The nuclear pore complex up close

Current Opinion in Cell Biology

Volumn 18, Issue 3, 2006, Pages 342-347

  Lim, Roderick YH ^a   Fahrenkrog, Birthe ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOPORIN;

ATOMIC FORCE MICROSCOPY; CELL MEMBRANE TRANSPORT; CELL STRUCTURE; COMPLEX FORMATION; ELECTRON MICROSCOPY; ENVIRONMENTAL FACTOR; HUMAN; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR PORE COMPLEX; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN TRANSPORT; REVIEW; X RAY CRYSTALLOGRAPHY;

ACTIVE TRANSPORT, CELL NUCLEUS; ANIMALS; CRYOELECTRON MICROSCOPY; CRYSTALLOGRAPHY, X-RAY; KINETICS; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, FLUORESCENCE; NUCLEAR PORE; NUCLEAR PORE COMPLEX PROTEINS; PROTEIN STRUCTURE, TERTIARY; TANDEM REPEAT SEQUENCES;

EID: 33646519676     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2006.03.006     Document Type: Review

References (49)

1. Fahrenkrog B., and Aebi U. The nuclear pore complex: nucleocytoplasmic transport and beyond. Nat Rev Mol Cell Biol 4 (2003) 757-766
2. Fahrenkrog B., Koser J., and Aebi U. The nuclear pore complex: a jack of all trades?. Trends Biochem Sci 29 (2004) 175-182
3. Schwartz T.U. Modularity within the architecture of the nuclear pore complex. Curr Opin Struct Biol 15 (2005) 221-226
4. Weis K. Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell 112 (2003) 441-451
5. Stoffler D., Feja B., Fahrenkrog B., Walz J., Typke D., and Aebi U. Cryo-electron tomography provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport. J Mol Biol 328 (2003) 119-130
6. Beck M., Forster F., Ecke M., Plitzko J.M., Melchior F., Gerisch G., Baumeister W., and Medalia O. Nuclear pore complex structure and dynamics revealed by cryoelectron tomography. Science 306 (2004) 1387-1390. Cryoelectron tomography study of intact, transport-active NPCs, providing a resolution of ∼8 nm. Dynamic rearrangements of the central plug and the central framework of the NPC could be detected.
7. Loiodice I., Alves A., Rabut G., Van Overbeek M., Ellenberg J., Sibarita J.B., and Doye V. The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis. Mol Biol Cell 15 (2004) 3333-3344
8. Belgareh N., Rabut G., Bai S.W., van Overbeek M., Beaudouin J., Daigle N., Zatsepina O.V., Pasteau F., Labas V., Fromont-Racine M., et al. An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells. J Cell Biol 154 (2001) 1147-1160
9. Krull S., Thyberg J., Bjorkroth B., Rackwitz H.R., and 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 (2004) 4261-4277
10. Harel A., Orjalo A.V., Vincent T., Lachish-Zalait A., Vasu S., Shah S., Zimmerman E., Elbaum M., and Forbes D.J. Removal of a single pore subcomplex results in vertebrate nuclei devoid of nuclear pores. Mol Cell 11 (2003) 853-864
11. Walther T.C., Alves A., Pickersgill H., Loiodice I., Hetzer M., Galy V., Hulsmann B.B., Kocher T., Wilm M., Allen T., et al. The conserved Nup107-160 complex is critical for nuclear pore complex assembly. Cell 113 (2003) 195-206
12. Ribbeck K., and Gorlich D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J 20 (2001) 1320-1330
13. Ribbeck K., and Gorlich D. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J 21 (2002) 2664-2671
14. Macara I.G. Transport into and out of the nucleus. Microbiol Mol Biol Rev 65 (2001) 570-594
15. Antonin W., Franz C., Haselmann U., Antony C., and Mattaj I.W. The integral membrane nucleoporin pom121 functionally links nuclear pore complex assembly and nuclear envelope formation. Mol Cell 17 (2005) 83-92. In vitro NE assembly assays show that POM121 is essential for NE formation, whereas gp210 appears to be dispensable. POM121 function depends on the presence of the Nup107-160 complex, suggesting a link between NPC and NE formation.
