Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Click Me!

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 3 November 2006:
Vol. 314. no. 5800, pp. 815 - 817
DOI: 10.1126/science.1132516

Reports

FG-Rich Repeats of Nuclear Pore Proteins Form a Three-Dimensional Meshwork with Hydrogel-Like Properties

Steffen Frey,1,2 Ralf P. Richter,3,4 Dirk Görlich1,2*

Nuclear pore complexes permit rapid passage of cargoes bound to nuclear transport receptors, but otherwise suppress nucleocytoplasmic fluxes of inert macromolecules ≥30 kilodaltons. To explain this selectivity, a sieve structure of the permeability barrier has been proposed that is created through reversible cross-linking between Phe and Gly (FG)–rich nucleoporin repeats. According to this model, nuclear transport receptors overcome the size limit of the sieve and catalyze their own nuclear pore-passage by a competitive disruption of adjacent inter-repeat contacts, which transiently opens adjoining meshes. Here, we found that phenylalanine-mediated inter-repeat interactions indeed cross-link FG-repeat domains into elastic and reversible hydrogels. Furthermore, we obtained evidence that such hydrogel formation is required for viability in yeast.

1 Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), INF 282, D-69120 Heidelberg, Germany.
2 Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, D-37077 Göttingen, Germany.
3 Institut für Physikalische Chemie, Universität Heidelberg, INF253, D-69120 Heidelberg, Germany.
4 Max-Planck-Institut für Metallforschung, Heisenbergstrasse 3, D-70569 Stuttgart, Germany.

* To whom correspondence should be addressed. E-mail: dg{at}zmbh.uni-heidelberg.de

Read the Full Text



THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Cells That Produce Deleterious Autoreactive Antibodies Are Vulnerable to Suicide.
H. Niu, D. T. M. Leung, C. H. Ma, E. C. Y. Law, F. C. H. Tam, and P.-L. Lim (2008)
J. Immunol. 181, 2246-2257
   Abstract »    Full Text »    PDF »
4Pi Microscopy of the Nuclear Pore Complex.
J. Huve, R. Wesselmann, M. Kahms, and R. Peters (2008)
Biophys. J. 95, 877-885
   Abstract »    Full Text »    PDF »
Genetic Analysis of the Caenorhabditis elegans GLH Family of P-Granule Proteins.
C. Spike, N. Meyer, E. Racen, A. Orsborn, J. Kirchner, K. Kuznicki, C. Yee, K. Bennett, and S. Strome (2008)
Genetics 178, 1973-1987
   Abstract »    Full Text »    PDF »
Discovering Novel Interactions at the Nuclear Pore Complex Using Bead Halo: A Rapid Method for Detecting Molecular Interactions of High and Low Affinity at Equilibrium.
S. S. Patel and M. F. Rexach (2008)
Mol. Cell. Proteomics 7, 121-131
   Abstract »    Full Text »    PDF »
Formation of a Tap/NXF1 Homotypic Complex Is Mediated through the Amino-Terminal Domain of Tap and Enhances Interaction with Nucleoporins.
L. H. Matzat, S. Berberoglu, and L. Levesque (2008)
Mol. Biol. Cell 19, 327-338
   Abstract »    Full Text »    PDF »
Crossing the Nuclear Envelope: Hierarchical Regulation of Nucleocytoplasmic Transport.
L. J. Terry, E. B. Shows, and S. R. Wente (2007)
Science 318, 1412-1416
   Abstract »    Full Text »    PDF »
Molecular Determinants of Binding between Gly-Leu-Phe-Gly Nucleoporins and the Nuclear Pore Complex.
G. A. Ratner, A. E. Hodel, and M. A. Powers (2007)
J. Biol. Chem. 282, 33968-33976
   Abstract »    Full Text »    PDF »
Functional Tat Transport of Unstructured, Small, Hydrophilic Proteins.
S. Richter, U. Lindenstrauss, C. Lucke, R. Bayliss, and T. Bruser (2007)
J. Biol. Chem. 282, 33257-33264
   Abstract »    Full Text »    PDF »
Nanomechanical Basis of Selective Gating by the Nuclear Pore Complex.
R. Y. H. Lim, B. Fahrenkrog, J. Koser, K. Schwarz-Herion, J. Deng, and U. Aebi (2007)
Science 318, 640-643
   Abstract »    Full Text »    PDF »
Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex.
L. J. Terry and S. R. Wente (2007)
J. Cell Biol. 178, 1121-1132
   Abstract »    Full Text »    PDF »
Mitosis, Not Just Open or Closed.
C. P. C. De Souza and S. A. Osmani (2007)
Eukaryot. Cell 6, 1521-1527
   Full Text »    PDF »
Multiple Conserved Domains of the Nucleoporin Nup124p and Its Orthologs Nup1p and Nup153 Are Critical for Nuclear Import and Activity of the Fission Yeast Tf1 Retrotransposon.
S. Sistla, J. V. Pang, C. X. Wang, and D. Balasundaram (2007)
Mol. Biol. Cell 18, 3692-3708
   Abstract »    Full Text »    PDF »
Distinct functions of the Drosophila Nup153 and Nup214 FG domains in nuclear protein transport.
N. Sabri, P. Roth, N. Xylourgidis, F. Sadeghifar, J. Adler, and C. Samakovlis (2007)
J. Cell Biol. 178, 557-565
   Abstract »    Full Text »    PDF »
Reversibility in nucleocytoplasmic transport.
R. B. Kopito and M. Elbaum (2007)
PNAS 104, 12743-12748
   Abstract »    Full Text »    PDF »
The Regulation of Nuclear Membrane Permeability by Ca2+ Signaling: A Tightly Regulated Pore or a Floodgate?.
K. Torok (2007)
Sci. STKE 2007, pe24
   Abstract »    Full Text »    PDF »
Gellular transport.
W. A. Wells (2006)
J. Cell Biol. 175, 678
   Full Text »    PDF »



ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)