Nuclear lamins: Their structure, assembly, and interactions

Journal of Structural Biology

Volumn 122, Issue 1-2, 1998, Pages 42-66

  Stuurman, Nico ^a   Heins, Susanne ^a   Aebi, Ueli ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

Author keywords

Assembly; Cytoskeleton; Electron microscopy; Intermediate filaments; Lamins; Nuclear envelope; Nuclear lamina; Nuclear skeleton

Indexed keywords

INTERMEDIATE FILAMENT PROTEIN; LAMIN;

AMINO ACID SEQUENCE; ANIMAL CELL; CELL NUCLEUS MEMBRANE; CELLULAR DISTRIBUTION; CHROMATIN STRUCTURE; CYTOSKELETON; DNA REPLICATION; INTERMEDIATE FILAMENT; MOLECULAR MODEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; REVIEW; SEQUENCE ANALYSIS;

EID: 0031686054     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.1998.3987     Document Type: Article

References (185)

1. Aaronson R. P., Blobel G. Isolation of nuclear pore complexes in association with a lamina. Proc. Natl Acad. Sci. USA. 72:1975;1007-1011.
2. Aebi U., Cohn J., Buhle L., Gerace L. The nuclear lamina is a meshwork of intermediate-type filaments. Nature. 323:1986;560-564.
3. Aebi U., Häner M., Troncoso J., Eichner R., Engel A. Unifying principles in intermediate filament (IF) structure and assembly. Protoplasma. 145:1988;73-81.
4. Akey C. W. Interactions and structure of the nuclear pore complex revealed by cryo-electron microscopy. J. Cell Biol. 109:1989;955-970.
5. Appelbaum J., Blobel G., Georgatos S. D. In vivo phosphorylation of the lamin B receptor: Binding of lamin B to its nuclear membrane receptor is affected by phosphorylation. J. Biol. Chem. 265:1990;4181-4184.
6. Ashery-Padan R., Ulitzur N., Arbel A., Goldberg M., Weiss A. M., Maus N., Fisher P. A., Gruenbaum Y. Localization and posttranslational modifications of otefin, a protein required for vesicle attachment to chromatin, duringDrosophila melanogaster. Mol. Cell. Biol. 17:1997a;4114-4123.
7. Ashery-Padan R., Weiss A. M., Feinstein N., Gruenbaum Y. Distinct regions specify the targeting of otefin to the nucleoplasmic side of the nuclear envelope. J. Biol. Chem. 272:1997b;2493-2499.
8. Beck L. A., Hosick T. J., Sinensky M. Incorporation of a product of mevalonic acid metabolism into proteins of Chinese hamster ovary cell nuclei. J. Cell Biol. 107:1988;1307-1316.
9. Beck L. A., Hosick T. J., Sinensky M. Isoprenylation is required for the processing of the lamin A precursor. J. Cell Biol. 110:1990;1489-1499.
10. Belmont A. S., Zhai Y., Thilenius A. Lamin B distribution and association with peripheral chromatin revealed by optical sectioning and electron microscopy tomography. J. Cell Biol. 123:1993;1671-1685.
11. Benavente R., Krohne G. Change of karyoskeleton during spermatogenesis ofXenopus: Proc. Natl. Acad. Sci. USA. 82:1985;6176-6180.
12. Benavente R., Krohne G., Franke W. W. Cell type-specific expression of nuclear lamina proteins during development ofXenopus laevis. Cell. 41:1985;177-190.
13. Berger R., Theodor L., Shoham J., Gokkel E., Brok Simoni F., Avraham K. B., Copeland N. G., Jenkins N. A., Rechavi G., Simon A. J. The characterization and localization of the mouse thymopoietin/lamina-associated polypeptide 2 gene and its alternatively spliced products. Genome Res. 6:1996;361-370.
14. Bione S., Maestrini E., Rivella S., Mancini M., Regis S., Romeo G., Toniolo D. Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy. Nature Genet. 8:1994;323-327.
15. Bossie C. A., Sanders M. M. A cDNA fromDrosophila melanogaster. J. Cell Sci. 104:1993;1263-1272.
16. Bridger J. M., Kill I. R., O'Farrell M., Hutchison C. J. Internal lamin structures within G1 nuclei of human dermal fibroblasts. J. Cell Sci. 104:1993;297-306.
17. Broers J. L., Machiels B. M., Kuijpers H. J., Smedts F., van den Kieboom R., Raymond Y., Ramaekers F. C. A- and B-type lamins are differentially expressed in normal human tissues. Histochem. Cell Biol. 107:1997;505-517.
