The molecular architecture of the nuclear pore complex (original) (raw)

• Lim, R. Y. & Fahrenkrog, B. The nuclear pore complex up close. Curr. Opin. Cell Biol. 18, 342–347 (2006)
  Article CAS PubMed Google Scholar
• Macara, I. G. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65, 570–594 (2001)
  Article CAS PubMed PubMed Central Google Scholar
• Weis, K. Nucleocytoplasmic transport: cargo trafficking across the border. Curr. Opin. Cell Biol. 14, 328–335 (2002)
  Article CAS PubMed Google Scholar
• Hetzer, M., Walther, T. C. & Mattaj, I. W. Pushing the envelope: Structure, function, and dynamics of the nuclear periphery. Annu. Rev. Cell Dev. Biol. 21, 347–380 (2005)
  Article CAS PubMed Google Scholar
• Tran, E. J. & Wente, S. R. Dynamic nuclear pore complexes: life on the edge. Cell 125, 1041–1053 (2006)
  Article CAS PubMed Google Scholar
• Rout, M. P. et al. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148, 635–651 (2000)
  Article CAS PubMed PubMed Central Google Scholar
• Cronshaw, J. M., Krutchinsky, A. N., Zhang, W., Chait, B. T. & Matunis, M. J. Proteomic analysis of the mammalian nuclear pore complex. J. Cell Biol. 158, 915–927 (2002)
  Article CAS PubMed PubMed Central Google Scholar
• Akey, C. W. & Radermacher, M. Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 122, 1–19 (1993)
  Article CAS PubMed Google Scholar
• Beck, M. et al. Nuclear pore complex structure and dynamics revealed by cryoelectron tomography. Science 306, 1387–1390 (2004)
  Article CAS PubMed ADS Google Scholar
• Hinshaw, J. E., Carragher, B. O. & Milligan, R. A. Architecture and design of the nuclear pore complex. Cell 69, 1133–1141 (1992)
  Article CAS PubMed Google Scholar
• Kiseleva, E. et al. Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments. J. Struct. Biol. 145, 272–288 (2004)
  Article CAS PubMed Google Scholar
• Stoffler, D. et al. Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport. J. Mol. Biol. 328, 119–130 (2003)
  Article CAS PubMed Google Scholar
• Yang, Q., Rout, M. P. & Akey, C. W. Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. Mol. Cell 1, 223–234 (1998)
  Article CAS PubMed Google Scholar
• Alber, F. et al. Determining the architectures of macromolecular assemblies. Nature doi: 10.1038/nature06404 (this issue).
• Krull, S., Thyberg, J., Bjorkroth, B., Rackwitz, H. R. & Cordes, V. C. Nucleoporins as components of the nuclear pore complex core structure and Tpr as the architectural element of the nuclear basket. Mol. Biol. Cell 15, 4261–4277 (2004)
  Article CAS PubMed PubMed Central Google Scholar
• Pante, N. & Kann, M. Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm. Mol. Biol. Cell 13, 425–434 (2002)
  Article CAS PubMed PubMed Central Google Scholar
• Devos, D. et al. Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PLoS Biol. 2, e380 (2004)
  Article PubMed PubMed Central CAS Google Scholar
• Devos, D. et al. Simple fold composition and modular architecture of the nuclear pore complex. Proc. Natl Acad. Sci. USA 103, 2172–2177 (2006)
  Article CAS PubMed PubMed Central ADS Google Scholar
• Fotin, A. et al. Molecular model for a complete clathrin lattice from electron cryomicroscopy. Nature 432, 573–579 (2004)
  Article CAS PubMed ADS Google Scholar
• Stagg, S. M. et al. Structure of the Sec13/31 COPII coat cage. Nature 439, 234–238 (2006)
  Article CAS PubMed ADS Google Scholar
• ter Haar, E., Musacchio, A., Harrison, S. C. & Kirchhausen, T. Atomic structure of clathrin: a β propeller terminal domain joins an α zigzag linker. Cell 95, 563–573 (1998)
  Article CAS PubMed PubMed Central Google Scholar
• Dokudovskaya, S. et al. Protease accessibility laddering: a proteomic tool for probing protein structure. Structure 14, 653–660 (2006)
  Article CAS PubMed Google Scholar
• Fath, S., Mancias, J. D., Bi, X. & Goldberg, J. Structure and organization of coat proteins in the COPII cage. Cell 129, 1325–1336 (2007)
  Article CAS PubMed Google Scholar
• Antonin, W. & Mattaj, I. W. Nuclear pore complexes: round the bend? Nature Cell Biol. 7, 10–12 (2005)
  Article CAS PubMed Google Scholar
• Drin, G. et al. A general amphipathic α-helical motif for sensing membrane curvature. Nature Struct. Mol. Biol. 14, 138–146 (2007)
  Article CAS Google Scholar
• Conti, E., Muller, C. W. & Stewart, M. Karyopherin flexibility in nucleocytoplasmic transport. Curr. Opin. Struct. Biol. 16, 237–244 (2006)
  Article CAS PubMed Google Scholar
• Akey, C. W. Structural plasticity of the nuclear pore complex. J. Mol. Biol. 248, 273–293 (1995)
  CAS PubMed Google Scholar
• Hinshaw, J. E. & Milligan, R. A. Nuclear pore complexes exceeding eightfold rotational symmetry. J. Struct. Biol. 141, 259–268 (2003)
  Article CAS PubMed Google Scholar
• Bryant, D. M. & Stow, J. L. The ins and outs of E-cadherin trafficking. Trends Cell Biol. 14, 427–434 (2004)
  Article CAS PubMed Google Scholar
• Strawn, L. A., Shen, T., Shulga, N., Goldfarb, D. S. & Wente, S. R. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nature Cell Biol. 6, 197–206 (2004)
