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. 1986 Aug 15;238(1):305–308. doi: 10.1042/bj2380305

Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins.

D A Parry, J F Conway, P M Steinert
PMCID: PMC1147131  PMID: 3800939

Abstract

Analysis of the amino acid sequences of lamins A and C has revealed that each chain has an almost continuous heptad-containing coiled-coil domain containing structural regularities in the linear disposition of the acidic and the basic residues. The data suggest that the lamin molecules are two-stranded ropes, that the two chains are parallel to one another and in axial register, and that the molecules aggregate in vivo through periodic ionic interactions. These results indicate that significant changes in stability of the nuclear envelope may be achieved between interphase and mitosis through changes in the degree of phosphorylation of the lamin proteins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Burke B., Gerace L. A cell free system to study reassembly of the nuclear envelope at the end of mitosis. Cell. 1986 Feb 28;44(4):639–652. doi: 10.1016/0092-8674(86)90273-4. [DOI] [PubMed] [Google Scholar]
  2. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
  3. Dwyer N., Blobel G. A modified procedure for the isolation of a pore complex-lamina fraction from rat liver nuclei. J Cell Biol. 1976 Sep;70(3):581–591. doi: 10.1083/jcb.70.3.581. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Garnier J., Osguthorpe D. J., Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol. 1978 Mar 25;120(1):97–120. doi: 10.1016/0022-2836(78)90297-8. [DOI] [PubMed] [Google Scholar]
  5. Geisler N., Kaufmann E., Weber K. Antiparallel orientation of the two double-stranded coiled-coils in the tetrameric protofilament unit of intermediate filaments. J Mol Biol. 1985 Mar 5;182(1):173–177. doi: 10.1016/0022-2836(85)90035-x. [DOI] [PubMed] [Google Scholar]
  6. Geisler N., Plessmann U., Weber K. The complete amino acid sequence of the major mammalian neurofilament protein (NF-L). FEBS Lett. 1985 Mar 25;182(2):475–478. doi: 10.1016/0014-5793(85)80357-4. [DOI] [PubMed] [Google Scholar]
  7. Geisler N., Weber K. The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins. EMBO J. 1982;1(12):1649–1656. doi: 10.1002/j.1460-2075.1982.tb01368.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gerace L., Blobel G. The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell. 1980 Jan;19(1):277–287. doi: 10.1016/0092-8674(80)90409-2. [DOI] [PubMed] [Google Scholar]
  9. Gerace L. Traffic control and structural proteins in the eukaryotic nucleus. Nature. 1985 Dec 12;318(6046):508–509. doi: 10.1038/318508a0. [DOI] [PubMed] [Google Scholar]
  10. Hanukoglu I., Fuchs E. The cDNA sequence of a Type II cytoskeletal keratin reveals constant and variable structural domains among keratins. Cell. 1983 Jul;33(3):915–924. doi: 10.1016/0092-8674(83)90034-x. [DOI] [PubMed] [Google Scholar]
  11. Lewis S. A., Balcarek J. M., Krek V., Shelanski M., Cowan N. J. Sequence of a cDNA clone encoding mouse glial fibrillary acidic protein: structural conservation of intermediate filaments. Proc Natl Acad Sci U S A. 1984 May;81(9):2743–2746. doi: 10.1073/pnas.81.9.2743. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Marchuk D., McCrohon S., Fuchs E. Remarkable conservation of structure among intermediate filament genes. Cell. 1984 Dec;39(3 Pt 2):491–498. doi: 10.1016/0092-8674(84)90456-2. [DOI] [PubMed] [Google Scholar]
  13. McKeon F. D., Kirschner M. W., Caput D. Homologies in both primary and secondary structure between nuclear envelope and intermediate filament proteins. Nature. 1986 Feb 6;319(6053):463–468. doi: 10.1038/319463a0. [DOI] [PubMed] [Google Scholar]
  14. Miake-Lye R., Kirschner M. W. Induction of early mitotic events in a cell-free system. Cell. 1985 May;41(1):165–175. doi: 10.1016/0092-8674(85)90071-6. [DOI] [PubMed] [Google Scholar]
  15. Quax-Jeuken Y. E., Quax W. J., Bloemendal H. Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence. Proc Natl Acad Sci U S A. 1983 Jun;80(12):3548–3552. doi: 10.1073/pnas.80.12.3548. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Shelton K. R., Higgins L. L., Cochran D. L., Ruffolo J. J., Jr, Egle P. M. Nuclear lamins of erythrocyte and liver. J Biol Chem. 1980 Nov 25;255(22):10978–10983. [PubMed] [Google Scholar]
  17. Steinert P. M., Parry D. A. Intermediate filaments: conformity and diversity of expression and structure. Annu Rev Cell Biol. 1985;1:41–65. doi: 10.1146/annurev.cb.01.110185.000353. [DOI] [PubMed] [Google Scholar]
  18. Steinert P. M., Steven A. C., Roop D. R. The molecular biology of intermediate filaments. Cell. 1985 Sep;42(2):411–420. doi: 10.1016/0092-8674(85)90098-4. [DOI] [PubMed] [Google Scholar]
  19. Steinert P. M., Steven A. C. Splitting hairs and other intermediate filaments. 1985 Aug 29-Sep 4Nature. 316(6031):767–767. doi: 10.1038/316767a0. [DOI] [PubMed] [Google Scholar]
  20. Weber K. Link between lamins and intermediate filaments. Nature. 1986 Apr 3;320(6061):402–402. doi: 10.1038/320401a0. [DOI] [PubMed] [Google Scholar]
  21. Zackroff R. V., Goldman A. E., Jones J. C., Steinert P. M., Goldman R. D. Isolation and characterization of keratin-like proteins from cultured cells with fibroblastic morphology. J Cell Biol. 1984 Apr;98(4):1231–1237. doi: 10.1083/jcb.98.4.1231. [DOI] [PMC free article] [PubMed] [Google Scholar]

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