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Volumn 90, Issue 6, 2006, Pages 1878-1894

Dissecting the contribution of diffusion and interactions to the mobility of nuclear proteins

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; NUCLEAR PROTEIN;

EID: 33645969033     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.105.071241     Document Type: Article
Times cited : (151)

References (60)
  • 2
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R. D., and T. Misteli. 2000. High mobility of proteins in the mammalian cell nucleus. Nature. 404:604-609.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 3
    • 0034649663 scopus 로고    scopus 로고
    • Dynamic binding of histone H1 to chromatin in living cells
    • Misteli, T., A. Gunjan, R. Hock, M. Bustin, and D. T. Brown. 2000. Dynamic binding of histone H1 to chromatin in living cells. Nature. 408:877-881.
    • (2000) Nature , vol.408 , pp. 877-881
    • Misteli, T.1    Gunjan, A.2    Hock, R.3    Bustin, M.4    Brown, D.T.5
  • 4
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: Rapid exchange with regulatory sites in living cells
    • McNally, J. G., W. G. Muller, D. Walker, R. Wolford, and G. L. Hager. 2000. The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science. 287:1262-1265.
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Muller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 5
    • 2142823918 scopus 로고    scopus 로고
    • On the movements of nuclear components in living cells
    • Bubulya, P. A., and D. L. Spector. 2004. On the movements of nuclear components in living cells. Exp. Cell Res. 296:4-11.
    • (2004) Exp. Cell Res. , vol.296 , pp. 4-11
    • Bubulya, P.A.1    Spector, D.L.2
  • 6
    • 3042760021 scopus 로고    scopus 로고
    • Global nature of dynamic protein-chromatin interactions in vivo: Three-dimensional genome scanning and dynamic interaction networks of chromatin proteins
    • Phair, R. D., P. Scaffidi, C. Elbi, J. Vecerova, A. Dey, K. Ozato, D. T. Brown, G. Hager, M. Bustin, and T. Misteli. 2004. Global nature of dynamic protein-chromatin interactions in vivo: three-dimensional genome scanning and dynamic interaction networks of chromatin proteins. Mol. Cell. Biol. 24:6393-6402.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6393-6402
    • Phair, R.D.1    Scaffidi, P.2    Elbi, C.3    Vecerova, J.4    Dey, A.5    Ozato, K.6    Brown, D.T.7    Hager, G.8    Bustin, M.9    Misteli, T.10
  • 7
    • 0038022717 scopus 로고    scopus 로고
    • Dynamics of chromatin, proteins, and bodies within the cell nucleus
    • Belmont, A. 2003. Dynamics of chromatin, proteins, and bodies within the cell nucleus. Curr. Opin. Cell Biol. 15:304-310.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 304-310
    • Belmont, A.1
  • 8
    • 0036532111 scopus 로고    scopus 로고
    • Protein dynamics in the nuclear compartment
    • Hager, G. L., C. Elbi, and M. Becker. 2002. Protein dynamics in the nuclear compartment. Curr. Opin. Genet. Dev. 12:137-141.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 137-141
    • Hager, G.L.1    Elbi, C.2    Becker, M.3
  • 9
    • 0035654399 scopus 로고    scopus 로고
    • Kinetic modelling approaches to in vivo imaging
    • Phair, R. D., and T. Misteli. 2001. Kinetic modelling approaches to in vivo imaging. Nat. Rev. Mol. Cell Biol. 2:898-907.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 898-907
    • Phair, R.D.1    Misteli, T.2
  • 11
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson, G. H., and J. Lippincott-Schwartz. 2002. A photoactivatable GFP for selective photolabeling of proteins and cells. Science. 297:1873-1877.
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 12
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod, D., D. E. Koppel, J. Schlessinger, E. Elson, and W. W. Webb. 1976. Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys. J. 16:1055-1069.
    • (1976) Biophys. J. , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Schlessinger, J.3    Elson, E.4    Webb, W.W.5
  • 13
    • 0025145492 scopus 로고
    • Quantification of transport and binding parameters using fluorescence recovery after photobleaching. Potential for in vivo applications
    • Kaufman, E. N., and R. K. Jain. 1990. Quantification of transport and binding parameters using fluorescence recovery after photobleaching. Potential for in vivo applications. Biophys. J. 58:873-885.