18. Buendia B., Courvalin J. C. Domain-specific disassembly and reassembly of nuclear membranes during mitosis. Exp. Cell Res. 230:1997;133-144.
19. Burke B., Gerace L. A cell free system to study reassembly of the nuclear envelope at the end of mitosis. Cell. 44:1986;639-652.
20. Chaudhary N., Courvalin J. C. Stepwise reassembly of the nuclear envelope at the end of mitosis. J. Cell Biol. 122:1993;295-306.
21. Chelsky D., Olson J. F., Koshland D. J. Cell cycle-dependent methyl esterification of lamin B. J. Biol. Chem. 262:1987;4303-4309.
22. Chelsky D., Sobotka C., O'Neill C. L. Lamin B methylation and assembly into the nuclear envelope. J. Biol. Chem. 264:1989;7637-7643.
23. Cheng J., Syder A. J., Yu Q. C., Letai A., Paller A. S., Fuchs E. The genetic basis of epidermolytic hyperkeratosis: A disorder of differentiation-specific epidermal keratin genes. Cell. 70:1992;811-819.
24. Chipev C. C., Korge B. P., Markova N., Bale S. J., DiGiovanna J. J., Compton J. G., Steinert P. M. A leucine → proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis. Cell. 70:1992;821-828.
25. Chipev C. C., Yang J. M., DiGiovanna J. J., Steinert P. M., Marekov L., Compton J. G., Bale S. J. Preferential sites in keratin 10 that are mutated in epidermolytic hyperkeratosis. Am. J. Hum. Genet. 54:1994;179-190.
26. Coates P. J., Hobbs R. C., Crocker J., Rowlands D. C., Murray P., Quinlan R., Hall P. A. Identification of the antigen recognized by the monoclonal antibody BU31 as lamins A and C. J. Pathol. 178:1996;21-29.
27. Collard J. F., Raymond Y. Transfection of human lamins A and C into mouse embryonal carcinoma cells possessing only lamin B. Exp. Cell Res. 186:1990;182-187.
28. Collas P., Courvalin J. C., Poccia D. Targeting of membranes to sea urchin sperm chromatin is mediated by a Lamin B receptor-like integral membrane protein. J. Cell Biol. 135:1996;1715-1725.
29. Collas P., Thompson L., Fields A. P., Poccia D. L., Courvalin J. C. Protein kinase C-mediated interphase lamin B phosphorylation and solubilization. J. Biol. Chem. 272:1997;21274-21280.
30. Conway J. F., Parry D. A. Structural features in the heptad substructure and longer range repeats of two-stranded alpha-fibrous proteins. Int. J. Biol. Macromol. 12:1990;328-334.
31. Conway J. F., Parry D. A. D. Intermediate filament structure. 3. Analysis of sequence homologies. Int. J. Biol. Macromol. 10:1988;79-98.
32. Coulombe P. A., Chan Y. M., Albers K., Fuchs E. Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitro. J. Cell Biol. 111:1990;3049-3064.
33. Coulombe P. A., Fuchs E. Epidermolysis bullosa simplex. Semin. Dermatol. 12:1993;173-190.
34. Coulombe P. A., Hutton M. E., Letai A., Hebert A., Paller A. S., Fuchs E. Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: Genetic and functional analyses. Cell. 66:1991;1301-1311.
35. Crewther W. G., Dowling L. M., Steinert P. M., Parry D. A. D. Structure of intermediate filaments. Int. J. Biol. Macromol. 5:1983;267-274.
36. Dodemont H., Riemer D., Weber K. Structure of an invertebrate gene encoding cytoplasmic intermediate filament (IF) proteins: Implications for the origin and the diversification of IF proteins. EMBO J. 9:1990;4083-4094.
37. Döring V., Stick R. Gene structure of nuclear lamin LIII ofXenopus laevis: EMBO J. 9:1990;4073-4081.
38. Draetta G. Cell cycle control in eukaryotes: Molecular mechanisms of cdc2 activation. Trends Biochem. Sci. 15:1990;378-383.
39. Eckelt A., Herrmann H., Franke W. W. Assembly of a tail-less mutant of the intermediate filament protein, vimentin, in vitro and in vivo. Eur. J. Cell Biol. 58:1992;319-330.
40. Ellenberg J., Siggia E. D., Moreira J. E., Smith C. L., Presley J. F., Worman H. J., Lippincott S. J. Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell Biol. 138:1997;1193-1206.
