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Volumn 250, Issue 1, 1997, Pages 30-38

In vitro assembly of Drosophila lamin Dm0. Lamin polymerization properties are conserved

Author keywords

10 nm filaments; Drosophila; Head to tail polymerization; Intermediate filament; Nuclear lamin; Nucleus

Indexed keywords

CYTOPLASM PROTEIN; DIMER; LAMIN; NUCLEAR PROTEIN; POLYMER; RECOMBINANT PROTEIN;

EID: 0030732818     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00030.x     Document Type: Article
Times cited : (23)

References (53)
  • 1
    • 0038319891 scopus 로고
    • Isolation of nuclear pore complexes in association with a lamina
    • Aaronson, R. P. & Blobel, G. (1975) Isolation of nuclear pore complexes in association with a lamina, Proc. Natl Acad. Sci. USA 72, 1007 - 1011.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 1007-1011
    • Aaronson, R.P.1    Blobel, G.2
  • 2
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi, U., Cohn, J., Buhle, L. & Gerace, L. (1986) The nuclear lamina is a meshwork of intermediate-type filaments, Nature 323, 560 - 564.
    • (1986) Nature , vol.323 , pp. 560-564
    • Aebi, U.1    Cohn, J.2    Buhle, L.3    Gerace, L.4
  • 3
    • 0023419545 scopus 로고
    • A glow discharge unit to render electron microscope grids and other surfaces hydrophilic
    • Aebi, U. & Pollard, T. D. (1987) A glow discharge unit to render electron microscope grids and other surfaces hydrophilic, Electron Microsc. Tech. 7, 29 - 33.
    • (1987) Electron Microsc. Tech. , vol.7 , pp. 29-33
    • Aebi, U.1    Pollard, T.D.2
  • 4
    • 0002344099 scopus 로고
    • Unifying principles in intermediate filament (IF) structure and assembly
    • Aebi, U., Häner, M., Troncoso, J., Eichner, R. & Engel, A. (1988) Unifying principles in intermediate filament (IF) structure and assembly, Protoplasma 145, 73 - 81.
    • (1988) Protoplasma , vol.145 , pp. 73-81
    • Aebi, U.1    Häner, M.2    Troncoso, J.3    Eichner, R.4    Engel, A.5
  • 5
    • 0022415540 scopus 로고
    • Intermediate filaments in non-neuronal cells of invertebrates: Isolation and biochemical characterization of intermediate filaments from the esophegal epithelium of the mollusc Helix pomatia
    • Bartnik, E., Osborn, M. & Weber, K. (1985) Intermediate filaments in non-neuronal cells of invertebrates: isolation and biochemical characterization of intermediate filaments from the esophegal epithelium of the mollusc Helix pomatia, J. Cell Biol. 101, 427 - 440.
    • (1985) J. Cell Biol. , vol.101 , pp. 427-440
    • Bartnik, E.1    Osborn, M.2    Weber, K.3
  • 7
    • 0025633303 scopus 로고
    • Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitro
    • Coulombe, P. A., Chan, Y.-M., Albers, K. & Fuchs, E. (1990) Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitro, J. Cell Biol. 111, 3049 - 3064.
    • (1990) J. Cell Biol. , vol.111 , pp. 3049-3064
    • Coulombe, P.A.1    Chan, Y.-M.2    Albers, K.3    Fuchs, E.4
  • 8
    • 0025013610 scopus 로고
    • Structure of an invertebrate gene encoding cytoplasmic intermediate filament (IF) proteins: Implicationsfor the origin and the diversification of if proteins
    • Dodemont, H., Riemer, D. & Weber, K. (1990) Structure of an invertebrate gene encoding cytoplasmic intermediate filament (IF) proteins: implicationsfor the origin and the diversification of IF proteins, EMBO J. 9, 4083 - 4094.
    • (1990) EMBO J. , vol.9 , pp. 4083-4094
    • Dodemont, H.1    Riemer, D.2    Weber, K.3
  • 10
    • 0023032014 scopus 로고
    • cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins
    • Fisher, D. Z., Chaudhary, N. & Blobel, G. (1986) cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins, Proc. Natl Acad. Sci. USA 83, 6450 - 6454.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 6450-6454
    • Fisher, D.Z.1    Chaudhary, N.2    Blobel, G.3
  • 11
    • 0023657388 scopus 로고
    • Nuclear lamins and cytoplasmic intermediate filament proteins: A growing multigene family
    • Franke, W. W. (1987) Nuclear lamins and cytoplasmic intermediate filament proteins: A growing multigene family, Cell 48, 3 - 4.