    • (1990) Biophys. J. , vol.58 , pp. 873-885
    • Kaufman, E.N.1    Jain, R.K.2
  • 14
    • 0027146418 scopus 로고
    • Fluorescence photobleaching with spatial Fourier analysis: Measurement of diffusion in light-scattering media
    • Berk, D. A., F. Yuan, M. Leunig, and R. K. Jain. 1993. Fluorescence photobleaching with spatial Fourier analysis: measurement of diffusion in light-scattering media. Biophys. J. 65:2428-2436.
    • (1993) Biophys. J. , vol.65 , pp. 2428-2436
    • Berk, D.A.1    Yuan, F.2    Leunig, M.3    Jain, R.K.4
  • 15
    • 0025833584 scopus 로고
    • Spatial Fourier analysis of video photobleaching measurements. Principles and optimization
    • Tsay, T. T., and K. A. Jacobson. 1991. Spatial Fourier analysis of video photobleaching measurements. Principles and optimization. Biophys. J. 60:360-368.
    • (1991) Biophys. J. , vol.60 , pp. 360-368
    • Tsay, T.T.1    Jacobson, K.A.2
  • 16
    • 0028861944 scopus 로고
    • Interpreting photoactivated fluorescence microscopy measurements of steady-state actin dynamics
    • Tardy, Y., J. L. McGrath, J. H. Hartwig, and C. F. Dewey. 1995. Interpreting photoactivated fluorescence microscopy measurements of steady-state actin dynamics. Biophys. J. 69:1674-1682.
    • (1995) Biophys. J. , vol.69 , pp. 1674-1682
    • Tardy, Y.1    McGrath, J.L.2    Hartwig, J.H.3    Dewey, C.F.4
  • 18
    • 2942690158 scopus 로고    scopus 로고
    • Analysis of binding reactions by fluorescence recovery after photobleaching
    • Sprague, B. L., R. L. Pego, D. A. Stavreva, and J. G. McNally. 2004. Analysis of binding reactions by fluorescence recovery after photobleaching. Biophys. J. 86:3473-3495.
    • (2004) Biophys. J. , vol.86 , pp. 3473-3495
    • Sprague, B.L.1    Pego, R.L.2    Stavreva, D.A.3    McNally, J.G.4
  • 22
    • 7944236264 scopus 로고    scopus 로고
    • Mapping the dynamic organization of the nuclear pore complex inside single living cells
    • Rabut, G., V. Doye, and J. Ellenberg. 2004. Mapping the dynamic organization of the nuclear pore complex inside single living cells. Nat. Cell Biol. 6:1114-1121.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1114-1121
    • Rabut, G.1    Doye, V.2    Ellenberg, J.3
  • 23
    • 1642377367 scopus 로고    scopus 로고
    • Measurement of dynamic protein binding to chromatin in vivo, using photobleaching microscopy
    • Phair, R. D., S. A. Gorski, and T. Misteli. 2004. Measurement of dynamic protein binding to chromatin in vivo, using photobleaching microscopy. Methods Enzymol. 375:393-414.
    • (2004) Methods Enzymol. , vol.375 , pp. 393-414
    • Phair, R.D.1    Gorski, S.A.2    Misteli, T.3
  • 24
    • 0035947299 scopus 로고    scopus 로고
    • Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B
    • Nemergut, M. E., C. A. Mizzen, T. Stukenberg, C. D. Allis, and I. G. Macara. 2001. Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B. Science. 292:1540-1543.
    • (2001) Science , vol.292 , pp. 1540-1543
    • Nemergut, M.E.1    Mizzen, C.A.2    Stukenberg, T.3    Allis, C.D.4    Macara, I.G.5
  • 26
    • 0041886608 scopus 로고    scopus 로고
    • Histone H1 and the dynamic regulation of chromatin function
    • Brown, D. T. 2003. Histone H1 and the dynamic regulation of chromatin function. Biochem. Cell Biol. 81:221-227.
    • (2003) Biochem. Cell Biol. , vol.81 , pp. 221-227
    • Brown, D.T.1
  • 27
    • 0345039879 scopus 로고    scopus 로고
    • Global chromosome positions are transmitted through mitosis in mammalian cells
    • Gerlich, D., J. Beaudouin, B. Kalbfuss, N. Daigle, R. Eils, and J. Ellenberg. 2003. Global chromosome positions are transmitted through mitosis in mammalian cells. Cell. 112:751-764.