41. Ellis D. J., Jenkins H., Whitfield W. G., Hutchison C. J. GST-lamin fusion proteins act as dominant negative mutants inXenopus. J. Cell Sci. 110:1997;2507-2518.
42. Engel A., Eichner R., Aebi U. Polymorphism of reconstituted human epidermal keratin filaments: Mass-per-unit-length and width measurements by scanning transmission electron microscopy. J. Ultrastruct. Res. 90:1985;323-335.
43. Farnsworth C. C., Wolda S. L., Gelb M. H., Glomset J. A. Human lamin B contains a farnesylated cysteine residue. J. Biol. Chem. 264:1989;20422-20429.
44. Fisher D. Z., Chaudhary N., Blobel G. cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc. Natl Acad. Sci. USA. 83:1986;6450-6454.
45. Foisner R., Gerace L. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell. 73:1993;1267-1279.
46. Fricker M., Hollinshead M., White N., Vaux D. Interphase nuclei of many mammalian cell types contain deep, dynamic, tubular membrane-bound invaginations of the nuclear envelope. J. Cell Biol. 136:1997;531-544.
47. Fuchs E. The cytoskeleton and disease: Genetic disorders of intermediate filaments. Annu. Rev. Genetics. 30:1996;197-231.
48. Fuchs E., Coulombe P., Cheng J., Chan Y. M., Hutton E., Syder A., Degenstein L., Yu Q. C., Letai A., Vassar R. Genetic bases of epidermolysis bullosa simplex and epidermolytic hyperkeratosis. J. Invest. Dermatol. 103:1994;S25-S30.
49. Fuchs E., Weber K. Intermediate filaments: Structure, dynamics, function and disease. Annu. Rev. Biochem. 63:1994;345-382.
50. Furukawa K., Glass C., Kondo T. Characterization of the chromatin binding activity of lamina-associated polypeptide (LAP) 2. Biochem. Biophys. Res. Commun. 238:1997;240-246.
51. Furukawa K., Hotta Y. cDNA cloning of a germ cell specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells. EMBO J. 12:1993;97-106.
52. Furukawa K., Inagaki H., Hotta Y. Identification and cloning of an mRNA coding for a germ cell-specific A-type lamin in mice. Exp. Cell Res. 212:1994;426-430.
53. Furukawa K., Pante N., Aebi U., Gerace L. Cloning of a cDNA for lamina-associated polypeptide 2 (LAP2) and identification of regions that specify targeting to the nuclear envelope. EMBO J. 14:1995;1626-1636.
54. Geisler N. Chemical crosslinking with disuccinimidyl tartrate defines the relative positions of the two antiparallel coiled coils of the desmin protofilament unit. FEBS Lett. 323:1993;63-67.
55. Geisler N., Schunemann J., Weber K. Chemical cross-linking indicates a staggered and antiparallel protofilament of desmin intermediate filaments and characterizes one higher-level complex between protofilaments. Eur. J. Biochem. 206:1992;841-852.
56. Geisler N., Weber K. The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins. EMBO J. 1:1982;1649-1656.
57. Georgatos S. D., Meier J., Simos G. Lamins and lamin-associated proteins. Curr. Opin. Cell Biol. 6:1994;347-353.
58. Gerace L., Blobel G. The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell. 19:1980;277-287.
59. Gerace L., Blum A., Blobel G. Immunocytochemical localization of the major polypeptides of the nuclear pore complex-lamina fraction: Interphase and mitotic distribution. J. Cell Biol. 79:1978;546-566.
60. Gerace L., Burke B. Functional organization of the nuclear envelope. Annu. Rev. Cell Biol. 4:1988;335-374.
61. Gieffers C., Krohne G. In vitro reconstitution of recombinant lamin A and a lamin A mutant lacking the carboxy-terminal tail. Eur. J. Cell Biol. 55:1991;191-199.
62. Glass C. A., Glass J. R., Taniura H., Hasel K. W., Blevitt J. M., Gerace L. The alpha-helical rod domain of human lamins A and C contains a chromatin binding site. EMBO J. 12:1993;4413-4424.
63. Goldberg M., Jenkins H., Allen T., Whitfield W. G., Hutchison C. J. Xenopus. J. Cell Sci. 108:1995;3451-3461.
64. Goldberg, M. Lu, H. Ashery-Padan, R. Weiss, A. M. Stuurman, N. Fisher, P. A. Gruenbaum, Y. Wolfner, M. F. 1998, Interactions amongDrosophila.