16. Franz C., Askjaer P., Antonin W., Iglesias C.L., Haselmann U., Schelder M., de Marco A., Wilm M., Antony C., and Mattaj I.W. Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates. EMBO J 24 (2005) 3519-3531. This study provides evidence that Nup155 is required for the formation of the NE in vivo and in vitro and further underlines the link between the NPC and NE formation.
17. Lutzmann M., Kunze R., Stangl K., Stelter P., Toth K.F., Bottcher B., and Hurt E. Reconstitution of Nup157 and Nup145N into the Nup84 complex. J Biol Chem 280 (2005) 18442-18451
18. Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., and Forbes D.J. Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export. J Cell Biol 155 (2001) 339-354
19. Fahrenkrog B., Maco B., Fager A.M., Koser J., Sauder U., Ullman K.S., and Aebi U. Domain-specific antibodies reveal multiple-site topology of Nup153 within the nuclear pore complex. J Struct Biol 140 (2002) 254-267
20. Frosst P., Guan T., Subauste C., Hahn K., and Gerace L. Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export. J Cell Biol 156 (2002) 617-630
21. Hase M.E., and Cordes V.C. Direct interaction with nup153 mediates binding of Tpr to the periphery of the nuclear pore complex. Mol Biol Cell 14 (2003) 1923-1940
22. Rabut G., Doye V., and Ellenberg J. Mapping the dynamic organization of the nuclear pore complex inside single living cells. Nat Cell Biol 6 (2004) 1114-1121
23. Griffis E.R., Craige B., Dimaano C., Ullman K.S., and Powers M.A. Distinct functional domains within nucleoporins Nup153 and Nup98 mediate transcription-dependent mobility. Mol Biol Cell 15 (2004) 1991-2002
24. Paulillo S.M., Phillips E.M., Koser J., Sauder U., Ullman K.S., Powers M.A., and Fahrenkrog B. Nucleoporin domain topology is linked to the transport status of the nuclear pore complex. J Mol Biol 351 (2005) 784-798. In this study, the domain topology of the nucleoporin Nup214/CAN within the NPC is mapped by immuno-EM in Xenopus oocytes and human somatic cells. Furthermore, this study shows for the first time that the location of the FG-repeat domains of Nup153 and Nup214 is influenced by the transport activity at the NPC.
25. Smythe C., Jenkins H.E., and Hutchison C.J. Incorporation of the nuclear pore basket protein nup153 into nuclear pore structures is dependent upon lamina assembly: evidence from cell-free extracts of Xenopus eggs. EMBO J 19 (2000) 3918-3931
26. Conti E., and Izaurralde E. Nucleocytoplasmic transport enters the atomic age. Curr Opin Cell Biol 13 (2001) 310-319
27. Fukuhara N., Fernandez E., Ebert J., Conti E., and Svergun D. Conformational variability of nucleo-cytoplasmic transport factors. J Biol Chem 279 (2004) 2176-2181
28. Berke I.C., Boehmer T., Blobel G., and Schwartz T.U. Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex. J Cell Biol 167 (2004) 591-597. This study describes the crystal structure of the N-terminal domain of hNup133 as β-propeller fold and predicts other β-propellers in a third of all nucleoporins.
29. •], the N-terminal domain of Nup159p exhibits a β-propeller fold, supporting the notion that β-propellers are a common structural motif of distinct nucleoporins.
30. Devos D., Dokudovskaya S., Alber F., Williams R., Chait B.T., Sali A., and Rout M.P. Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PLoS Biol 2 (2004) e380. Computational and biochemical analysis of seven nucleoporins of the Nup84p complex predicts these nucleoporins to contain a β-propeller fold, a α-solenoid fold or a distinctive arrangement of both, similar to proteins found in vesicle-coating complexes. The roles of these structures in membrane curvature and NE closure are discussed.