    • (2003) Cell , vol.112 , pp. 751-764
    • Gerlich, D.1    Beaudouin, J.2    Kalbfuss, B.3    Daigle, N.4    Eils, R.5    Ellenberg, J.6
  • 28
    • 0034925739 scopus 로고    scopus 로고
    • Evaluation of retroviral vector design in defined chromosomal loci by FLP-mediated cassette replacement
    • Verhoeyen, E., H. Hauser, and D. Wirth. 2001. Evaluation of retroviral vector design in defined chromosomal loci by FLP-mediated cassette replacement. Hum. Gene Ther. 12:933-944.
    • (2001) Hum. Gene Ther. , vol.12 , pp. 933-944
    • Verhoeyen, E.1    Hauser, H.2    Wirth, D.3
  • 29
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasome-mediated turnover of unliganded and liganded ER-α on responsive promoters is an integral feature of estrogen signaling
    • Reid, G., M. Hübner, R. Métivier, H. Brand, S. Denger, D. Manu, J. Beaudouin, J. Ellenberg, and F. Gannon. 2003. Cyclic, proteasome-mediated turnover of unliganded and liganded ER-α on responsive promoters is an integral feature of estrogen signaling. Mol. Cell. 11:695-707.
    • (2003) Mol. Cell. , vol.11 , pp. 695-707
    • Reid, G.1    Hübner, M.2    Métivier, R.3    Brand, H.4    Denger, S.5    Manu, D.6    Beaudouin, J.7    Ellenberg, J.8    Gannon, F.9
  • 30
    • 0034852706 scopus 로고    scopus 로고
    • Four-dimensional imaging and quantitative reconstruction to analyse complex spatiotemporal processes in live cells
    • Gerlich, D., J. Beaudouin, M. Gebhard, J. Ellenberg, and R. Eils. 2001. Four-dimensional imaging and quantitative reconstruction to analyse complex spatiotemporal processes in live cells. Nat. Cell Biol. 3:852-855.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 852-855
    • Gerlich, D.1    Beaudouin, J.2    Gebhard, M.3    Ellenberg, J.4    Eils, R.5
  • 31
    • 7944224713 scopus 로고    scopus 로고
    • Automatic real-time three-dimensional cell tracking by fluorescence microscopy
    • Rabut, G., and J. Ellenberg. 2004. Automatic real-time three-dimensional cell tracking by fluorescence microscopy. J. Microsc. 216(Pt2):131-137.
    • (2004) J. Microsc. , vol.216 , Issue.2 PART , pp. 131-137
    • Rabut, G.1    Ellenberg, J.2
  • 33
    • 0035954427 scopus 로고    scopus 로고
    • Kinetics of core histones in living human cells: Little exchange of H3 and H4 and some rapid exchange of H2B
    • Kimura, H., and P. R. Cook. 2001. Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B. J. Cell Biol. 153:1341-1353.
    • (2001) J. Cell Biol. , vol.153 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 34
    • 0036006293 scopus 로고    scopus 로고
    • Chromatin motion is constrained by association with nuclear compartments in human cells
    • Chubb, J. R., S. Boyle, P. Perry, and W. A. Bickmore. 2002. Chromatin motion is constrained by association with nuclear compartments in human cells. Curr. Biol. 12:439-445.
    • (2002) Curr. Biol. , vol.12 , pp. 439-445
    • Chubb, J.R.1    Boyle, S.2    Perry, P.3    Bickmore, W.A.4
  • 35
    • 0031009827 scopus 로고    scopus 로고
    • Chromatin dynamics in interphase nuclei and its implications for nuclear structure
    • Abney, J. R., B. Cutler, M. L. Fillbach, D. Axelrod, and B. A. Scalettar. 1997. Chromatin dynamics in interphase nuclei and its implications for nuclear structure. J. Cell Biol. 137:1459-1468.
    • (1997) J. Cell Biol. , vol.137 , pp. 1459-1468
    • Abney, J.R.1    Cutler, B.2    Fillbach, M.L.3    Axelrod, D.4    Scalettar, B.A.5
  • 36
    • 0037285568 scopus 로고    scopus 로고
    • Quantitative motion analysis and visualization of cellular structures
    • Gerlich, D., J. Mattes, and R. Eils. 2003. Quantitative motion analysis and visualization of cellular structures. Methods. 29:3-13.