65. Goldberg M. W., Allen T. D. 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.
66. Goldberg M. W., Solovei I., Allen T. D. Nuclear pore complex structure in birds. J. Struct. Biol. 119:1997;284-294.
67. Goldman A. E., Maul G., Steinert P. M., Yang H. Y., Goldman R. D. Keratin-like proteins that coisolate with intermediate filaments of BHK-21 cells are nuclear lamins. Proc. Natl. Acad. Sci. USA. 83:1986;3839-3843.
68. Goldman A. E., Moir R. D., Montag L. M., Stewart M., Goldman R. D. Pathway of incorporation of microinjected lamin A into the nuclear envelope. J. Cell Biol. 119:1992;725-735.
69. Gonnet G. H. New algorithms for the computation of evolutionary phylogenetic trees. Computational Methods in Genome Research. 1994;Plenum, New York.
70. II. J. Biol. Chem. 269:1994;19074-19080.
71. 0. J. Cell Biol. 106:1988;585-596.
72. Guilly M. N., Kolb J. P., Gosti F., Godeau F., Courvalin J. C. Lamins A and C are not expressed at early stages of human lymphocyte differentiation. Exp. Cell Res. 189:1990;145-147.
73. Harris C. A., Andryuk P. J., Cline S. W., Mathew S., Siekierka J. J., Goldstein G. Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO beta to rat lamin-associated polypeptide 2. Genomics. 28:1995;198-205.
74. Hatzfeld M., Weber K. Modulation of keratin intermediate filament assembly by single amino acid exchanges in the consensus sequence at the C-terminal end of the rod domain. J. Cell Sci. 99:1991;351-362.
75. Heald R., McKeon F. Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis. Cell. 61:1990;579-589.
76. Heins S., Aebi U. Making heads and tails of intermediate filament assembly, dynamics and networks. Curr. Opin. Cell Biol. 6:1994;25-33.
77. Heins S., Wong P. C., Müller S., Goldie K., Cleveland D. W., Aebi U. The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formation. J. Cell Biol. 123:1993;1517-1533.
78. 2Escherichia coli: J. Cell Biol. 113:1991;485-495.
79. 2. J. Struct. Biol. 108:1992;74-89.
80. Hennekes H., Nigg E. A. The role of isoprenylation in membrane attachments of nuclear lamins: A single point mutation prevents proteolytic cleavage of the lamin A precursors and confers membrane binding properties. J. Cell Sci. 107:1994;1019-1029.
81. Herrmann H., Aebi U. Intermediate filament assembly: Fibrillogenesis is driven by decisive dimer-dimer interactions. Curr. Opin. Struct. Biol. 8:1998;177-185.
82. Herrmann H., Häner M., Brettel M., Muller S. A., Goldie K. N., Fedtke B., Lustig A., Franke W. W., Aebi U. Structure and assembly properties of the intermediate filament protein vimentin: The role of its head, rod and tail domains. J. Mol. Biol. 264:1996;933-953.
83. Höger T. H., Krohne G., Kleinschmidt J. A. Interaction ofXenopus. Exp. Cell Res. 197:1991;280-289.
84. Höger T. H., Zatloukal K., Waizenegger I., Krohne G. Characterization of a second highly conserved B-type lamin present in cells previously thought to contain only a single B-type lamin. Chromosoma. 100:1990;67-69.
85. Holtz D., Tanaka R. A., Hartwig J., McKeon F. The CaaX motif of lamin A functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope. Cell. 59:1989;969-977.
86. Hozak P., Sasseville A. M. J., Raymond Y., Cook P. R. Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells. J. Cell Sci. 108:1995;635-644.
87. Hutchison C. J., Cox R., Ford C. C. The control of DNA replication in a cell-free extract that recapitulates a basic cell cycle in vitro. Development. 103:1988;553-566.
88. Kallman F., Wessells N. K. Periodic repeat units of epithelial cell tonofilaments. J. Cell Biol. 32:1967;227-231.
89. Kawahire S., Takeuchi M., Gohshi T., Sasagawa S., Shimada M., Takahashi M., Abe T. K., Ueda T., Kuwano R., Hikawa A., Ichimura T., Omata S., Horigome T. cDNA cloning of nuclear localization signal binding protein NBP60, a rat homologue of lamin B receptor, and identification of binding sites of human lamin B receptor for nuclear localization signals and chromatin. J. Biochem. Tokyo. 121:1997;881-889.