    • (1987) Cell , vol.48 , pp. 3-4
    • Franke, W.W.1
  • 12
    • 0028287112 scopus 로고
    • Intermediate filaments and disease: Mutations that cripple cell strength
    • Fuchs, E. (1994) Intermediate filaments and disease: mutations that cripple cell strength, J. Cell Biol. 125, 511 - 516.
    • (1994) J. Cell Biol. , vol.125 , pp. 511-516
    • Fuchs, E.1
  • 13
    • 0020338526 scopus 로고
    • The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins
    • Geisler, N. & Weber, K. (1982) The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins, EMBO J. 1, 1649 - 1656.
    • (1982) EMBO J. , vol.1 , pp. 1649-1656
    • Geisler, N.1    Weber, K.2
  • 14
    • 0018093261 scopus 로고
    • Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction
    • Gerace, L., Blum, A. & Blobel, G. (1978) Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction, J. Cell Biol. 79, 546 - 566.
    • (1978) J. Cell Biol. , vol.79 , pp. 546-566
    • Gerace, L.1    Blum, A.2    Blobel, G.3
  • 15
    • 0025745453 scopus 로고
    • In vitro reconstitution of recombinant lamin A and a lamin A mutant lacking the carboxy-terminal tail
    • Gieffers, C. & Krohne, G. (1991) In vitro reconstitution of recombinant lamin A and a lamin A mutant lacking the carboxy-terminal tail, Eur. J. Cell Biol. 55, 191 - 199.
    • (1991) Eur. J. Cell Biol. , vol.55 , pp. 191-199
    • Gieffers, C.1    Krohne, G.2
  • 16
    • 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, T. D. (1996) The nuclear pore complex and lamina: three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy, J. Mol. Biol. 257, 848 - 865.
    • (1996) J. Mol. Biol. , vol.257 , pp. 848-865
    • Goldberg, M.W.1    Allen, T.D.2
  • 18
    • 0012426291 scopus 로고    scopus 로고
    • Glycerol spraying/low angle rotary metal shadowing
    • (Celis, J. E., ed.) Academic Press, Inc., San Diego
    • Häner, M., Bremer, A. & Aebi, U. (1998) Glycerol spraying/low angle rotary metal shadowing, in Cell Biology: a laboratory handbook. 2nd edn (Celis, J. E., ed.) pp. 292 - 298. Academic Press, Inc., San Diego.
    • (1998) Cell Biology: A Laboratory Handbook. 2nd Edn , pp. 292-298
    • Häner, M.1    Bremer, A.2    Aebi, U.3
  • 19
    • 0020614212 scopus 로고
    • The cDNA sequence of a type II cytoskeletal keratin reveals constant and variable structural diomains among keratins
    • Hanukoglu, I. & Fuchs, E. (1983) The cDNA sequence of a type II cytoskeletal keratin reveals constant and variable structural diomains among keratins, Cell 33, 915 - 924.
    • (1983) Cell , vol.33 , pp. 915-924
    • Hanukoglu, I.1    Fuchs, E.2
  • 20
    • 0025352896 scopus 로고
    • Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis
    • Heald, R. & McKeon, F. D. (1990) Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis, Cell 61, 579 - 589.
    • (1990) Cell , vol.61 , pp. 579-589
    • Heald, R.1    McKeon, F.D.2
  • 21
    • 0027763184 scopus 로고
    • The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formation
    • Heins, S., Wong, P. C., Muller, S., Goldie, K., Cleveland, D. W. & Aebi, U. (1993) The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formation, J. Cell Biol. 123, 1517 - 1533.
    • (1993) J. Cell Biol. , vol.123 , pp. 1517-1533
    • Heins, S.1    Wong, P.C.2    Muller, S.3    Goldie, K.4    Cleveland, D.W.5    Aebi, U.6
  • 22
    • 0028091403 scopus 로고
    • Making heads and tails of intermediate filament assembly, dynamics and networks
    • Heins, S. & Aebi, U. (1994) Making heads and tails of intermediate filament assembly, dynamics and networks, Curr. Opin. Cell Biol. 6, 25 - 33.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 25-33
    • Heins, S.1    Aebi, U.2
  • 24
    • 0026568833 scopus 로고
    • The role of the head and tail domain in lamin structure and assembly: Analysis of bacterially expressed chicken lamin A and truncated B2 lamins
    • Heitlinger, E., Peter, M., Lustig, A., Villiger, W., Nigg, E. A. & Aebi. U. (1992) The role of the head and tail domain in lamin structure and assembly: analysis of bacterially expressed chicken lamin A and truncated B2 lamins, J. Struct. Biol. 108, 74 - 89.
