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. 1985 May 1;100(5):1408–1414. doi: 10.1083/jcb.100.5.1408

Lateral diffusion in nuclear membranes

PMCID: PMC2113861  PMID: 3988794

Abstract

Chemical modification of rat liver nuclei with citraconic anhydride selectively removed outer nuclear membrane. This conclusion was based on (a) transmission electron microscopy, (b) lipid analysis, (c) lamin B as an inner membrane-associated marker, and (d) the demonstration of phospholipid lateral mobility on outer membrane-depleted nuclei as a criteria for inner membrane integrity. Addition of urea or N- ethylmaleimide resulted in the additional disruption of inner membrane. Fluorescence photobleaching was used to determine the long range (greater than 4 microns) lateral transport of lectin receptors and a phospholipid analog in both membranes. The diffusion coefficient for wheat germ agglutinin on whole nuclei was 3.9 X 10(-10) cm2/s whereas the diffusion coefficient for wheat germ agglutinin in outer membrane- depleted nuclei was less than or equal to 10(-12) cm2/s. Phospholipid mobilities were the same in whole and outer membrane-depleted nuclei (3.8 X 10(-9) cm2/s). The protein diffusion differences observed between whole and outer membrane-depleted nuclei may be interpreted in the context of two functionally different membrane systems that compose the double bilayer of the nucleus.