90. Kiseleva E., Goldberg M. W., Daneholt B., Allen T. D. RNP export is mediated by structural reorganization of the nuclear pore basket. J. Mol. Biol. 260:1996;304-311.
91. 2. J. Cell Biol. 113:1991;13-23.
92. Klapper M., Exner K., Kempf A., Gehrig C., Stuurman N., Fisher P., Krohne G. Assembly of A- and B-type lamins studied in vivo with the baculovirus system. J. Cell Sci. 110:1997;2519-2532.
93. Lane E. B., Rugg E. L., Navsaria H., Leigh I. M., Heagerty A. H., Ishida Y. A., Eady R. A. A mutation in the conserved helix termination peptide of keratin 5 in hereditary skin blistering. Nature. 356:1992;244-246.
94. Lehner C. F., Stick R., Eppenberger H. M., Nigg E. A. Differential expression of nuclear lamin proteins during chicken development. J. Cell Biol. 105:1987;577-587.
95. Lenz B. B., Wismar J., Fuchs S., Reifegerste R., Buchner E., Betz H., Schmitt B. Insertional mutation of theDrosophila. J. Cell Biol. 137:1997;1001-1016.
96. Letai A., Coulombe P. A., Fuchs E. Do the ends justify the mean? Proline mutations at the ends of the keratin coiled-coil rod segment are more disruptive than internal mutations. J. Cell Biol. 116:1992;1181-1195.
97. Letai A., Coulombe P. A., McCormick M. B., Yu Q. C., Hutton E., Fuchs E. Disease severity correlates with position of keratin point mutations in patients with epidermolysis bullosa simplex. Proc. Natl. Acad. Sci. USA. 90:1993;3197-3201.
98. Letai A., Fuchs E. The importance of intramolecular ion pairing in intermediate filaments. Proc. Natl. Acad. Sci. USA. 92:1995;92-96.
99. Lin F., Worman H. J. Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C. J. Biol. Chem. 268:1993;16321-16326.
100. Loewinger L., McKeon F. Mutations in the nuclear lamin proteins resulting in their aberrant assembly in the cytoplasm. EMBO J. 7:1988;2301-2309.
101. Lopez J. M., Wolfner M. F. The developmentally regulatedDrosophila. J. Cell Sci. 110:1997;643-651.
102. Lourim D., Kempf A., Krohne G. Characterization and quantitation of three B-type lamins inXenopus. J. Cell Sci. 1996;1775-1785.
103. 1. Cell. 70:1992;949-959.
104. Ludérus M. E. E., den Blaauwen J. L., de Smit O. J. B., Compton D. A., van Driel R. Binding of matrix attachment regions to lamin polymers involves single-stranded regions and the minor groove. Mol. Cell. Biol. 14:1994;6297-6305.
105. Lutz R. J., Trujillo M. A., Denham K. S., Wenger L., Sinensky M. Nucleoplasmic localization of prelamin A: Implications for prenylation-dependent lamin A assembly into the nuclear lamina. Proc. Natl. Acad. Sci. USA. 89:1992;3000-3004.
106. Machiels B. M., Zorenc A. H., Endert J. M., Kuijpers H. J., van E. G., Ramaekers F. C., Broers J. L. An alternative splicing product of the lamin A/C gene lacks exon 10. J. Biol. Chem. 271:1996;9249-9253.
107. Maison C., Pyrpasopoulou A., Theodoropoulos P. A., Georgatos S. D. The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles. EMBO J. 16:1997;4839-4850.
108. Maller J. L., Gautier J., Langan T. A., Lohka M. J., Shenoy S., Shalloway D., Nurse P. Maturation-promoting factor and the regulation of the cell cycle. J. Cell Sci. Suppl. 12:1989;53-63.
109. Manilal S., Nguyen T. M., Sewry C. A., Morris G. E. The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein. Hum. Mol. Genet. 5:1996;801-808.
110. Martin L., Crimaudo C., Gerace L. cDNA cloning and characterization of lamina-associated polypeptide 1C (LAP1C), an integral protein of the inner nuclear membrane. J. Biol. Chem. 270:1995;8822-8828.
111. McConnell S. J., Yaffe M. P. Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein. J. Cell Biol. 118:1992;385-395.
112. McConnell S. J., Yaffe M. P. Intermediate filament formation by a yeast protein essential for organelle inheritance. Science. 260:1993;687-689.