    • (1992) J. Struct. Biol. , vol.108 , pp. 74-89
    • Heitlinger, E.1    Peter, M.2    Lustig, A.3    Villiger, W.4    Nigg, E.A.5    Aebi, U.6
  • 25
    • 0030596170 scopus 로고    scopus 로고
    • Structure and assembly properties of the intermediate filament protein vimentin: The role of its head. rod and tail domains
    • Herrmann, H., Haner, M., Brettel, M., Muller, S. A., Goldie, K. N., Fedtke, B., Lustig, A., Franke, W. W. & Aebi, U. (1996) Structure and assembly properties of the intermediate filament protein vimentin: the role of its head. rod and tail domains, J. Mol. Biol. 264, 933 - 953.
    • (1996) J. Mol. Biol. , vol.264 , pp. 933-953
    • Herrmann, H.1    Haner, M.2    Brettel, M.3    Muller, S.A.4    Goldie, K.N.5    Fedtke, B.6    Lustig, A.7    Franke, W.W.8    Aebi, U.9
  • 26
    • 0014050617 scopus 로고
    • Periodic repeat units of epithelial cell tonofilaments
    • Kallman, F. & Wessells, N. K. (1967) Periodic repeat units of epithelial cell tonofilaments, J. Cell Biol. 32, 227 - 231.
    • (1967) J. Cell Biol. , vol.32 , pp. 227-231
    • Kallman, F.1    Wessells, N.K.2
  • 27
    • 0022569822 scopus 로고
    • The nuclear lamins: A multigene family of proteins in evolution and differentiation
    • Krohne, G. & Benavente, R. (1986) The nuclear lamins: A multigene family of proteins in evolution and differentiation, Exp. Cell Res. 162, 1 - 10.
    • (1986) Exp. Cell Res. , vol.162 , pp. 1-10
    • Krohne, G.1    Benavente, R.2
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680 - 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0026511054 scopus 로고
    • Do ends justify the the mean? Proline mutations at the ends of the keratin coiled-coil rod segment are more disruptive than internal mutations
    • Letai, A., Coulombe, P. & Fuchs, E. (1992) Do ends justify the the mean? Proline mutations at the ends of the keratin coiled-coil rod segment are more disruptive than internal mutations, J. Cell Biol. 116, 1181 - 1195.
    • (1992) J. Cell Biol. , vol.116 , pp. 1181-1195
    • Letai, A.1    Coulombe, P.2    Fuchs, E.3
  • 30
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of eoiled-coil structures
    • Lupas, A. (1996) Prediction and analysis of eoiled-coil structures, Methods Enzyinol. 266, 513 - 525.
    • (1996) Methods Enzyinol. , vol.266 , pp. 513-525
    • Lupas, A.1
  • 31
    • 0022648101 scopus 로고
    • Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins
    • McKeon, F. D., Kirschner, M. W. & Caput, D. (1986) Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins, Nature 319, 463 - 468.
    • (1986) Nature , vol.319 , pp. 463-468
    • McKeon, F.D.1    Kirschner, M.W.2    Caput, D.3
  • 32
    • 0025754857 scopus 로고
    • Nuclear lamin proteins: Domains required for nuclear targeting, assembly, and cell-cycle regulated dynamics
    • McKeon, F. D. (1991) Nuclear lamin proteins: domains required for nuclear targeting, assembly, and cell-cycle regulated dynamics, Curr. Opin. Cell Biol. 3, 82 - 86.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 82-86
    • McKeon, F.D.1
  • 33
    • 0025338951 scopus 로고
    • Expression and characterization of human lamin C
    • Moir, R. D., Quinlan, R. A. & Stewart, M. (1990) Expression and characterization of human lamin C, FEBS 268, 301 - 305.
    • (1990) FEBS , vol.268 , pp. 301-305
    • Moir, R.D.1    Quinlan, R.A.2    Stewart, M.3
  • 34
    • 0025876766 scopus 로고
    • Expression in Escherichia coli of human lamins A and C: Influence of head and tail domains on assembly properties and paracrystal formation
    • Moir, R. D., Donaldson, A. D. & Stewart, M. (1991) Expression in Escherichia coli of human lamins A and C: influence of head and tail domains on assembly properties and paracrystal formation, J. Cell Sci. 99, 363 - 372.
