메뉴 건너뛰기




Volumn 36, Issue 6, 2008, Pages 1339-1343

A new model for nuclear lamina organization

Author keywords

Isoprenylation; Lamin; Laminopathy; Nuclear envelope; Nuclear lamina organization

Indexed keywords

INTERMEDIATE FILAMENT PROTEIN; LAMIN; LAMIN A; LAMIN B;

EID: 59149098009     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0361339     Document Type: Conference Paper
Times cited : (53)

References (45)
  • 1
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: Their structure, assembly, and interactions
    • Stuurman, N., Heins, S. and Aebi, U. (1998) Nuclear lamins: their structure, assembly, and interactions. J. Struct. Biol. 122, 42-66
    • (1998) J. Struct. Biol , vol.122 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 2
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann, H. and Aebi, U. (2004) Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 73, 749-789
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 3
    • 0022519369 scopus 로고
    • The nuclear lamina is a meshwork of intermediate-type filaments
    • Aebi, U., Cohn, J., Buhle, L. and 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
  • 4
    • 0025804024 scopus 로고
    • Expression of chicken lamin B2 in Escherichia coli: Characterization of its structure, assembly, and molecular interactions
    • Heitlinger, E., Peter, M., Häner, M., Lustig, A., Aebi, U. and Nigg, E.A. (1991) Expression of chicken lamin B2 in Escherichia coli: characterization of its structure, assembly, and molecular interactions. J. Cell Biol. 113, 485-495
    • (1991) J. Cell Biol , vol.113 , pp. 485-495
    • Heitlinger, E.1    Peter, M.2    Häner, M.3    Lustig, A.4    Aebi, U.5    Nigg, E.A.6
  • 5
    • 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. and 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
  • 6
    • 0037227428 scopus 로고    scopus 로고
    • The single nuclear lamin of Caenorrhabditis elegans forms in vitro stable intermediate filaments and paracrystals with a reduced axial periodicity
    • Karabinos, A., Schunemann, J., Meyer, M., Aebi, U. and Weber, K. (2003) The single nuclear lamin of Caenorrhabditis elegans forms in vitro stable intermediate filaments and paracrystals with a reduced axial periodicity. J. Mol. Biol. 325, 241-247
    • (2003) J. Mol. Biol , vol.325 , pp. 241-247
    • Karabinos, A.1    Schunemann, J.2    Meyer, M.3    Aebi, U.4    Weber, K.5
  • 7
    • 0021859643 scopus 로고
    • Changes in the nuclear lamina composition during early development of Xenopus laevis
    • Stick, R. and Hausen, P. (1985) Changes in the nuclear lamina composition during early development of Xenopus laevis. Cell 41, 191-200
    • (1985) Cell , vol.41 , pp. 191-200
    • Stick, R.1    Hausen, P.2
  • 8
    • 0021842623 scopus 로고
    • Cell type-specific expression of nuclear lamina proteins during development of Xenopus laevis
    • Benavente, R., Krohne, G. and Franke, W.W. (1985) Cell type-specific expression of nuclear lamina proteins during development of Xenopus laevis. Cell 41, 177-190
    • (1985) Cell , vol.41 , pp. 177-190
    • Benavente, R.1    Krohne, G.2    Franke, W.W.3
  • 9
    • 0024561417 scopus 로고
    • Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: A developmental study
    • Röber, R.A., Weber, K. and Osborn, M. (1989) Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: a developmental study. Development 105, 365-378
    • (1989) Development , vol.105 , pp. 365-378
    • Röber, R.A.1    Weber, K.2    Osborn, M.3
  • 11
    • 0024064963 scopus 로고
    • Mutations in the nuclear lamin proteins resulting in their aberrant assembly in the cytoplasm
    • Loewinger, L. and McKeon, F. (1988) Mutations in the nuclear lamin proteins resulting in their aberrant assembly in the cytoplasm. EMBO J. 7, 2301-2309
    • (1988) EMBO J , vol.7 , pp. 2301-2309
    • Loewinger, L.1    McKeon, F.2
  • 12
    • 0028274845 scopus 로고
    • The role of isoprenylation in membrane attachment of nuclear lamins: A single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties
