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Volumn 287, Issue 4, 1999, Pages 741-752

Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy

Author keywords

Nuclear calcium signalling; Nuclear pore complex; Nucleocytoplasmic transport; Time lapse atomic force microscopy; Transmission electron cryomicroscopy

Indexed keywords

ADENOSINE TRIPHOSPHATE; BUFFER; CALCIUM ION; ION;

EID: 0033537992     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2637     Document Type: Article
Times cited : (136)

References (52)
  • 1
    • 0023419545 scopus 로고
    • A glow discharge unit to render electron microscopy grids and other surfaces hydrophilic
    • Aebi U., Pollard T. D. A glow discharge unit to render electron microscopy grids and other surfaces hydrophilic. J. Electron Microsc. Tech. 7:1987;29-33.
    • (1987) J. Electron Microsc. Tech. , vol.7 , pp. 29-33
    • Aebi, U.1    Pollard, T.D.2
  • 2
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi U., Cohn J., Buhle E. L., Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature. 323:1986;560-564.
    • (1986) Nature , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, E.L.3    Gerace, L.4
  • 3
    • 0024417594 scopus 로고
    • Interactions and structure of the nuclear pore complex revealed by cryo-electron microscopy
    • Akey C. W. Interactions and structure of the nuclear pore complex revealed by cryo-electron microscopy. J. Cell Biol. 109:1989;955-970.
    • (1989) J. Cell Biol. , vol.109 , pp. 955-970
    • Akey, C.W.1
  • 4
    • 0029021928 scopus 로고
    • Structural plasticity of the nuclear pore complex
    • Akey C. W. Structural plasticity of the nuclear pore complex. J. Mol. Biol. 248:1995;273-293.
    • (1995) J. Mol. Biol. , vol.248 , pp. 273-293
    • Akey, C.W.1
  • 5
    • 0027287349 scopus 로고
    • Architecture of the Xenopus nuclear pore complex revealed by 3-dimensional cryo-electron microscopy
    • Akey C. W., Radermacher M. Architecture of the Xenopus nuclear pore complex revealed by 3-dimensional cryo-electron microscopy. J. Cell Biol. 122:1993;1-19.
    • (1993) J. Cell Biol. , vol.122 , pp. 1-19
    • Akey, C.W.1    Radermacher, M.2
  • 6
    • 0029743063 scopus 로고    scopus 로고
    • Targeting and function in mRNA export of nuclear pore complex protein NUP153
    • Bastos R., Lin A., Enarson M., Burke B. Targeting and function in mRNA export of nuclear pore complex protein NUP153. J. Cell Biol. 134:1996;1141-1156.
    • (1996) J. Cell Biol. , vol.134 , pp. 1141-1156
    • Bastos, R.1    Lin, A.2    Enarson, M.3    Burke, B.4
  • 7
    • 0028315910 scopus 로고
    • Structure and activation dynamics of RBL-2H3 cells observed with scanning force microscopy
    • Braunstein D., Spudich A. Structure and activation dynamics of RBL-2H3 cells observed with scanning force microscopy. Biophys. J. 66:1994;1717-1725.
    • (1994) Biophys. J. , vol.66 , pp. 1717-1725
    • Braunstein, D.1    Spudich, A.2
  • 9
    • 0030951962 scopus 로고    scopus 로고
    • High resolution imaging of native biological sample surfaces using scanning probe microscopy
    • Engel A., Schoenenberger C. A., Müller D. J. High resolution imaging of native biological sample surfaces using scanning probe microscopy. Curr. Opin. Struct. Biol. 7:1997;279-284.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 279-284
    • Engel, A.1    Schoenenberger, C.A.2    Müller, D.J.3
  • 10
    • 0032476576 scopus 로고    scopus 로고
    • Molecular architecture of the yeast nuclear pore complex: Localization of Nsp1p subcomplexes
    • Fahrenkrog B., Hurt E. C., Aebi U., Panté N. Molecular architecture of the yeast nuclear pore complex: localization of Nsp1p subcomplexes. J. Cell Biol. 143:1998;577-588.
