z, Lulevich V, Liu FT, Liu GY. Applications of atomic force microscopy in biophysical chemistry of cells. J Phys Chem B 2010; 114:5971-82.
    • (2010) J Phys Chem B , vol.114 , pp. 5971-5982
    • Deng, Z.1    Lulevich, V.2    Liu, F.T.3    Liu, G.Y.4
  • 66
    • 78149285270 scopus 로고    scopus 로고
    • Video imaging of walking myosin V by high-speed atomic force microscopy
    • Kodera N, Yamamoto D, Ishikawa R, Ando T. Video imaging of walking myosin V by high-speed atomic force microscopy. Nature 2010; 468:72-6.
    • (2010) Nature , vol.468 , pp. 72-76
    • Kodera, N.1    Yamamoto, D.2    Ishikawa, R.3    Ando, T.4
  • 67
    • 61849101492 scopus 로고    scopus 로고
    • Putting enterohemorrhagic E. coli on a pedestal
    • Yi CR, Goldberg MB. Putting enterohemorrhagic E. coli on a pedestal. Cell Host Microbe 2009; 5:215-7.
    • (2009) Cell Host Microbe , vol.5 , pp. 215-217
    • Yi, C.R.1    Goldberg, M.B.2
  • 68
    • 43049126506 scopus 로고    scopus 로고
    • Invadopodia
    • Weaver AM. Invadopodia. Curr Biol 2008; 18:362-4.
    • (2008) Curr Biol , vol.18 , pp. 362-364
    • Weaver, A.M.1
  • 69
    • 78449267306 scopus 로고    scopus 로고
    • Cdc42-interacting protein 4 promotes breast cancer cell invasion and formation of invadopodia through activation of N-WASp
    • Pichot CS, Arvanitis C, Hartig SM, Jensen SA, Bechill J, Marzouk S, et al. Cdc42-interacting protein 4 promotes breast cancer cell invasion and formation of invadopodia through activation of N-WASp. Cancer Res 2010; 70:8347-562.
    • (2010) Cancer Res , vol.70 , pp. 8347-8562
    • Pichot, C.S.1    Arvanitis, C.2    Hartig, S.M.3    Jensen, S.A.4    Bechill, J.5    Marzouk, S.6
  • 70
    • 77049108859 scopus 로고    scopus 로고
    • The actin-bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion
    • Li A, Dawson JC, Forero-Vargas M, Spence HJ, Yu X, Konig I, et al. The actin-bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion. Curr Biol 2010; 20:339-45.
    • (2010) Curr Biol , vol.20 , pp. 339-345
    • Li, A.1    Dawson, J.C.2    Forero-Vargas, M.3    Spence, H.J.4    Yu, X.5    Konig, I.6
  • 71
    • 77951771838 scopus 로고    scopus 로고
    • Actin, microtubules and vimentin intermediate filaments cooperate for elongation of invadopodia
    • Schoumacher M, Goldman RD, Louvard D, Vignjevic DM. Actin, microtubules and vimentin intermediate filaments cooperate for elongation of invadopodia. J Cell Biol 2010; 189:541-56.
    • (2010) J Cell Biol , vol.189 , pp. 541-556
    • Schoumacher, M.1    Goldman, R.D.2    Louvard, D.3    Vignjevic, D.M.4
  • 72
    • 79956208360 scopus 로고    scopus 로고
    • Fascin: Invasive filopodia promoting metastasis
    • Machesky LM, Li A. Fascin: Invasive filopodia promoting metastasis. Commun Integr Biol 2010; 3:263-70.
    • (2010) Commun Integr Biol , vol.3 , pp. 263-270
    • Machesky, L.M.1    Li, A.2


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