    • Hennekes, H. and Nigg, E.A. (1994) The role of isoprenylation in membrane attachment of nuclear lamins: a single point mutation prevents proteolytic cleavage of the lamin A precursor and confers membrane binding properties. J. Cell Sci. 107, 1019-1029
    • (1994) J. Cell Sci , vol.107 , pp. 1019-1029
    • Hennekes, H.1    Nigg, E.A.2
  • 13
    • 0028913164 scopus 로고
    • Analysis of nuclear lamin isoprenylation in Xenopus oocytes: Isoprenylation of lamin B3 precedes its uptake into the nucleus
    • Firmbach-Kraft, I. and Stick, R. (1995) Analysis of nuclear lamin isoprenylation in Xenopus oocytes: isoprenylation of lamin B3 precedes its uptake into the nucleus. J. Cell Biol. 129, 17-24
    • (1995) J. Cell Biol , vol.129 , pp. 17-24
    • Firmbach-Kraft, I.1    Stick, R.2
  • 14
    • 0024839672 scopus 로고
    • Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C-terminal CXXM motif
    • Vorburger, K., Kitten, G.T. and Nigg, E.A. (1989) Modification of nuclear lamin proteins by a mevalonic acid derivative occurs in reticulocyte lysates and requires the cysteine residue of the C-terminal CXXM motif. EMBO J. 8, 4007-4013
    • (1989) EMBO J , vol.8 , pp. 4007-4013
    • Vorburger, K.1    Kitten, G.T.2    Nigg, E.A.3
  • 15
    • 33748760066 scopus 로고    scopus 로고
    • Farnesylated lamins, progeroid syndromes and farnesyl transferase inhibitors
    • Rusiñol, A.E. and Sinensky, M.S. (2006) Farnesylated lamins, progeroid syndromes and farnesyl transferase inhibitors. J. Cell Sci. 119, 3265-3272
    • (2006) J. Cell Sci , vol.119 , pp. 3265-3272
    • Rusiñol, A.E.1    Sinensky, M.S.2
  • 16
    • 0025845750 scopus 로고
    • The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2
    • Kitten, G.T. and Nigg, E.A. (1991) The CaaX motif is required for isoprenylation, carboxyl methylation, and nuclear membrane association of lamin B2. J. Cell Biol. 113, 13-23
    • (1991) J. Cell Biol , vol.113 , pp. 13-23
    • Kitten, G.T.1    Nigg, E.A.2
  • 17
    • 0032431736 scopus 로고    scopus 로고
    • The role of sequences unique to nuclear intermediate filaments in the targeting and assembly of human lamin B: Evidence for lack of interaction of lamin B with its putative receptor
    • Mical, T.I. and Monteiro, M.J. (1998) The role of sequences unique to nuclear intermediate filaments in the targeting and assembly of human lamin B: evidence for lack of interaction of lamin B with its putative receptor. J. Cell Sci. 111, 3471-3485
    • (1998) J. Cell Sci , vol.111 , pp. 3471-3485
    • Mical, T.I.1    Monteiro, M.J.2
  • 18
    • 0018840796 scopus 로고
    • The nuclear envelope lamina is reversibly depolymerized during mitosis
    • Gerace, L. and Blobel, G. (1980) The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell 19, 277-287
    • (1980) Cell , vol.19 , pp. 277-287
    • Gerace, L.1    Blobel, G.2
  • 19
    • 0028204109 scopus 로고
    • Type B lamins remain associated with the integral nuclear envelope protein p58 during mitosis: Implications for nuclear reassembly
    • Meier, J. and Georgatos, S.D. (1994) Type B lamins remain associated with the integral nuclear envelope protein p58 during mitosis: implications for nuclear reassembly. EMBO J. 13, 1888-1898
    • (1994) EMBO J , vol.13 , pp. 1888-1898
    • Meier, J.1    Georgatos, S.D.2
  • 21
    • 30844434561 scopus 로고    scopus 로고
    • Prelamin A, Zmpste24, misshapen cell nuclei, and progeria: New evidence suggesting that protein farnesylation could be important for disease pathogenesis
    • Young, S.G., Fong, L.G. and Michaelis, S. (2005) Prelamin A, Zmpste24, misshapen cell nuclei, and progeria: new evidence suggesting that protein farnesylation could be important for disease pathogenesis. J. Lipid Res. 46, 2531-2558
    • (2005) J. Lipid Res , vol.46 , pp. 2531-2558
    • Young, S.G.1    Fong, L.G.2    Michaelis, S.3
  • 22
    • 0033926099 scopus 로고    scopus 로고
    • Lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics
    • Dechat, T., Vlcek, S. and Foisner, R. (2000) Lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics. J. Struct. Biol. 129, 335-345
    • (2000) J. Struct. Biol , vol.129 , pp. 335-345
    • Dechat, T.1    Vlcek, S.2    Foisner, R.3
  • 23
    • 41649097238 scopus 로고    scopus 로고
    • Nuclear lamins: Major factors in the structural organization and function of the nucleus and chromatin
