Identification of a novel, highly variable amino-terminal amino acid sequence element in the nuclear intermediate filament protein lamin B2 from higher vertebrates

FEBS Letters

Volumn 580, Issue 26, 2006, Pages 6211-6216

  Schumacher, Jens ^a   Reichenzeller, Michaela ^a   Kempf, Tore ^a   Schnölzer, Martina ^a   Herrmann, Harald ^a  

^a GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

Author keywords

Intermediate filaments; Lamin B2; Nuclear envelope

Indexed keywords

COMPLEMENTARY DNA; GREEN FLUORESCENT PROTEIN; LAMIN B; LAMIN B2; PROTEIN ANTIBODY; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CATTLE; CHIMPANZEE; CODON; CONTROLLED STUDY; DNA DETERMINATION; FEMALE; GENE EXPRESSION; HUMAN; HUMAN CELL; HUMAN CELL CULTURE; IMMUNOBLOTTING; IMMUNOFLUORESCENCE MICROSCOPY; INTERMEDIATE FILAMENT; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN SYNTHESIS; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; TRANSLATION INITIATION; VERTEBRATE;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CODON, INITIATOR; HUMANS; LAMIN TYPE B; MOLECULAR SEQUENCE DATA; NUCLEAR LAMINA; NUCLEAR PROTEINS; SEQUENCE HOMOLOGY; TRANSFECTION; VERTEBRATES;

BOS TAURUS; PAN TROGLODYTES; VERTEBRATA;

EID: 33751060219     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.10.023     Document Type: Article

References (30)

1. Gotzmann J., and Foisner R. A-type lamin complexes and regenerative potential: a step towards understanding laminopathic diseases?. Histochem. Cell. Biol. 125 (2006) 33-41
2. Broers J.L., Ramaekers F.C., Bonne G., Yaou R.B., and Hutchison C.J. Nuclear lamins: laminopathies and their role in premature ageing. Physiol. Rev. 86 (2006) 967-1008
3. Gruenbaum Y., Margalit A., Goldman R.D., Shumaker D.K., and Wilson K.L. The nuclear lamina comes of age. Nat. Rev. Mol. Cell Biol. 6 (2005) 21-31
4. Herrmann H., and Aebi U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 73 (2004) 749-789
5. Gerace L., and Blobel G. The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell 19 (1980) 277-287
6. Fuchs E., and Weber K. Intermediate filaments: structure, dynamics, function, and disease. Annu. Rev. Biochem. 63 (1994) 345-382
7. Herrmann H., Hesse M., Reichenzeller M., Aebi U., and Magin T.M. Functional complexity of intermediate filament cytoskeletons: from structure to assembly to gene ablation. Int. Rev. Cytol. 223 (2003) 83-175
8. McKeon F.D., Kirschner M.W., and Caput D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature 319 (1986) 463-468
9. Fisher D.Z., Chaudhary N., and 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
10. Alsheimer M., and Benavente R. Change of karyoskeleton during mammalian spermatogenesis: expression pattern of nuclear lamin C2 and its regulation. Exp. Cell Res. 228 (1996) 181-188
11. Meier R., Muller P.R., Hirt A., Leibundgut K., Ridolfi-Luthy A., and Wagner H.P. Differential phosphorylation of lamin B2 in normal and leukemic cells. Leuk. Res. 21 (1997) 841-847
12. Spann T.P., Moir R.D., Goldman A.E., Stick R., and 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
13. Herrmann H., and Wiche G. Specific in situ phosphorylation of plectin in detergent-resistant cytoskeletons from cultured Chinese hamster ovary cells. J. Biol. Chem. 258 (1983) 14610-14618
14. Hoger T.H., Zatloukal K., Waizenegger I., and 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 99 (1990) 379-390
15. Strelkov S.V., Schumacher J., Burkhard P., Aebi U., and Herrmann H. Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins. J. Mol. Biol. 343 (2004) 1067-1080
16. Franke W.W., Schiller D.L., Moll R., Winter S., Schmid E., Engelbrecht I., Denk H., Krepler R., and Platzer B. Diversity of cytokeratins. Differentiation specific expression of cytokeratin polypeptides in epithelial cells and tissues. J. Mol. Biol. 153 (1981) 933-959
17. Hofmann I., Schnolzer M., Kaufmann I., and Franke W.W. Symplekin, a constitutive protein of karyo- and cytoplasmic particles involved in mRNA biogenesis in Xenopus laevis oocytes. Mol. Biol. Cell 13 (2002) 1665-1676
18. Ramaekers F.C., Boomkens T.R., and Bloemendal H. Cytoskeletal and contractile structures in bovine lens cell differentiation. Exp. Cell Res. 135 (1981) 454-461
19. Reichenzeller M., Burzlaff A., Lichter P., and Herrmann H. In vivo observation of a nuclear channel-like system: evidence for a distinct interchromosomal domain compartment in interphase cells. J. Struct. Biol. 129 (2000) 175-185
20. Lourim D., and Krohne G. Membrane-associated lamins in Xenopus egg extracts: identification of two vesicle populations. J. Cell Biol. 123 (1993) 501-512
21. Kaufmann E., Geisler N., and Weber K. SDS-PAGE strongly overestimates the molecular masses of the neurofilament proteins. FEBS Lett. 170 (1984) 81-84
22. Herrmann H., Dalton J.M., and Wiche G. Microheterogeneity of microtubule-associated proteins, MAP-1 and MAP-2, and differential phosphorylation of individual subcomponents. J. Biol. Chem. 260 (1985) 5797-5803
23. Biamonti G., Giacca M., Perini G., Contreas G., Zentilin L., Weighardt F., Guerra M., Della Valle G., Saccone S., Riva S., et al. The gene for a novel human lamin maps at a highly transcribed locus of chromosome 19 which replicates at the onset of S-phase. Mol. Cell Biol. 12 (1992) 3499-3506
24. Zewe M., Höger T.H., Fink T., Lichter P., Krohne G., and Franke W.W. Gene structure and chromosomal localization of the murine laminB2 gene. Eur. J. Cell Biol. 56 (1991) 342-350
25. Lees J.F., Shneidman P.S., Skuntz S.F., Carden M.J., and Lazzarini R.A. The structure and organization of the human heavy neurofilament subunit (NF-H) and the gene encoding it. EMBO J. 7 (1988) 1947-1955
26. Lehner C.F., Kurer V., Eppenberger H.M., and Nigg E.A. The nuclear lamin protein family in higher vertebrates. Identification of quantitatively minor lamin proteins by monoclonal antibodies. J. Biol. Chem. 261 (1986) 13293-13301
27. Mattout A., Dechat T., Adam S.A., Goldman R.D., and Gruenbaum Y. Nuclear lamins, diseases and aging. Curr. Opin. Cell Biol. 18 (2006) 335-341
28. Hegele R.A., Cao H., Liu D.M., Costain G.A., Charlton-Menys V., Rodger N.W., and Durrington P.N. Sequencing of the reannotated LMNB2 gene reveals novel mutations in patients with acquired partial lipodystrophy. Am. J. Hum. Genet. 79 (2006) 383-389
29. Landry J.R., Mager D.L., and Wilhelm B.T. Complex controls: the role of alternative promoters in mammalian genomes. Trends Genet. 19 (2003) 640-648
30. Paixao S., Colaluca I.N., Cubells M., Peverali F.A., Destro A., Giadrossi S., Giacca M., Falaschi A., Riva S., and Biamonti G. Modular structure of the human lamin B2 replicator. Mol. Cell Biol. 24 (2004) 2958-2967