    • (1998) J. Cell Biol. , vol.143 , pp. 577-588
    • Fahrenkrog, B.1    Hurt, E.C.2    Aebi, U.3    Panté, N.4
  • 11
    • 0029786355 scopus 로고    scopus 로고
    • Aldosterone activates the nuclear pore transporter in cultured kidney cells imaged with atomic force microscopy
    • Folprecht G., Schneider S., Oberleithner H. Aldosterone activates the nuclear pore transporter in cultured kidney cells imaged with atomic force microscopy. Pflügers Arch. Eur. J. Physiol. 432:1996;831-838.
    • (1996) Pflügers Arch. Eur. J. Physiol. , vol.432 , pp. 831-838
    • Folprecht, G.1    Schneider, S.2    Oberleithner, H.3
  • 12
    • 0029869424 scopus 로고    scopus 로고
    • The nuclear pore complex and lamina: Three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy
    • Goldberg M. W., Allen. The nuclear pore complex and lamina: three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy. J. Mol. Biol. 257:1996;848-865.
    • (1996) J. Mol. Biol. , vol.257 , pp. 848-865
    • Goldberg, M.W.1    Allen2
  • 13
    • 0031056904 scopus 로고    scopus 로고
    • Dimples, pores, starrings, and thin rings on growing nuclear envelopes: Evidence for structural intermediates in nuclear pore complex assembly
    • Goldberg M. W., Wiese C., Allen T. D., Wilson K. L. Dimples, pores, starrings, and thin rings on growing nuclear envelopes: evidence for structural intermediates in nuclear pore complex assembly. J. Cell Sci. 110:1997;409-420.
    • (1997) J. Cell Sci. , vol.110 , pp. 409-420
    • Goldberg, M.W.1    Wiese, C.2    Allen, T.D.3    Wilson, K.L.4
  • 14
    • 0000473509 scopus 로고
    • Exploring native nuclear pore complex structure and conformation by scanning force microscopy in physiological buffers
    • Goldie K. N., Panté N., Engel A., Aebi U. Exploring native nuclear pore complex structure and conformation by scanning force microscopy in physiological buffers. J. Vac. Sci. Technol. ser. B. 12:1994;1482-1485.
    • (1994) J. Vac. Sci. Technol. Ser. B , vol.12 , pp. 1482-1485
    • Goldie, K.N.1    Panté, N.2    Engel, A.3    Aebi, U.4
  • 16
    • 0030824317 scopus 로고    scopus 로고
    • Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly
    • Grandi P., Dang T., Panté N., Schevchenko A., Mann M., Forbes D., Hurt E. C. Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly. Mol. Biol. Cell. 8:1997;2017-2038.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2017-2038
    • Grandi, P.1    Dang, T.2    Panté, N.3    Schevchenko, A.4    Mann, M.5    Forbes, D.6    Hurt, E.C.7
  • 17
    • 0028851245 scopus 로고
    • Depletion of calcium from the lumen of endoplasmic reticulum reversibly inhibits passive diffusion and signal-mediated transport into the nucleus
    • Greber U. F., Gerace L. Depletion of calcium from the lumen of endoplasmic reticulum reversibly inhibits passive diffusion and signal-mediated transport into the nucleus. J. Cell Biol. 128:1995;5-14.
    • (1995) J. Cell Biol. , vol.128 , pp. 5-14
    • Greber, U.F.1    Gerace, L.2
  • 18
    • 0026776959 scopus 로고
    • Architecture and design of the nuclear pore complex
    • Hinshaw S. E., Carragher B. O., Milligan R. A. Architecture and design of the nuclear pore complex. Cell. 69:1992;1133-1141.
    • (1992) Cell , vol.69 , pp. 1133-1141
    • Hinshaw, S.E.1    Carragher, B.O.2    Milligan, R.A.3
  • 19
    • 0026323478 scopus 로고
    • Towards a 3-D model of the nuclear pore complex
    • Jarnik M., Aebi U. Towards a 3-D model of the nuclear pore complex. J. Struct. Biol. 107:1991;291-308.