    • Dechat, T., Pfleghaar, K., Sengupta, K., Shimi, T., Shumaker, D.K., Solimando, L. and Goldman, R.D. (2008) Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin. Genes Dev. 22, 832-853
    • (2008) Genes Dev , vol.22 , pp. 832-853
    • Dechat, T.1    Pfleghaar, K.2    Sengupta, K.3    Shimi, T.4    Shumaker, D.K.5    Solimando, L.6    Goldman, R.D.7
  • 24
    • 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 101, 566-574
    • (1992) Chromosoma , vol.101 , pp. 566-574
    • Stick, R.1
  • 25
    • 0027936303 scopus 로고
    • The gene structure of B-type nuclear lamins of Xenopus laevis: Implications for the evolution of the vertebrate lamin family
    • Stick, R. (1994) The gene structure of B-type nuclear lamins of Xenopus laevis: implications for the evolution of the vertebrate lamin family. Chromosome Res. 2, 376-382
    • (1994) Chromosome Res , vol.2 , pp. 376-382
    • Stick, R.1
  • 27
    • 0023766203 scopus 로고
    • Heterotypic and homotypic associations between the nuclear lamins: Site-specificity and control by phosphorylation
    • Georgatos, S.D., Stournaras, C. and Blobel, G. (1980) Heterotypic and homotypic associations between the nuclear lamins: site-specificity and control by phosphorylation. Proc. Natl. Acad. Sci. U.S.A. 85, 4325-4329
    • (1980) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 4325-4329
    • Georgatos, S.D.1    Stournaras, C.2    Blobel, G.3
  • 28
    • 0029160015 scopus 로고
    • Protein-protein interactions between human nuclear lamins expressed in yeast
    • Ye, Q. and Worman, H.J. (1995) Protein-protein interactions between human nuclear lamins expressed in yeast. Exp. Cell Res. 219, 292-298
    • (1995) Exp. Cell Res , vol.219 , pp. 292-298
    • Ye, Q.1    Worman, H.J.2
  • 29
    • 5644250530 scopus 로고    scopus 로고
    • The stability of the nuclear lamina polymer changes with the composition of lamin subtypes according to their individual binding strengths
    • Schirmer, E.C. and Gerace, L. (2004) The stability of the nuclear lamina polymer changes with the composition of lamin subtypes according to their individual binding strengths. J. Biol. Chem. 279, 42811-42817
    • (2004) J. Biol. Chem , vol.279 , pp. 42811-42817
    • Schirmer, E.C.1    Gerace, L.2
  • 31
    • 1842584782 scopus 로고    scopus 로고
    • Proteins that bind A-type lamins: Integrating isolated clues
    • Zastrow, M.S., Vlcek, S. and Wilson, K.L. (2002) Proteins that bind A-type lamins: integrating isolated clues. J. Cell Sci. 117, 979-987
    • (2002) J. Cell Sci , vol.117 , pp. 979-987
    • Zastrow, M.S.1    Vlcek, S.2    Wilson, K.L.3
  • 32
    • 32244437071 scopus 로고    scopus 로고
    • Nuclear titin interacts with A- and B-type lamins in vitro and in vivo
    • Zastrow, M.S., Flaherty, D.B., Benian, G.M. and Wilson, K.L. (2006) Nuclear titin interacts with A- and B-type lamins in vitro and in vivo. J. Cell Sci. 119, 239-249
    • (2006) J. Cell Sci , vol.119 , pp. 239-249
    • Zastrow, M.S.1    Flaherty, D.B.2    Benian, G.M.3    Wilson, K.L.4
  • 33
    • 5144220584 scopus 로고    scopus 로고
    • Crystal structure of the human lamin A coil 2B dimer: Implications for the head-to-tail association of nuclear lamins
    • Strelkov, S.V., Schumacher, J., Burkhard, P., Aebi, U. and Herrmann, H. (2004) Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins. J. Mol. Biol. 343, 1067-1080
    • (2004) J. Mol. Biol , vol.343 , pp. 1067-1080
    • Strelkov, S.V.1    Schumacher, J.2    Burkhard, P.3    Aebi, U.4    Herrmann, H.5
  • 34
    • 0026453303 scopus 로고
    • Purification and immunological detection of pea nuclear intermediate filaments: Evidence for plant nuclear lamins
    • McNaulty, A.K. and Saunders, M.J. (1992) Purification and immunological detection of pea nuclear intermediate filaments: evidence for plant nuclear lamins. J. Cell Sci. 103, 407-414
    • (1992) J. Cell Sci , vol.103 , pp. 407-414
    • McNaulty, A.K.1    Saunders, M.J.2
  • 35
    • 0027435594 scopus 로고
    • Immunological characterisation of lamins in the nuclear matrix of onion cells