113. McCormick M. B., Kouklis P., Syder A., Fuchs E. The roles of the rod end and the tail in vimentin IF assembly and IF network formation. J. Cell Biol. 122:1993;395-407.
114. McKeon F. D., Kirschner M. W., Caput D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature. 319:1986;463-468.
115. McLachlan A. D. Coiled coil formation and sequence regularities in the helical regions of alpha-keratin. J. Mol. Biol. 124:1978;297-304.
116. Meier J., Campbell K. H., Ford C. C., Stick R., Hutchison C. J. The role of lamin LIII in nuclear assembly and DNA replication, in cell-free extracts ofXenopus. J. Cell Sci. 98:1991;271-279.
117. Meng J. J., Khan S., Ip W. Charge interactions in the rod domain drive formation of tetramers during intermediate filament assembly. J. Biol. Chem. 269:1994;18679-18685.
118. Moir R. D., Donaldson A. D., Stewart M. Expression inEscherichia coli. J. Cell Sci. 99:1991;363-372.
119. Moir R. D., Montaglowy M., Goldman R. D. Dynamic properties of nuclear lamins: Lamin B is associated with sites of DNA replication. J. Cell Biol. 125:1994;1201-1212.
120. Nagano A., Koga R., Ogawa M., Kurano Y., Kawada J., Okada R., Hayashi Y. K., Tsukahara T., Arahata K. Emerin deficiency at the nuclear membrane in patients with Emery-Dreifuss muscular dystrophy. Nature Genet. 12:1996;254-259.
121. Newport J. Nuclear reconstitution in vitro: stages of assembly around protein-free DNA. Cell. 48:1987;205-217.
122. Newport J. W., Wilson K. L., Dunphy W. G. A lamin-independent pathway for nuclear envelope assembly. J. Cell Biol. 111:1990;2247-2259.
123. Nigg E. A. The nuclear envelope. Curr. Opin. Cell Biol. 1:1989;435-440.
124. Nigg E. A. Assembly and cell cycle dynamics of the nuclear lamina. Semin. Cell Biol. 3:1992;245-253.
125. Nigg E. A., Kitten G. T., Vorburger K. Targeting lamin proteins to the nuclear envelope: The role of CaaX box modifications. Biochem. Soc. Trans. 20:1992;500-504.
126. Nikolakaki E., Meier J., Simos G., Georgatos S. D., Giannakouros T. Mitotic phosphorylation of the lamin B receptor by a serine/arginine kinase and p34(cdc2). J. Biol. Chem. 272:1997;6208-6213.
127. Nikolakaki E., Simos G., Georgatos S. D., Giannakouros T. A nuclear envelope-associated kinase phosphorylates arginine-serine motifs and modulates interactions between the lamin B receptor and other nuclear proteins. J. Biol. Chem. 271:1996;8365-8372.
128. Osman M., Paz M., Landesman Y., Fainsod A., Gruenbaum Y. Molecular analysis of theDrosophila. Genomics. 8:1990;217-224.
129. Paddy M. R., Belmont A. S., Saumweber H., Agard D. A., Sedat J. W. Interphase nuclear envelope lamins form a discontinuous network that interacts with only a fraction of the chromatin in the nuclear periphery. Cell. 62:1990;89-106.
130. Parry D. A., Conway J. F., Steinert P. M. Structural studies on lamin: Similarities and differences between lamin and intermediate-filament proteins. Biochem. J. 238:1986;305-308.
131. Parry D. A., Crewther W. G., Fraser R. D., MacRae T. P. Structure of alpha-keratin: Structural implication of the amino acid sequences of the type I and type II chain segments. J. Mol. Biol. 113:1977;449-454.
132. Parry D. A. D., Fraser R. D. B. Intermediate filament structure. 1. Analysis of IF protein sequence data. Int. J. Biol. Macromol. 7:1985;203-213.
133. Parry D. A. D., Steinert P. M. Intermediate Filament Structure. 1995;R. G. Landes Company, Austin.
134. Peter M., Heitlinger E., Häner M., Aebi U., Nigg E. A. Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase. EMBO J. 10:1991;1535-1544.
135. 1. J. Mol. Biol. 208:1989;393-404.
136. Peter M., Nakagawa J., Doree M., Labbe J. C., Nigg E. A. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell. 61:1990;591-602.
137. Peter M., Nigg E. A. Ectopic expression of an A-type lamin does not interfere with differentiation of lamin A-negative embryonal carcinoma cells. J. Cell Sci. 100:1991;589-598.