    • (1991) J. Struct. Biol. , vol.107 , pp. 291-308
    • Jarnik, M.1    Aebi, U.2
  • 20
    • 0028957621 scopus 로고
    • Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy
    • Müller D. L., Schabert F. A., Büldt G., Engel A. Imaging purple membranes in aqueous solutions at sub-nanometer resolution by atomic force microscopy. Biophys. J. 68:1995a;1681-1686.
    • (1995) Biophys. J. , vol.68 , pp. 1681-1686
    • Müller, D.L.1    Schabert, F.A.2    Büldt, G.3    Engel, A.4
  • 21
    • 0028998339 scopus 로고
    • Force-induced conformational change of bacteriorhodopsin
    • Müller D. J., Büldt G., Engel A. Force-induced conformational change of bacteriorhodopsin. J. Mol. Biol. 249:1995b;239-243.
    • (1995) J. Mol. Biol. , vol.249 , pp. 239-243
    • Müller, D.J.1    Büldt, G.2    Engel, A.3
  • 22
    • 0030058166 scopus 로고    scopus 로고
    • Conformational change of the hexagonally packed intermediate layer imaged by atomic force microscopy
    • Müller D. L., Baumeister W., Engel A. Conformational change of the hexagonally packed intermediate layer imaged by atomic force microscopy. J. Bacteriol. 178:1996;3025-3030.
    • (1996) J. Bacteriol. , vol.178 , pp. 3025-3030
    • Müller, D.L.1    Baumeister, W.2    Engel, A.3
  • 23
    • 0031194365 scopus 로고    scopus 로고
    • Structural changes in native membrane proteins monitored at sub-nm resolution with the atomic force microscope
    • Müller D. J., Schoenenberger C. A., Schabert F., Engel A. Structural changes in native membrane proteins monitored at sub-nm resolution with the atomic force microscope. J. Struct. Biol. 119:1997a;149-157.
    • (1997) J. Struct. Biol. , vol.119 , pp. 149-157
    • Müller, D.J.1    Schoenenberger, C.A.2    Schabert, F.3    Engel, A.4
  • 24
    • 0342890045 scopus 로고    scopus 로고
    • Preparation techniques for the observation of native biological specimens with the atomic force microscope
    • Müller D. L., Engel A., Amrein M. Preparation techniques for the observation of native biological specimens with the atomic force microscope. Biosen. Bioelectr. 12:1997b;867-877.
    • (1997) Biosen. Bioelectr. , vol.12 , pp. 867-877
    • Müller, D.L.1    Engel, A.2    Amrein, M.3
  • 25
    • 0030964105 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Signals, mechanisms and regulation
    • Nigg E. Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature. 386:1997;779-787.
    • (1997) Nature , vol.386 , pp. 779-787
    • Nigg, E.1
  • 26
    • 0028029555 scopus 로고
    • Imaging nuclear pores of aldosterone-sensitive kidney cells by atomic force microscopy
    • Oberleithner H., Brinckmann E., Schwab A., Krohne G. Imaging nuclear pores of aldosterone-sensitive kidney cells by atomic force microscopy. Proc. Natl Acad. Sci. USA. 91:1994;9784-9788.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9784-9788
    • Oberleithner, H.1    Brinckmann, E.2    Schwab, A.3    Krohne, G.4
  • 27
    • 0029814364 scopus 로고    scopus 로고
    • Atomic force microscopy visualizes ATP-dependent dissociation of multimeric TATA-binding protein before translocation into the cell nucleus
    • Oberleithner H., Schneider S., Bustamante J. O. Atomic force microscopy visualizes ATP-dependent dissociation of multimeric TATA-binding protein before translocation into the cell nucleus. Pflügers Arch. Eur. J. Physiol. 432:1996;839-844.
