Field, M. C. & Dacks, J. B.
First and last ancestors: reconstructing evolution of the endomembrane system with ESCRTs, vesicle coat proteins, and nuclear pore complexes. Curr. Opin. Cell Biol.
21, 4–13 (2009).
Brickner, J. H.
Transcriptional memory at the nuclear periphery. Curr. Opin. Cell Biol.
21, 127–133 (2009).
Towbin, B. D., Meister, P. & Gasser, S. M.
The nuclear envelope — a scaffold for silencing?
Curr. Opin. Genet. Dev.
19, 180–186 (2009).
Degrasse, J. A.
et al. Evidence for a shared nuclear pore complex architecture that is conserved from the last common eukaryotic ancestor. Mol. Cell. Proteomics
8, 2119–2130 (2009). Proteomic analyses of NPC-containing fractions from a divergent eukaryote (Trypanosoma brucei) provide conclusive evidence that the general blueprint of NPC architecture was already established in the last common eukaryotic ancestor.
Suntharalingam, M. & Wente, S. R.
Peering through the pore: nuclear pore complex structure, assembly, and function. Dev. Cell
4, 775–789 (2003).
Elad, N., Maimon, T., Frenkiel-Krispin, D., Lim, R. Y. & Medalia, O.
Structural analysis of the nuclear pore complex by integrated approaches. Curr. Opin. Struct. Biol.
19, 226–232 (2009).
et al. Determining the architectures of macromolecular assemblies. Nature
450, 683–694 (2007).
et al. The molecular architecture of the nuclear pore complex. Nature
450, 695–701 (2007). Together with reference 7, this work describes the development of a computational method that combines a diverse set of biophysical and proteomic data to construct a comprehensive medium resolution three-dimensional map describing the relative arrangement of all components of the S. cerevisiae NPC.
Brohawn, S. G., Partridge, J. R., Whittle, J. R. & Schwartz, T. U.
The nuclear pore complex has entered the atomic age. Structure
17, 1156–1168 (2009).
Lutzmann, M., Kunze, R., Buerer, A., Aebi, U. & Hurt, E.
Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins. EMBO J.
21, 387–397 (2002).
D'Angelo, M. A., Anderson, D., Richard, E. & Hetzer, M.
Nuclear pores form de novo from both sides of the nuclear envelope. Science
312, 440–443 (2006).
et al. The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly. J. Cell Biol.
185, 459–473 (2009).
et al. Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PLoS Biol.
2, e380 (2004).
et al. Simple fold composition and modular architecture of the nuclear pore complex. Proc. Natl Acad. Sci. USA
103, 2172–2177 (2006).
Bonifacino, J. S. & Glick, B. S.
The mechanisms of vesicle budding and fusion. Cell
116, 153–166 (2004).
Köhler, A. & Hurt, E. C.
Exporting RNA from the nucleus to the cytoplasm. Nature Rev. Mol. Cell Biol.
8, 761–773 (2007).
Molecular mechanism of the nuclear protein import cycle. Nature Rev. Mol. Cell Biol.
8, 195–208 (2007).
Akey, C. W. & Goldfarb, D. S.
Protein import through the nuclear pore complex is a multistep process. J. Cell Biol.
109, 971–982 (1989).
Nachury, M. V. & Weis, K.
The direction of transport through the nuclear pore can be inverted. Proc. Natl Acad. Sci. USA
96, 9622–9627 (1999).
Kuersten, S., Ohno, M. & Mattaj, I. W.
Nucleocytoplasmic transport: Ran, beta and beyond. Trends Cell Biol.
11, 497–503 (2001).
Terry, L. J. & Wente, S. R.
Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport. Eukaryot. Cell
8, 1814–1827 (2009).
Radu, A., Moore, M. S. & Blobel, G.
The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex. Cell
81, 215–222 (1995).
Bayliss, R., Littlewood, T. & Stewart, M.
Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking. Cell
102, 99–108 (2000).
Denning, D. P. & Rexach, M. F.