    • (1991) J. Cell Sci. , vol.99 , pp. 363-372
    • Moir, R.D.1    Donaldson, A.D.2    Stewart, M.3
  • 35
    • 0029198668 scopus 로고
    • The dynamic properties and possible functions of nuclear lamins
    • (Berezney, R. & Jeon, K. W., eds) Academic Press, Inc., San Diego
    • Moir, R. D., Spann, T. P. & Goldman, R. D. (1995) The dynamic properties and possible functions of nuclear lamins, in Structural and functional organization of the unclear matrix (Berezney, R. & Jeon, K. W., eds) pp. 141- 182, Academic Press, Inc., San Diego.
    • (1995) Structural and Functional Organization of the Unclear Matrix , pp. 141-182
    • Moir, R.D.1    Spann, T.P.2    Goldman, R.D.3
  • 36
    • 0028096967 scopus 로고
    • Determinants for intracellular sorting of cytoplasmic and nuclear intermediate filaments
    • Monteiro, M. J., Hicks, C., Gu, L. & Janicki, S. (1994) Determinants for intracellular sorting of cytoplasmic and nuclear intermediate filaments, J. Cell Biol. 127, 1327 - 1343.
    • (1994) J. Cell Biol. , vol.127 , pp. 1327-1343
    • Monteiro, M.J.1    Hicks, C.2    Gu, L.3    Janicki, S.4
  • 37
    • 0010322166 scopus 로고
    • Nuclear lamin proteins: Common structures for paracrystalline, filamentous and lattice forms
    • Parry, D. A. D., Conway, J. P., Goldman, A. E., Goldman, R. D. & Steinert, P. M. (1987) Nuclear lamin proteins: common structures for paracrystalline, filamentous and lattice forms, Int. J. Biol. Macromol. 9, 137 - 145.
    • (1987) Int. J. Biol. Macromol. , vol.9 , pp. 137-145
    • Parry, D.A.D.1    Conway, J.P.2    Goldman, A.E.3    Goldman, R.D.4    Steinert, P.M.5
  • 40
    • 0026778228 scopus 로고
    • Analysis of the cDNA and gene encoding a cytoplasmic intermediate filament (IF) protein from the cephalochordate Branchiostoma lanceolatum: Implications for the evolution of the if protein family
    • Riemer, D., Dodemont, H. & Weber, K. (1992) Analysis of the cDNA and gene encoding a cytoplasmic intermediate filament (IF) protein from the cephalochordate Branchiostoma lanceolatum: implications for the evolution of the IF protein family, Eur. J. Cell Biol. 58, 128 - 135.
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 128-135
    • Riemer, D.1    Dodemont, H.2    Weber, K.3
  • 42
    • 85045802190 scopus 로고
    • Biosynthesis and interconversion of Drosophiln nuclear lamin isoforms during normal cell growth and in response to heat shock
    • Smith, D. E., Gruenbaum, Y., Berrios, M. & Fisher, P. A. (1987) Biosynthesis and interconversion of Drosophiln nuclear lamin isoforms during normal cell growth and in response to heat shock, J. Cell Biol. 108, 255 - 265.
    • (1987) J. Cell Biol. , vol.108 , pp. 255-265
    • Smith, D.E.1    Gruenbaum, Y.2    Berrios, M.3    Fisher, P.A.4
  • 43
    • 0020540886 scopus 로고
    • Complete amino acid sequence of a mouse epidermal keratin subunit and implications for the structure of intermediate filaments
    • Steinen, P. M., Rice, R. H., Roop, D. R., Trus, B. L. & Steven, A. C. (1983) Complete amino acid sequence of a mouse epidermal keratin subunit and implications for the structure of intermediate filaments, Nature 302, 794 - 800.
    • (1983) Nature , vol.302 , pp. 794-800
    • Steinen, P.M.1    Rice, R.H.2    Roop, D.R.3    Trus, B.L.4    Steven, A.C.5
  • 44
    • 0023951297 scopus 로고
    • Molecular and cellular biology of intermediate filaments
    • Steinert, P. M. & Roop, D. R. (1988) Molecular and cellular biology of intermediate filaments, Anmt. Rev. Biochem. 57, 593 - 625.