    • (1996) Pflügers Arch. Eur. J. Physiol. , vol.432 , pp. 839-844
    • Oberleithner, H.1    Schneider, S.2    Bustamante, J.O.3
  • 28
    • 0032489013 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The last 200 nanometers
    • Ohno M., Fornerod M., Mattaj I. W. Nucleocytoplasmic transport: the last 200 nanometers. Cell. 92:1998;327-336.
    • (1998) Cell , vol.92 , pp. 327-336
    • Ohno, M.1    Fornerod, M.2    Mattaj, I.W.3
  • 29
    • 0027199147 scopus 로고
    • The nuclear pore complex
    • Panté N., Aebi U. The nuclear pore complex. J. Cell Biol. 122:1993;977-984.
    • (1993) J. Cell Biol. , vol.122 , pp. 977-984
    • Panté, N.1    Aebi, U.2
  • 30
    • 0028819808 scopus 로고
    • Exploring nuclear pore complex structure and function in molecular detail
    • Panté N., Aebi U. Exploring nuclear pore complex structure and function in molecular detail. J. Cell Sci. 19:1995;1-11.
    • (1995) J. Cell Sci. , vol.19 , pp. 1-11
    • Panté, N.1    Aebi, U.2
  • 31
    • 0029952023 scopus 로고    scopus 로고
    • Toward the molecular dissection of protein import into nuclei
    • Panté N., Aebi U. Toward the molecular dissection of protein import into nuclei. Curr. Opin. Cell Biol. 8:1996a;397-406.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 397-406
    • Panté, N.1    Aebi, U.2
  • 32
    • 0029922169 scopus 로고    scopus 로고
    • Molecular dissection of the nuclear pore complex
    • Panté N., Aebi U. Molecular dissection of the nuclear pore complex. Crit. Rev. Biochem. Mol. Biol. 31:1996b;153-199.
    • (1996) Crit. Rev. Biochem. Mol. Biol. , vol.31 , pp. 153-199
    • Panté, N.1    Aebi, U.2
  • 33
    • 0344231927 scopus 로고    scopus 로고
    • The nuclear pore complex: Toward its molecular architecture, structure and function
    • Panté N., Aebi U. The nuclear pore complex: toward its molecular architecture, structure and function. Membrane Protein Transport. 3:1996c;1-47.
    • (1996) Membrane Protein Transport , vol.3 , pp. 1-47
    • Panté, N.1    Aebi, U.2
  • 34
    • 0029797940 scopus 로고    scopus 로고
    • Sequential binding of import ligands to distinct nucleopore regions during their nuclear import
    • Panté N., Aebi U. Sequential binding of import ligands to distinct nucleopore regions during their nuclear import. Science. 273:1996d;1729-1732.
    • (1996) Science , vol.273 , pp. 1729-1732
    • Panté, N.1    Aebi, U.2
  • 35
    • 0027931054 scopus 로고
    • Interactions and 3-D localization of a group of nuclear pore complex proteins
    • Panté N., Bastos R., McMorrow I., Burke B., Aebi U. Interactions and 3-D localization of a group of nuclear pore complex proteins. J. Cell Biol. 126:1994;603-617.
    • (1994) J. Cell Biol. , vol.126 , pp. 603-617
    • Panté, N.1    Bastos, R.2    McMorrow, I.3    Burke, B.4    Aebi, U.5
  • 37
    • 0032549121 scopus 로고    scopus 로고
    • The nucleus's revolving door
    • Pennisi E. The nucleus's revolving door. Science. 279:1998;1129-1131.
    • (1998) Science , vol.279 , pp. 1129-1131
    • Pennisi, E.1
  • 39
    • 0031239585 scopus 로고    scopus 로고
    • Nuclear calcium and the regulation of the nuclear pore complex
    • Perez-Terzic C., Jaconi M., Clapham D. E. Nuclear calcium and the regulation of the nuclear pore complex. Bioassays. 19:1997;787-792.
