Lamins

Methods in Cell Biology

Volumn 2004, Issue 78, 2004, Pages 573-596

  Krohne, Georg ^a  

^a UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

LAMIN; RECOMBINANT PROTEIN;

ANIMAL; ARMYWORM; ARTICLE; BACULOVIRUS; BIOSYNTHESIS; CELL LINE; CELL NUCLEUS; CHEMISTRY; DIALYSIS; ESCHERICHIA COLI; GEL CHROMATOGRAPHY; GENETIC TRANSFECTION; GENETICS; HELA CELL; HUMAN; IMMUNOPRECIPITATION; ISOLATION AND PURIFICATION; LIVER; METABOLISM;

ANIMALS; BACULOVIRIDAE; CELL LINE; CELL NUCLEUS; CHROMATOGRAPHY, AGAROSE; DIALYSIS; ESCHERICHIA COLI; HELA CELLS; HUMANS; IMMUNOPRECIPITATION; LAMINS; LIVER; RECOMBINANT PROTEINS; SPODOPTERA; TRANSFECTION;

EID: 14244266213     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0091-679x(04)78020-6     Document Type: Review

References (45)

1. Aebi, U., Cohn, J., Buhle, L., and Gerace, L. (1986). The nuclear lamina is a meshwork of intermediate-type filaments. Nature (London) 323, 560-564.
2. Alsheimer, M., von Glasenapp, E., Hock, R., and Benavente, R. (1999). Architecture of the nuclear periphery of rat pachytene spermatocytes: Distribution of nuclear envelope proteins in relation to synaptonemal complex attachment sites. Mol. Biol. Cell 10, 1235-1245.
3. Benavente, R., and Krohne, G. (1998). In vivo systems to study the dynamics of nuclear lamins. In "Methods in Cell Biology" (M. Berrios, ed.), Vol 53, pp. 591-602. Academic Press, San Diego.
4. 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.
5. Cohen, M., Lee, K. K., Wilson, K. L., and Gruenbaum, Y. (2001). Transcriptional repression, apoptosis, human disease and the functional evolution of the nuclear lamina. Trends Biochem. Sci. 26, 41-47.
6. Collard, J. F., and Raymond, Y. (1990). Transfection of human lamins A and C into mouse embryonal carcinoma cells possessing only lamin B. Exp. Cell Res. 186, 182-187.
7. Dechat, T., Vleck, S., and Foisner, R. (2000a). Lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics. J. Struct. Biol. 129, 335-345.
8. Dechat, T., Korbei, B., Vaughan, O. A., Vlcek, S., Hutchison, C. J., and Foisner, R. (2000b). Lamina-associated polypeptide 2α binds intranuclear A-type lamins. J. Cell Sci. 113, 3473-3484.
9. Erber, A., Riemer, D., Hofemeister, H., Bovenschulte, M., Stick, R., Panopoulou, G., Lehrach, H., and Weber, K. (1999). Characterization of the Hydra lamin and its gene: a molecular phylogeny of metazoan lamins. J. Mol. Evol. 49, 260-271.
10. Foisner, R., and Gerace, L. (1993). Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 73, 1267-1279.
11. Furukawa, K., and Hotta, Y. (1993). cDNA cloning of a germ line specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells. EMBO J. 12, 97-106.
12. Gant, T. M., Harris, C. A., and Wilson, K. L. (1999). Roles of LAP2 proteins in nuclear assembly and DNA replication: Truncated LAP2β proteins alter lamina assembly, envelope formation, nuclear size, and DNA replication efficiency in Xenopus laevis extracts. J. Cell Biol. 144, 1083-1096.
13. Gieffers, C., and 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.
14. Glass, J. R., and Gerace, L. (1990). Lamins A and C bind and assemble at the surface of mitotic chromosomes. J. Cell Biol. 111, 1047-1057.
15. Goldman, R. D., Gruenbaum, Y., Moir, R. D., Shumaker, D. K., and Spann, T. P. (2002). Nuclear lamins: Building blocks of nuclear architecture. Genes Dev. 16, 533-547.
16. Gruenbaum, Y., Goldman, R. D., Meyuhas, R., Mills, E., Margalit, A., Fridkin, A., Dayani, Y., Prokocimer, M., and Enosh, A. (2003). The nuclear lamina and its functions in the nucleus. Int. Rev. Cytol. 226, 1-62.
17. Hennekes, H., and Nigg, E. (1994). The role of isoprenylation in membrane attachment of nuclear lamins,. J. Cell Sci. 107, 1019-1029.
18. Hofemeister, H., Kuhn, C., Franke, W. W., Weber, K., and Stick, R. (2002). Conservation of the gene structure and membrane targeting signals of germ cell specific lamin LIII in amphibians and fish. Eur. J. Cell Biol. 81, 51-60.
19. Karabinos, A., Schunemann, J., Meyer, M., Aebi, U., and Weber, K. (2003). The single nuclear lamin of Caenorhabditis elegans forms in vitro stable intermediate filaments and paracrystals with a reduced axial periodicity. J. Mol. Biol. 325, 241-247.
20. Kaufmann, S. H., Gibson, W., and Shaper, J. H. (1983). Characterization of the major polypeptide of the rat liver nuclear envelope. J. Biol. Chem. 258, 2710-2719.