138. Peter M., Sanghera J. S., Pelech S. L., Nigg E. A. Mitogen-activated protein kinases phosphorylate nuclear lamins and display sequence specificity overlapping that of mitotic protein kinase p34cdc2. Eur. J. Biochem. 205:1992;287-294.
139. Powell L., Burke B. Internuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: In vivo evidence for the interaction of p55 with the nuclear lamina. J. Cell Biol. 111:1990;2225-2234.
140. Pyrpasopoulou A., Meier J., Maison C., Simos G., Georgatos S. D. The lamin B receptor (LBR) provides essential chromatin docking sites at the nuclear envelope. EMBO J. 15:1996;7108-7119.
141. Riemer D., Stuurman N., Berrios M., Hunter C., Fisher P. A., Weber K. Expression ofDrosophila. J. Cell Sci. 108:1995;3189-3198.
142. Riemer D., Weber K. The organization of the gene forDrosophilaDrosophila. Eur. J. Cell Biol. 63:1994;299-306.
143. Ris H. High-resolution field-emission scanning electron microscopy of nuclear pore complex. Scanning. 19:1997;368-375.
144. Röber R. A., Sauter H., Weber K., Osborn M. Cells of the cellular immune and hemopoietic system of the mouse lack lamins A/C: Distinction versus other somatic cells. J. Cell Sci. 95:1990;587-598.
145. Röber R. A., Weber K., Osborn M. Differential timing of nuclear lamin A/C expression in the various organs of the mouse embryo and the young animal: A developmental study. Development. 105:1989;365-378.
146. Schneider S., Folprecht G., Krohne G., Oberleithner H. Immunolocalization of lamins and nuclear pore complex proteins by atomic force microscopy. Pflugers Arch. 430:1995;795-801.
147. Senior A., Gerace L. Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina. J. Cell Biol. 107:1988;2029-2036.
148. Simos G., Georgatos S. D. The inner nuclear membrane protein p58 associates in vivo with a p58 kinase and the nuclear lamins. EMBO J. 11:1992;4027-4036.
149. Simos G., Georgatos S. D. The lamin B receptor-associated protein p34 shares sequence homology and antigenic determinants with the splicing factor 2-associated protein p32. FEBS Lett. 346:1994;225-228.
150. Simos G., Maison C., Georgatos S. D. Characterization of p18, a component of the lamin B receptor complex and a new integral membrane protein of the avian erythrocyte nuclear envelope. J. Biol. Chem. 271:1996;12617-12625.
151. Smith S., Blobel G. Colocalization of vertebrate lamin B and lamin B receptor (LBR) in nuclear envelopes and in LBR-induced membrane stacks of the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 91:1994;10124-10128.
152. Soullam B., Worman H. J. Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane. J. Cell Biol. 130:1995;15-27.
153. Spann T. P., Moir R. D., Goldman A. E., Stick R., Goldman R. D. Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis. J. Cell Biol. 136:1997;1201-1212.
154. Steinert P. M. Analysis of the mechanism of assembly of mouse keratin 1/keratin 10 intermediate filaments in vitro suggests that intermediate filaments are built from multiple oligomeric units rather than a unique tetrameric building block. J. Struct. Biol. 107:1991a;175-188.
155. Steinert P. M. Organization of coiled-coil molecules in native mouse keratin 1/keratin 10 intermediate filaments: Evidence for alternating rows of antiparallel in-register and antiparallel staggered molecules. J. Struct. Biol. 107:1991b;157-174.
156. Steinert P. M., Bale S. J. Genetic skin diseases caused by mutations in keratin intermediate filaments. Trends Genet. 9:1993;280-284.
157. Steinert P. M., Marekov L. N., Fraser R. D., Parry D. A. Keratin intermediate filament structure: Crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly. J. Mol. Biol. 230:1993a;436-452.
158. Steinert P. M., Marekov L. N., Parry D. A. Conservation of the structure of keratin intermediate filaments: Molecular mechanism by which different keratin molecules integrate into preexisting keratin intermediate filaments during differentiation. Biochemistry. 32:1993b;10046-10056.
159. Steinert P. M., Marekov L. N., Parry D. A. 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. 268:1993c;24916-24925.
160. Steinert P. M., Roop D. R. Molecular and cellular biology of intermediate filaments. Annu. Rev. Biochem. 57:1988;593-625.