  Article CAS PubMed Google Scholar
• Rout, M. P., Aitchison, J. D., Magnasco, M. O. & Chait, B. T. Virtual gating and nuclear transport: the hole picture. Trends Cell Biol. 13, 622–628 (2003)
  Article CAS PubMed Google Scholar
• Denning, D. P., Patel, S. S., Uversky, V., Fink, A. L. & Rexach, M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc. Natl Acad. Sci. USA 100, 2450–2455 (2003)
  Article CAS PubMed PubMed Central ADS Google Scholar
• Liu, S. M. & Stewart, M. Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p. J. Mol. Biol. 349, 515–525 (2005)
  Article CAS PubMed Google Scholar
• Peters, R. Translocation through the nuclear pore complex: selectivity and speed by reduction-of-dimensionality. Traffic 6, 421–427 (2005)
  Article CAS PubMed Google Scholar
• Ribbeck, K. & Gorlich, D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 20, 1320–1330 (2001)
  Article CAS PubMed PubMed Central Google Scholar
• Isgro, T. A. & Schulten, K. Binding dynamics of isolated nucleoporin repeat regions to importin-β. Structure 13, 1869–1879 (2005)
  Article CAS PubMed Google Scholar
• Isgro, T. A. & Schulten, K. Association of nuclear pore FG-repeat domains to NTF2 import and export complexes. J. Mol. Biol. 366, 330–345 (2007)
  Article CAS PubMed Google Scholar
• Stewart, M. Molecular mechanism of the nuclear protein import cycle. Nature Rev. Mol. Cell Biol. 8, 195–208 (2007)
  Article CAS Google Scholar
• Zilman, A., Di Talia, S., Chait, B. T., Rout, M. P. & Magnasco, M. O. Efficiency, selectivity, and robustness of nucleocytoplasmic transport. PLoS Comput. Biol. 3, e125 (2007)
  Article PubMed PubMed Central ADS CAS Google Scholar
• Paulillo, S. M. et al. Nucleoporin domain topology is linked to the transport status of the nuclear pore complex. J. Mol. Biol. 351, 784–798 (2005)
  Article CAS PubMed Google Scholar
• Lim, R. Y. et al. Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Proc. Natl Acad. Sci. USA 103, 9512–9517 (2006)
  Article CAS PubMed PubMed Central ADS Google Scholar
• Hawryluk-Gara, L. A., Shibuya, E. K. & Wozniak, R. W. Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Mol. Biol. Cell 16, 2382–2394 (2005)
  Article CAS PubMed PubMed Central Google Scholar
• King, M. C., Lusk, C. P. & Blobel, G. Karyopherin-mediated import of integral inner nuclear membrane proteins. Nature 442, 1003–1007 (2006)
  Article CAS PubMed ADS Google Scholar
• Saksena, S., Summers, M. D., Burks, J. K., Johnson, A. E. & Braunagel, S. C. Importin-α-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope. Nature Struct. Mol. Biol. 13, 500–508 (2006)
  Article CAS Google Scholar
• Aitchison, J. D., Rout, M. P., Marelli, M., Blobel, G. & Wozniak, R. W. Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p. J. Cell Biol. 131, 1133–1148 (1995)
  Article CAS PubMed Google Scholar
• Marelli, M., Aitchison, J. D. & Wozniak, R. W. Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p. J. Cell Biol. 143, 1813–1830 (1998)
  Article CAS PubMed PubMed Central Google Scholar
• Siniossoglou, S. et al. A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 84, 265–275 (1996)
  Article CAS PubMed Google Scholar
• Wente, S. R., Rout, M. P. & Blobel, G. A new family of yeast nuclear pore complex proteins. J. Cell Biol. 119, 705–723 (1992)
  Article CAS PubMed Google Scholar
• Unwin, P. N. & Milligan, R. A. A large particle associated with the perimeter of the nuclear pore complex. J. Cell Biol. 93, 63–75 (1982)
  Article CAS PubMed Google Scholar
• Scannell, D. R., Butler, G. & Wolfe, K. H. Yeast genome evolution-the origin of the species. Yeast (in the press)
• Schledzewski, K., Brinkmann, H. & Mendel, R. R. Phylogenetic analysis of components of the eukaryotic vesicle transport system reveals a common origin of adaptor protein complexes 1, 2, and 3 and the F subcomplex of the coatomer COPI. J. Mol. Evol. 48, 770–778 (1999)
  Article CAS PubMed ADS Google Scholar
• Grandi, P. et al. A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p. J. Cell Biol. 130, 1263–1273 (1995)
  Article CAS PubMed Google Scholar
• Belgareh, N. et al. Functional characterization of a Nup159p-containing nuclear pore subcomplex. Mol. Biol. Cell 9, 3475–3492 (1998)
  Article CAS PubMed PubMed Central Google Scholar
• Bailer, S. M. et al. Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex. J. Biol. Chem. 275, 23540–23548 (2000)
  Article CAS PubMed Google Scholar
• Bailer, S. M., Balduf, C. & Hurt, E. The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport. Mol. Cell. Biol. 21, 7944–7955 (2001)
  Article CAS PubMed PubMed Central Google Scholar
• Pettersen, E. F. et al. UCSF Chimera–a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605–1612 (2004)
  Article CAS PubMed Google Scholar
• Soding, J., Biegert, A. & Lupas, A. N. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res. 33, W244–W248 (2005)
  Article PubMed PubMed Central CAS Google Scholar