21. Klapper, M., Exner, K., Kempf, A., Gehrig, C., Stuurman, N., Fisher, P. A., and Krohne, G. (1997). Assembly of A- and B-type lamins studied in vivo with the baculovirus system. J. Cell Sci. 110, 2519-2532.
22. Krimm, I., Ostlund, C., Gilquin, B., Couprie, J., Hossenlopp, P., Mornon, J. P., Bonne, G., Courvalin, J. C., Worman, H. J., and Zinn-Justin, S. (2002). The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy. Structure (Camb) 10, 811-823.
23. Krohne, G. (1998). Lamin assembly in vivo. In "Subcellular Biochemistry: Intermediate Filaments" (H. Herrmann and J. Robin Harris, eds.), pp. 563-586. Plenum Publishing, London, UK.
24. Krohne, G., and Franke, W. W. (1983). Proteins of pore complex-lamina structures from nuclei and membranes. Methods Enzymol. 963, 597-608.
25. Krohne, G., Stuurman, N., and Kempf, A. (1998). Assembly of Drosophila lamin DmO and C mutant proteins studied with the baculovirus system. Eur. J. Cell Biol. 77, 276-283.
26. Krohne, G., Waizenegger, I., and Höger, T. H. (1989). The conserved carboxy-terminal cysteine of nuclear lamins is essential for lamin association with the nuclear envelope. J. Cell Biol. 109, 2003-2011.
27. 1 of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily. EMBO J. 6, 3801-3808.
28. Kyhse-Andersen, J. (1984). Electroblotting of multiple gels: A simple apparatus without tank for rapid transfer of proteins form polyacrylamide to nitrocellulose. J. Biochem. Biophys. Methods 10, 203-210.
29. Laemmli, U. (1970). Cleavage of structural proteins during assembly of the head of the bacteriophage T4. Nature (London) 227, 680-685.
30. Lang, C., and Krohne, G. (2003). Lamina-associated polypeptide 2β (LAP2β) is contained in a protein complex together with A- and B-type lamins. Eur. J. Cell Biol. 82, 143-153.
31. Lebel, S., Lampron, C., Royal, A., and Raymond, Y. (1987). Lamins A and C appear during retinoic acid-induced differentiation of mouse embryonal carcinoma cells. J. Cell Biol. 105, 1099-1104.
32. Lehner, C. F., Kurer, V., Eppenberger, H. M., and Nigg, E. A. (1986). The nuclear lamin protein family in higher vertebrates. Identification of quantitatively minor lamin proteins by monoclonal antibodies. J. Biol. Chem. 261, 13293-13301.
33. Lehner, C. F., Stick, R., Eppenberger, H. M., and Nigg, E. A. (1987). Differential expression of nuclear lamin proteins during chicken development. J. Cell Biol. 105, 577-587.
34. 1 protein synthesis during meiotic maturation. J. Cell Sci. 109, 1775-1785.
35. Lourim, D., and Krohne, G. (1993). Membrane-associated lamins in Xenopus egg extracts: Identification of two vesicle populations. J. Cell Biol. 123, 501-512.
36. Maske, C. P., Hollinshead, M. S., Higbee, N. C., Bergo, M. O., Young, S. G., and Vaux, D. J. (2003). A carboxyl-terminal interaction of lamin B1 is dependent on the CAAX endoprotease Reel and carboxymethylation. J. Cell Biol. 162, 1223-1232.
37. Newmeyer, D., and Wilson, K. (1991). Egg extracts for nuclear import and nuclear assembly reactions. Methods Cell Biol. 36, 607-635.
38. Olins, A. L., Herrmann, H., Lichter, P., Kratzmeier, M., Doenecke, D., and Olins, D. E. (2001). Nuclear envelope and chromatin compositional differences comparing undifferentiated and retinoic acid- and phorbol ester-treated HL-60 cells. Exp. Cell Res. 268, 115-127.
39. Riemer, D., Dodemont, H., and Weber, K. (1993). A nuclear lamin of the nematode Caenorhabditis elegans with unusual structural features; cDNA cloning and gene organization. Eur. J. Cell Biol. 62, 214-223.
40. Schmidt, M., and Krohne, G. (1995). In vivo assembly kinetics of fluorescently labeled Xenopus lamin A mutants. Eur. J. Cell Biol. 68, 345-354.
41. Schmidt, M., Tschödrich-Rotter, M., Peters, R., and Krohne, G. (1994). Properties of fluorescently labeled Xenopus lamin A in vivo. Eur. J. Cell Biol. 65, 70-81.
42. Spann, T. P., Moir, R. D., Goldman, A. E., Stick, R., and Goldman, R. D. (1997). Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis. J. Cell Biol. 136, 1201-1212.
43. Stuurman, N., Heins, S., and Aebi, U. (1998). Nuclear lamins: Their structure, assembly, and interactions. J. Struct. Biol. 122, 42-66.
44. Wagner, N., Weber, D., Seitz, S., and Krohne, G. (2004). The lamin B receptor of Drosophila melanogaster. J. Cell Sci. 117, 2015-2028.
45. Weber, K., Plessmann, U., and Traub, P. (1989). 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, 411-414.