    • Mínguez, A. and Moreno Díaz de la Espina, S. (1993) Immunological characterisation of lamins in the nuclear matrix of onion cells. J. Cell Sci. 106, 431-439
    • (1993) J. Cell Sci , vol.106 , pp. 431-439
    • Mínguez, A.1    Moreno Díaz de la Espina, S.2
  • 36
    • 0031562693 scopus 로고    scopus 로고
    • Peripheral framework of carrot cell nucleus contains a novel protein predicted to exhibit a long α-helical domain
    • Masuda, K., Xu, Z.J., Takahashi, S., Ito, A., Ono, M., Nomura, K. and Inoue, M. (1997) Peripheral framework of carrot cell nucleus contains a novel protein predicted to exhibit a long α-helical domain. Exp. Cell Res. 232, 173-181
    • (1997) Exp. Cell Res , vol.232 , pp. 173-181
    • Masuda, K.1    Xu, Z.J.2    Takahashi, S.3    Ito, A.4    Ono, M.5    Nomura, K.6    Inoue, M.7
  • 37
    • 35748984432 scopus 로고    scopus 로고
    • LITTLE NUCLEI genes affecting nuclear morphology in Arabidopsis thaliana
    • Dittmer, T.A., Stacey, N.J., Sugimoto-Shirasu, K. and Richards, E.J. (2007) LITTLE NUCLEI genes affecting nuclear morphology in Arabidopsis thaliana. Plant Cell 19, 2793-2803
    • (2007) Plant Cell , vol.19 , pp. 2793-2803
    • Dittmer, T.A.1    Stacey, N.J.2    Sugimoto-Shirasu, K.3    Richards, E.J.4
  • 38
    • 0025144559 scopus 로고
    • Selective digestion of nuclear envelopes from Xenopus oocyte germinal vesicles: Possible structural role for the nuclear lamina
    • Whytock, S., Moir, R.D. and Stewart, M. (1990) Selective digestion of nuclear envelopes from Xenopus oocyte germinal vesicles: possible structural role for the nuclear lamina. J. Cell Sci. 97, 571-580
    • (1990) J. Cell Sci , vol.97 , pp. 571-580
    • Whytock, S.1    Moir, R.D.2    Stewart, M.3
  • 39
    • 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. and 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
  • 40
    • 38949154474 scopus 로고    scopus 로고
    • Filaments made from A- and B-type lamins differ in structure and organization
    • Goldberg, M.W., Huttenlauch, I., Hutchison, C.J. and Stick, R. (2008) Filaments made from A- and B-type lamins differ in structure and organization. J. Cell Sci. 121, 215-225
    • (2008) J. Cell Sci , vol.121 , pp. 215-225
    • Goldberg, M.W.1    Huttenlauch, I.2    Hutchison, C.J.3    Stick, R.4
  • 41
    • 0024095062 scopus 로고
    • cDNA cloning of the developmentally regulated lamin LIII of Xenopus laevis
    • Stick, R. (1988) cDNA cloning of the developmentally regulated lamin LIII of Xenopus laevis. EMBO J. 7, 3189-3197
    • (1988) EMBO J , vol.7 , pp. 3189-3197
    • Stick, R.1
  • 42
    • 0027104231 scopus 로고
    • High resolution scanning electron microscopy of the nuclear envelope: Demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores
    • Goldberg, M.W. and Allen, T.D. (1992) High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores. J. Cell Biol. 119, 1429-1440
    • (1992) J. Cell Biol , vol.119 , pp. 1429-1440
    • Goldberg, M.W.1    Allen, T.D.2
  • 43
    • 0027525230 scopus 로고
    • The nuclear pore complex: Three dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlying structure uncovered by proteolysis
    • Goldberg, M.W. and Allen, T.D. (1993) The nuclear pore complex: three dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlying structure uncovered by proteolysis. J. Cell Sci. 106, 261-274
    • (1993) J. Cell Sci , vol.106 , pp. 261-274
    • Goldberg, M.W.1    Allen, T.D.2
  • 44
    • 34249668426 scopus 로고    scopus 로고
    • Proteins that associate with lamins: Many faces, many functions
    • Schirmer, E.C. and Foisner, R. (2007) Proteins that associate with lamins: many faces, many functions. Exp. Cell Res. 313, 2167-2179
    • (2007) Exp. Cell Res , vol.313 , pp. 2167-2179
    • Schirmer, E.C.1    Foisner, R.2
  • 45
    • 12344259997 scopus 로고    scopus 로고
    • Intranuclear membrane structure formations by CaaX-containing nuclear proteins
    • Ralle, T., Grund, C., Franke, W.W. and Stick, R. (2004) Intranuclear membrane structure formations by CaaX-containing nuclear proteins. J. Cell Sci. 117, 6095-6104
    • (2004) J. Cell Sci , vol.117 , pp. 6095-6104
    • Ralle, T.1    Grund, C.2    Franke, W.W.3    Stick, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.