161. Steinert P. M., Yang J. M., Bale S. J., Compton J. G. Concurrence between the molecular overlap regions in keratin intermediate filaments and the locations of keratin mutations in genodermatoses. Biochem. Biophys. Res. Commun. 197:1993d;840-848.
162. Stewart C., Burke B. Teratocarcinoma stem cells and early mouse embryos contain only a single major lamin polypeptide closely resembling lamin B. Cell. 51:1987;383-392.
163. Stewart M. Intermediate filament structure and assembly. Curr. Opin. Cell Biol. 5:1993;3-11.
164. Stick R., Hausen P. Changes in the nuclear lamina composition during early development ofXenopus laevis. Cell. 41:1985;191-200.
165. Stuurman N. Identification of a conserved phosphorylation site modulating nuclear lamin polymerization. FEBS Lett. 401:1997;171-174.
166. Stuurman N., Sasse B., Fisher P. A. Intermediate filament polymerization: Molecular analysis of nuclear lamin head-to-tail binding. J. Struct. Biol. 117:1996;1-15.
167. Taniura H., Glass C., Gerace L. A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones. J. Cell Biol. 131:1995;33-44.
168. Thompson L. J., Fields A. P. betaII protein kinase C is required for the G2/M phase transition of cell cycle. J. Biol. Chem. 271:1996;15045-15053.
169. Ulitzur N., Harel A., Feinstein N., Gruenbaum Y. Lamin activity is essential for nuclear envelope assembly in aDrosophila. J. Cell Biol. 119:1992;17-25.
170. Ulitzur N., Harel A., Goldberg M., Feinstein N., Gruenbaum Y. Nuclear membrane vesicle targeting to chromatin in aDrosophila. Mol. Biol. Cell. 8:1997;1439-1448.
171. Vorburger K., Kitten G. T., Nigg E. A. 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. 8:1989;4007-4013.
172. Weber K., Plessmann U., Traub P. Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor: Implications for the structure of the nuclear lamina. FEBS Lett. 257:1989a;411-414.
173. Weber K., Plessmann U., Ulrich W. 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. 8:1989b;3221-32217.
174. Weber K., Riemer D., Dodemont H. Aspects of the evolution of the lamin/intermediate filament protein family: A current analysis of invertebrate intermediate filament proteins. Biochem. Soc. Trans. 19:1991;1021-1023.
175. Wilson A. K., Coulombe P. A., Fuchs E. The roles of K5 and K14 head, tail, and R/K L L E G E domains in keratin filament assembly in vitro. J. Cell Biol. 119:1992;401-414.
176. Wolda S. L., Glomset J. A. Evidence for modification of lamin B by a product of mevalonic acid. J. Biol. Chem. 263:1988;5997-6000.
177. Wolin S. L., Krohne G., Kirschner M. W. A new lamin inXenopus. EMBO J. 6:1987;3809-3818.
178. Worman H. J., Yuan J., Blobel G., Georgatos S. D. A lamin B receptor in the nuclear envelope. Proc. Natl. Acad. Sci. USA. 85:1988;8531-8534.
179. Yang J. M., Chipev C. C., DiGiovanna J. J., Bale S. J., Marekov L. N., Steinert P. M., Compton J. G. Mutations in the H1 and 1A domains in the keratin 1 gene in epidermolytic hyperkeratosis. J. Invest. Dermatol. 102:1994;17-23.
180. Yang L., Guan T., Gerace L. Lamin-binding fragment of LAP2 inhibits increase in nuclear volume during the cell cycle and progression into S phase. J. Cell Biol. 139:1997;1077-1087.
181. Ye Q., Callebaut I., Pezhman A., Courvalin J. C., Worman H. J. Domain-specific interactions of human HP1-type chromodomain proteins and inner nuclear membrane protein LBR. J. Biol. Chem. 272:1997;14983-14989.
182. Ye Q., Worman H. J. Primary structure analysis and lamin B and DNA binding of human LBR, an integral protein of the nuclear envelope inner membrane. J. Biol. Chem. 269:1994;11306-11311.
183. Ye Q., Worman H. J. Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous toDrosophila. J. Biol. Chem. 271:1996;14653-14656.
184. Zhang C., Jenkins H., Goldberg M. W., Allen T. D., Hutchison C. J. Nuclear lamina and nuclear matrix organization in sperm pronuclei assembled in Xenopus egg extract. J. Cell Sci. 109:1996;2275-2286.
185. Zhao K., Harel A., Stuurman N., Guedalia D., Gruenbaum Y. Binding of