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Selected References

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  1. AMES B. N., DUBIN D. T. The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J Biol Chem. 1960 Mar;235:769–775. [PubMed] [Google Scholar]
  2. Aaronson R. P., Blobel G. On the attachment of the nuclear pore complex. J Cell Biol. 1974 Sep;62(3):746–754. doi: 10.1083/jcb.62.3.746. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. GURR M. I., FINEAN J. B., HAWTHORNE J. N. THE PHOSPHOLIPIDS OF LIVER-CELL FRACTIONS. I. THE PHOSPHOLIPID COMPOSITION OF THE LIVER-CELL NUCLEUS. Biochim Biophys Acta. 1963 Aug 27;70:406–416. doi: 10.1016/0006-3002(63)90770-4. [DOI] [PubMed] [Google Scholar]
  4. Gerace L., Blobel G. Nuclear lamina and the structural organization of the nuclear envelope. Cold Spring Harb Symp Quant Biol. 1982;46(Pt 2):967–978. doi: 10.1101/sqb.1982.046.01.090. [DOI] [PubMed] [Google Scholar]
  5. Gerace L., Ottaviano Y., Kondor-Koch C. Identification of a major polypeptide of the nuclear pore complex. J Cell Biol. 1982 Dec;95(3):826–837. doi: 10.1083/jcb.95.3.826. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gertler A. Selective, reversible loss of elastolytic activity of elastase and subtilisin resulting from electrostatic changes due to maleylation. Eur J Biochem. 1971 Nov 11;23(1):36–40. doi: 10.1111/j.1432-1033.1971.tb01589.x. [DOI] [PubMed] [Google Scholar]
  7. Jones N. C., Osborn M. J. Interaction of Salmonella typhimurium with phospholipid vesicles. Incorporation of exogenous lipids into intact cells. J Biol Chem. 1977 Oct 25;252(20):7398–7404. [PubMed] [Google Scholar]
  8. Kaufmann S. H., Gibson W., Shaper J. H. Characterization of the major polypeptides of the rat liver nuclear envelope. J Biol Chem. 1983 Feb 25;258(4):2710–2719. [PubMed] [Google Scholar]
  9. Kay R. R., Fraser D., Johnston I. R. A method for the rapid isolation of nuclear membranes from rat liver. Characterisation of the membrane preparation and its associated DNA polymerase. Eur J Biochem. 1972 Oct 17;30(1):145–154. doi: 10.1111/j.1432-1033.1972.tb02081.x. [DOI] [PubMed] [Google Scholar]
  10. Kirschner R. H., Rusli M., Martin T. E. Characterization of the nuclear envelope, pore complexes, and dense lamina of mouse liver nuclei by high resolution scanning electron microscopy. J Cell Biol. 1977 Jan;72(1):118–132. doi: 10.1083/jcb.72.1.118. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Koppel D. E., Sheetz M. P., Schindler M. Lateral diffusion in biological membranes. A normal-mode analysis of diffusion on a spherical surface. Biophys J. 1980 Apr;30(1):187–192. doi: 10.1016/S0006-3495(80)85087-9. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Koppel D. E., Sheetz M. P., Schindler M. Matrix control of protein diffusion in biological membranes. Proc Natl Acad Sci U S A. 1981 Jun;78(6):3576–3580. doi: 10.1073/pnas.78.6.3576. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lam K. S., Kasper C. B. Electrophoretic analysis of three major nuclear envelope polypeptides. Topological relationship and sequence homology. J Biol Chem. 1979 Nov 25;254(22):11713–11720. [PubMed] [Google Scholar]
  14. Miller T. E., Huang C. Y., Pogo A. O. Rat liver nuclear skeleton and ribonucleoprotein complexes containing HnRNA. J Cell Biol. 1978 Mar;76(3):675–691. doi: 10.1083/jcb.76.3.675. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Moldow C. F., Zucker-Franklin D., Gordon A., Hospelhorn V., Silber R. Studies on the succinylation of erythrocyte membranes. Biochim Biophys Acta. 1972 Jan 17;255(1):133–148. doi: 10.1016/0005-2736(72)90015-6. [DOI] [PubMed] [Google Scholar]
  16. Schatten G., Thoman M. Nuclear surface complex as observed with the high resolution scanning electron microscope. Visualization of the membrane surfaces of the neclear envelope and the nuclear cortex from Xenopus laevis oocytes. J Cell Biol. 1978 May;77(2):517–535. doi: 10.1083/jcb.77.2.517. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Schindler M. Alterations in nuclear anatomy by chemical modification of proteins in isolated rat liver nuclei. Exp Cell Res. 1984 Jan;150(1):84–96. doi: 10.1016/0014-4827(84)90704-3. [DOI] [PubMed] [Google Scholar]
  18. Schindler M., Rosenbusch J. P. Chemical modification of matrix porin from Escherichia coli: probing the pore topology of a transmembrane protein. J Cell Biol. 1982 Mar;92(3):742–746. doi: 10.1083/jcb.92.3.742. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Schlessinger J., Elson E. L., Webb W. W., Yahara I., Rutishauser U., Edelman G. M. Receptor diffusion on cell surfaces modulated by locally bound concanavalin A. Proc Natl Acad Sci U S A. 1977 Mar;74(3):1110–1114. doi: 10.1073/pnas.74.3.1110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Seyfred M. A., Wells W. W. Subcellular incorporation of 32P into phosphoinositides and other phospholipids in isolated hepatocytes. J Biol Chem. 1984 Jun 25;259(12):7659–7665. [PubMed] [Google Scholar]
  21. Shaper J. H., Pardoll D. M., Kaufmann S. H., Barrack E. R., Vogelstein B., Coffey D. S. The relationship of the nuclear matrix to cellular structure and function. Adv Enzyme Regul. 1978;17:213–248. doi: 10.1016/0065-2571(79)90015-3. [DOI] [PubMed] [Google Scholar]
  22. Smith S. J., Adams H. R., Smetana K., Busch H. Isolation of the outer layer of the nuclear envelope. Composition of the RNA. Exp Cell Res. 1969 May;55(2):185–197. doi: 10.1016/0014-4827(69)90480-7. [DOI] [PubMed] [Google Scholar]
  23. Steck T. L., Yu J. Selective solubilization of proteins from red blood cell membranes by protein perturbants. J Supramol Struct. 1973;1(3):220–232. doi: 10.1002/jss.400010307. [DOI] [PubMed] [Google Scholar]

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