    • (1988) Anmt. Rev. Biochem. , vol.57 , pp. 593-625
    • Steinert, P.M.1    Roop, D.R.2
  • 45
    • 0027160195 scopus 로고
    • Keratin intermediate structure: Crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly
    • Steinert, P. M., Marekov, L. N., Fraser, R. D. B. & Parry, D. A. D. (1993a) Keratin intermediate structure: crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly, J. Mol. Biol. 230, 436 - 452.
    • (1993) J. Mol. Biol. , vol.230 , pp. 436-452
    • Steinert, P.M.1    Marekov, L.N.2    Fraser, R.D.B.3    Parry, D.A.D.4
  • 46
    • 0027435278 scopus 로고
    • Diversity of intermediate filament structure: Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments
    • Steinert, P. M., Marekov, L. N. & Parry, D. A. D. (1993b) Diversity of intermediate filament structure: evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments, J. Biol. Chem. 268, 24916 - 24925.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24916-24925
    • Steinert, P.M.1    Marekov, L.N.2    Parry, D.A.D.3
  • 47
    • 0027550657 scopus 로고
    • Intermediate filament structure and assembly
    • Stewart, M. (1993) Intermediate filament structure and assembly, Curr. Opin. Cell Biol. 5, 3 - 11.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 3-11
    • Stewart, M.1
  • 48
    • 0026670970 scopus 로고
    • The gene structure of Xenopus nuclear lamin A: A model for the evolution of A-type from B-type lamins by exon shuffling
    • Stick, R. (1992) The gene structure of Xenopus nuclear lamin A: a model for the evolution of A-type from B-type lamins by exon shuffling, Chromosoma (Berl.) 101, 566 - 574.
    • (1992) Chromosoma (Berl.) , vol.101 , pp. 566-574
    • Stick, R.1
  • 49
    • 0030198913 scopus 로고    scopus 로고
    • Intermediate filament protein polymerization: Molecular analysis of Drosophila nuclear lamin head-to-tail binding
    • Stuurman, N., Sasse, B. & Fisher, P. A. (1996) Intermediate filament protein polymerization: molecular analysis of Drosophila nuclear lamin head-to-tail binding, J. Struct. Biol. 117, 1 - 15.
    • (1996) J. Struct. Biol. , vol.117 , pp. 1-15
    • Stuurman, N.1    Sasse, B.2    Fisher, P.A.3
  • 50
    • 0025787346 scopus 로고
    • Squid low molecular mass neurofilament proteins are a novel class of neurofilament protein. A nuclear lamin-like core and multiple distinct proteins formed by alternative RNA processing
    • Szaro, B. G., Pant, H. C., Way, J. & Battey, J. (1991) Squid low molecular mass neurofilament proteins are a novel class of neurofilament protein. A nuclear lamin-like core and multiple distinct proteins formed by alternative RNA processing, J. Biol. Chem. 266, 15035 - 15041.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15035-15041
    • Szaro, B.G.1    Pant, H.C.2    Way, J.3    Battey, J.4
  • 51
    • 0024439979 scopus 로고
    • A second higher vertebrate B-type lamin: CDNA sequence determination and in vitro processing of chicken lamin B2
    • Vorburger, K., Lehner, C. F., Kitten, G. T., Eppenberger, H. M. & Nigg, E. A. (1989) A second higher vertebrate B-type lamin: cDNA sequence determination and in vitro processing of chicken lamin B2, J. Mol. Biol. 208, 405 - 415.
    • (1989) J. Mol. Biol. , vol.208 , pp. 405-415
    • Vorburger, K.1    Lehner, C.F.2    Kitten, G.T.3    Eppenberger, H.M.4    Nigg, E.A.5
  • 52
    • 0024447881 scopus 로고
    • Cytoplasmic intermediate filament proteins of invertebrates are closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization of two muscle proteins of a nematode
    • Weber, K., Plessmann, U. & Ulrich, W. (1989) Cytoplasmic intermediate filament proteins of invertebrates are closer to nuclear lamins than are vertebrate intermediate filament proteins; sequence characterization of two muscle proteins of a nematode, EMBO J. 8, 3221 - 3227.
    • (1989) EMBO J. , vol.8 , pp. 3221-3227
    • Weber, K.1    Plessmann, U.2    Ulrich, W.3
  • 53
    • 0014328849 scopus 로고
    • The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy
    • Wrigley, N. (1968) The lattice spacing of crystalline catalase as an internal standard of length in electron microscopy, J. Ultrastruct. Res. 24, 454 - 464.
    • (1968) J. Ultrastruct. Res. , vol.24 , pp. 454-464
    • Wrigley, N.1


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