31. Denning D.P., Patel S.S., Uversky V., Fink A.L., and Rexach M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc Natl Acad Sci USA 100 (2003) 2450-2455
32. Denning D.P., Uversky V., Patel S.S., Fink A.L., and Rexach M. The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. J Biol Chem 277 (2002) 33447-33455
33. Bayliss R., Littlewood T., and Stewart M. Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking. Cell 102 (2000) 99-108
34. Liu S.M., and Stewart M. Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p. J Mol Biol 349 (2005) 515-525. This study addresses for the first time the functional role of the hydrophilic linker regions that dominate the FG-repeat regions in nucleoporins. The crystal structure of the C-terminal region of Nup1p in complex with Kap95p documents that these linker regions are crucial to the affinity of the nucleoporin for Kap95p.
35. Matsuura Y., Lange A., Harreman M.T., Corbett A.H., and Stewart M. Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import. EMBO J 22 (2003) 5358-5369
36. Yang W., Gelles J., and Musser S.M. Imaging of single-molecule translocation through nuclear pore complexes. Proc Natl Acad Sci USA 101 (2004) 12887-12892. The nuclear import of a model cargo is studied by single-molecule fluorescence microscopy in permeabilized cells. Cargo translocation through the central pore of the NPC appears to be a random walk and exit from the central pore is the rate-limiting step.
37. Kubitscheck U., Grunwald D., Hoekstra A., Rohleder D., Kues T., Siebrasse J.P., and Peters R. Nuclear transport of single molecules: dwell times at the nuclear pore complex. J Cell Biol 168 (2005) 233-243. In this single-molecule fluorescence microscopy study, the position of two nucleoporins relative to each other is resolved in permeabilized cells. Furthermore, dwell times for nuclear transport receptors at the NPC are measured and show that translocation for receptors loaded with cargo is accelerated. The implications for nucleocytoplasmic transport are discussed.
38. Hoppener C., Siebrasse J.P., Peters R., Kubitscheck U., and Naber A. High-resolution near-field optical imaging of single nuclear pore complexes under physiological conditions. Biophys J 88 (2005) 3681-3688
39. Shahin V., Albermann L., Schillers H., Kastrup L., Schäfer C., Ludwig Y., Stock C., and Oberleithner H. Steroids dilate nuclear pores imaged with atomic force microscopy. J Cell Physiol 202 (2005) 591-601
40. Kastrup L., Oberleithner H., Ludwig Y., Schäfer C., and Shahin V. Nuclear envelope barrier leak induced by dexamethasone. J Cell Physiol 206 (2006) 428-434
41. Mooren O.L., Erickson E.S., Moore-Nichols D., and Dunn R.C. Nuclear side conformational changes in the nuclear pore complex following calcium release from the nuclear membrane. Phys Biol 1 (2004) 125-134
42. Lim R.Y., Aebi U., and Stoffler D. From the trap to the basket: getting to the bottom of the nuclear pore complex. Chromosoma 115 (2006) 15-26
43. Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., and Chait B.T. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol 148 (2000) 635-651
44. Strawn L.A., Shen T., Shulga N., Goldfarb D.S., and Wente S.R. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat Cell Biol 6 (2004) 197-206
45. Zeitler B., and Weis K. The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo. J Cell Biol 167 (2004) 583-590
46. Ribbeck K., and Gorlich D. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J 21 (2002) 2664-2671
47. Bickel T., and Bruinsma R. The nuclear pore complex mystery and anomalous diffusion in reversible gels. Biophys J 83 (2002) 3079-3087
48. Kustanovich T., and Rabin Y. Metastable network model of protein transport through nuclear pores. Biophys J 86 (2004) 2008-2016
49. ••] after the completion of the MD simulation.