    • (1997) Bioassays , vol.19 , pp. 787-792
    • Perez-Terzic, C.1    Jaconi, M.2    Clapham, D.E.3
  • 40
    • 0032523832 scopus 로고    scopus 로고
    • ATP-induced shape changes of nuclear pores visualized with the atomic force microscope
    • Rakowska A., Danker T., Schneider S. W., Oberleithner H. ATP-induced shape changes of nuclear pores visualized with the atomic force microscope. J. Membrane Biol. 163:1998;129-136.
    • (1998) J. Membrane Biol. , vol.163 , pp. 129-136
    • Rakowska, A.1    Danker, T.2    Schneider, S.W.3    Oberleithner, H.4
  • 41
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • Reichelt R., Holzenburg A., Buhle E. L. Jr, Jarnik M., Engel A., Aebi U. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 110:1990;883-894.
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle E.L., Jr.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 42
    • 0018650401 scopus 로고
    • Digital image processing: The semper system
    • Saxton W. O., Pitt T. J., Homer M. Digital image processing: the semper system. Ultramicroscopy. 4:1979;343-354.
    • (1979) Ultramicroscopy , vol.4 , pp. 343-354
    • Saxton, W.O.1    Pitt, T.J.2    Homer, M.3
  • 43
    • 0028020713 scopus 로고
    • Reproducible acquisition of Escherichia coli OmpF porin surfaces probed by atomic force microscopy
    • Schabert F., Engel A. Reproducible acquisition of Escherichia coli OmpF porin surfaces probed by atomic force microscopy. Biophys. J. 67:1994;2394-2403.
    • (1994) Biophys. J. , vol.67 , pp. 2394-2403
    • Schabert, F.1    Engel, A.2
  • 44
    • 0028986125 scopus 로고
    • Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy
    • Schabert F. A., Henri C., Engel A. Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy. Science. 268:1995;92-94.
    • (1995) Science , vol.268 , pp. 92-94
    • Schabert, F.A.1    Henri, C.2    Engel, A.3
  • 46
    • 0032489840 scopus 로고    scopus 로고
    • Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr
    • Shah S., Tugendreich S., Forbes D. Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr. J. Cell Biol. 141:1998;31-49.
    • (1998) J. Cell Biol. , vol.141 , pp. 31-49
    • Shah, S.1    Tugendreich, S.2    Forbes, D.3
  • 48
    • 0020472010 scopus 로고
    • A large particle associated with the perimeter of the nuclear pore complex
    • Unwin P. N. T., Milligan R. A. A large particle associated with the perimeter of the nuclear pore complex. J. Cell Biol. 93:1982;63-75.
    • (1982) J. Cell Biol. , vol.93 , pp. 63-75
    • Unwin, P.N.T.1    Milligan, R.A.2
  • 49
    • 0027406608 scopus 로고
    • New approach for atomic force microscopy of membrane proteins
    • Yang L., Tamm L. K., Tillak T. W., Shao Z. New approach for atomic force microscopy of membrane proteins. J. Mol. Biol. 229:1993;286-290.
    • (1993) J. Mol. Biol. , vol.229 , pp. 286-290
    • Yang, L.1    Tamm, L.K.2    Tillak, T.W.3    Shao, Z.4
  • 50
    • 0031604505 scopus 로고    scopus 로고
    • Three-dimensional architecture of the yeast nuclear pore complex: Functional and evolutionary implications
    • Yang Q., Rout M. P., Akey C. W. Three-dimensional architecture of the yeast nuclear pore complex: functional and evolutionary implications. Mol. Cell. 1:1998;223-234.
    • (1998) Mol. Cell , vol.1 , pp. 223-234
    • Yang, Q.1    Rout, M.P.2    Akey, C.W.3
  • 52
    • 0029900425 scopus 로고    scopus 로고
    • Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p
    • Zabel U., Doye V., Tekotte H., Wepf R., Grandi P., Hurt E. C. Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p. J. Cell Biol. 133:1996;1141-1152.
    • (1996) J. Cell Biol. , vol.133 , pp. 1141-1152
    • Zabel, U.1    Doye, V.2    Tekotte, H.3    Wepf, R.4    Grandi, P.5    Hurt, E.C.6


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