    • (2003) Methods , vol.29 , pp. 3-13
    • Gerlich, D.1    Mattes, J.2    Eils, R.3
  • 37
    • 0031689215 scopus 로고    scopus 로고
    • Intracellular fluorescent probe concentrations by confocal microscopy
    • Fink, C., F. Morgan, and L. M. Loew. 1998. Intracellular fluorescent probe concentrations by confocal microscopy. Biophys. J. 75:1648-1658.
    • (1998) Biophys. J. , vol.75 , pp. 1648-1658
    • Fink, C.1    Morgan, F.2    Loew, L.M.3
  • 38
    • 0141530988 scopus 로고    scopus 로고
    • Three-dimensional fluorescence recovery after photobleaching with the confocal scanning laser microscope
    • Braeckmans, K., L. Peeters, N. N. Sanders, S. C. De Smedt, and J. Demeester. 2003. Three-dimensional fluorescence recovery after photobleaching with the confocal scanning laser microscope. Biophys. J. 85:2240-2252.
    • (2003) Biophys. J. , vol.85 , pp. 2240-2252
    • Braeckmans, K.1    Peeters, L.2    Sanders, N.N.3    De Smedt, S.C.4    Demeester, J.5
  • 39
    • 0033807598 scopus 로고    scopus 로고
    • Diffusion in inhomogeneous media: Theory and simulations applied to whole cell photobleach recovery
    • Siggia, E. D., J. Lippincott-Schwartz, and S. Bekiranov. 2000. Diffusion in inhomogeneous media: theory and simulations applied to whole cell photobleach recovery. Biophys. J. 79:1761-1770.
    • (2000) Biophys. J. , vol.79 , pp. 1761-1770
    • Siggia, E.D.1    Lippincott-Schwartz, J.2    Bekiranov, S.3
  • 40
    • 0031000601 scopus 로고    scopus 로고
    • Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: Cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion
    • Swaminathan, R., C. P. Hoang, and A. S. Verkman. 1997. Photobleaching recovery and anisotropy decay of green fluorescent protein GFP-S65T in solution and cells: cytoplasmic viscosity probed by green fluorescent protein translational and rotational diffusion. Biophys. J. 72:1900-1907.
    • (1997) Biophys. J. , vol.72 , pp. 1900-1907
    • Swaminathan, R.1    Hoang, C.P.2    Verkman, A.S.3
  • 41
    • 0029558909 scopus 로고
    • Molecular characterisation of recombinant green fluorescent protein by fluorescence correlation microscopy
    • Terry, B. R., E. K. Matthews, and J. Haseloff. 1995. Molecular characterisation of recombinant green fluorescent protein by fluorescence correlation microscopy. Biochem. Biophys. Res. Commun. 217:21-27.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 21-27
    • Terry, B.R.1    Matthews, E.K.2    Haseloff, J.3
  • 43
    • 0030742748 scopus 로고    scopus 로고
    • Translational diffusion of macromolecule-sized solutes in cytoplasm and nucleus
    • Seksek, O., J. Biwersi, and A. S. Verkman. 1997. Translational diffusion of macromolecule-sized solutes in cytoplasm and nucleus. J. Cell Biol. 138:131-142.
    • (1997) J. Cell Biol. , vol.138 , pp. 131-142
    • Seksek, O.1    Biwersi, J.2    Verkman, A.S.3
  • 44
    • 0034640133 scopus 로고    scopus 로고
    • Anomalous diffusion of fluorescent probes inside living cell nuclei investigated by spatially resolved fluorescence correlation spectroscopy
    • Wachsmuth, M., W. Waldeck, and J. Langowski. 2000. Anomalous diffusion of fluorescent probes inside living cell nuclei investigated by spatially resolved fluorescence correlation spectroscopy. J. Mol. Biol. 298:677-689.
    • (2000) J. Mol. Biol. , vol.298 , pp. 677-689
    • Wachsmuth, M.1    Waldeck, W.2    Langowski, J.3
  • 47
    • 0347990552 scopus 로고    scopus 로고
    • The dynamic association of RCC1 with chromatin is modulated by RAN-dependent nuclear transport
    • Cushman, I., D. Stenoien, and M. S. Moore. 2004. The dynamic association of RCC1 with chromatin is modulated by RAN-dependent nuclear transport. Mol. Biol. Cell. 15:245-255.
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 245-255
    • Cushman, I.1    Stenoien, D.2    Moore, M.S.3
  • 48
    • 0037416202 scopus 로고    scopus 로고
    • A mechanism of coupling RCC1 mobility to RanGTP production on the chromatin in vivo
    • Li, H. Y., D. Wirtz, and Y. Zheng. 2003. A mechanism of coupling RCC1 mobility to RanGTP production on the chromatin in vivo. J. Cell Biol. 160:635-644.
    • (2003) J. Cell Biol. , vol.160 , pp. 635-644
    • Li, H.Y.1    Wirtz, D.2    Zheng, Y.3
  • 50
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner, M., D. O'Carroll, S. Rea, K. Mechtler, and T. Jenuwein. 2001. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature. 410:116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 51
    • 0034649621 scopus 로고    scopus 로고
    • Rapid exchange of histone H1.1 on chromatin in living human cells
    • Lever, M. A., J. P. Th'ng, X. Sun, and M. J. Hendzel. 2000. Rapid exchange of histone H1.1 on chromatin in living human cells. Nature. 408:873-876.
    • (2000) Nature , vol.408 , pp. 873-876
    • Lever, M.A.1    Th'ng, J.P.2    Sun, X.3    Hendzel, M.J.4
  • 52
    • 0020568317 scopus 로고
    • Theoretical analysis of fluorescence photobleaching recovery experiments
    • Soumpasis, D. M. 1983. Theoretical analysis of fluorescence photobleaching recovery experiments. Biophys. J. 41:95-97.
    • (1983) Biophys. J. , vol.41 , pp. 95-97
    • Soumpasis, D.M.1
  • 53
    • 2942596544 scopus 로고    scopus 로고
    • Network of dynamic interactions between histone H1 and high-mobility-group proteins in chromatin
    • Catez, F., H. Yang, K. J. Tracey, R. Reeves, T. Misteli, and M. Bustin. 2004. Network of dynamic interactions between histone H1 and high-mobility-group proteins in chromatin. Mol. Cell. Biol. 24:4321-4328.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4321-4328
    • Catez, F.1    Yang, H.2    Tracey, K.J.3    Reeves, R.4    Misteli, T.5    Bustin, M.6
  • 56
    • 0029790690 scopus 로고    scopus 로고
    • Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: Structural transitions and transcriptional repression
    • Ura, K., K. Nightingale, and A. P. Wolffe. 1996. Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: structural transitions and transcriptional repression. EMBO J. 15:4959-4969.
    • (1996) EMBO J. , vol.15 , pp. 4959-4969
    • Ura, K.1    Nightingale, K.2    Wolffe, A.P.3
  • 57
    • 0014945567 scopus 로고
    • The lac repressoroperator interaction. 3. Kinetic studies
    • Riggs, A. D., S. Bourgeois, and M. Cohn. 1970. The lac repressoroperator interaction. 3. Kinetic studies. J. Mol. Biol. 53:401-417.
    • (1970) J. Mol. Biol. , vol.53 , pp. 401-417
    • Riggs, A.D.1    Bourgeois, S.2    Cohn, M.3
  • 58
    • 3042579602 scopus 로고    scopus 로고
    • How do site-specific DNAbinding proteins find their targets?
    • Halford, S. E., and J. F. Marko. 2004. How do site-specific DNAbinding proteins find their targets? Nucleic Acids Res. 32:3040-3052.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3040-3052
    • Halford, S.E.1    Marko, J.F.2
  • 59
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • von Hippel, P. H., and O. G. Berg. 1989. Facilitated target location in biological systems. J. Biol. Chem. 264:675-678.
    • (1989) J. Biol. Chem. , vol.264 , pp. 675-678
    • Von Hippel, P.H.1    Berg, O.G.2
  • 60
    • 0035793376 scopus 로고    scopus 로고
    • Protein dynamics: Implications for nuclear architecture and gene expression
    • Misteli, T. 2001. Protein dynamics: implications for nuclear architecture and gene expression. Science. 291:843-847.
    • (2001) Science , vol.291 , pp. 843-847
    • Misteli, T.1


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