Rapid evolution exposes the boundaries of domain structure and function in natively unfolded FG nucleoporins. Mol. Cell. Proteomics
6, 272–282 (2007).
Rout, M. P.
et al. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol.
148, 635–651 (2000).
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). Mass spectrometry analysis defines the proteome of the mammalian NPC for the first time and paves the way for a more detailed characterization of NPC structure and function.
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).
Lim, R. Y.
et al. Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Proc. Natl Acad. Sci. USA
103, 9512–9517 (2006).
Patel, S. S., Belmont, B. J., Sante, J. M. & Rexach, M. F.
Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell
129, 83–96 (2007).
et al. Artificial nanopores that mimic the transport selectivity of the nuclear pore complex. Nature
457, 1023–1027 (2009).
Akey, C. W.
Visualization of transport-related configurations of the nuclear pore transporter. Biophys. J.
58, 341–355 (1990).
Rexach, M. & Blobel, G.
Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell
83, 683–692 (1995).
Ben-Efraim, I. & Gerace, L.
Gradient of increasing affinity of importin β for nucleoporins along the pathway of nuclear import. J. Cell Biol.
152, 411–417 (2001).
Strawn, L. A., Shen, T., Shulga, N., Goldfarb, D. S. & Wente, S. R.
Minimal nuclear pore complexes define FG repeat domains essential for transport. Naure. Cell Biol.
6, 197–206 (2004).
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).
Translocation through the nuclear pore: Kaps pave the way. Bioessays
31, 466–477 (2009). Excellent introductory review describing current nuclear transport models in the light of the latest data obtained by single transporter recording, optical super-resolution microscopy and transport assays on artificial nanopores.
Lim, R. Y.
et al. Nanomechanical basis of selective gating by the nuclear pore complex. Science
318, 640–643 (2007).
Ribbeck, K. & Gorlich, D.
The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J.
21, 2664–2671 (2002).
Frey, S., Richter, R. P. & Görlich, D.
FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science
314, 815–817 (2006).
Frey, S. & Görlich, D.
A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell
130, 512–523 (2007).
Mohr, D., Frey, S., Fischer, T., Guttler, T. & Gorlich, D.
Characterisation of the passive permeability barrier of nuclear pore complexes. EMBO J.
28, 2541–2553 (2009).
et al. Amyloid-like interactions within nucleoporin FG hydrogels. Proc. Natl Acad. Sci. USA
107, 6281–6285 (2010).
Macara, I. G.
Transport into and out of the nucleus. Microbiol Mol. Biol. Rev.
65, 570–594 (2001).
Krishnan, V. V.
et al. Intramolecular cohesion of coils mediated by phenylalanine–glycine motifs in the natively unfolded domain of a nucleoporin. PLoS Comput. Biol.
4, e1000145 (2008).
Miao, L. & Schulten, K.
Transport-related structures and processes of the nuclear pore complex studied through molecular dynamics. Structure
17, 449–459 (2009).
et al. Simple kinetic relationships and nonspecific competition govern nuclear import rates in vivo. J. Cell Biol.
175, 579–593 (2006).
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).
Engelhardt, P. & Pusa, K.
Nuclear pore complexes: “press-stud” elements of chromosomes in pairing and control. Nature New Biol.
240, 163–166 (1972).
Gene gating: a hypothesis. Proc. Natl Acad. Sci. USA
82, 8527–8529 (1985). The first formulation of the hypothesis that NPCs serve as gene-gating organelles that are capable of interacting specifically with transcriptionally active portions of the genome.
Kehlenbach, R. H., Dickmanns, A., Kehlenbach, A., Guan, T. & Gerace, L.
A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export. J. Cell Biol.
145, 645–657 (1999).
et al. Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p. EMBO J.
18, 4332–4347 (1999).
et al. Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex. Nature Cell Biol.
9, 788–796 (2007).
Carmody, S. R. & Wente, S. R.
mRNA nuclear export at a glance. J. Cell Sci.
122, 1933–1937 (2009).
Minakhina, S., Myers, R., Druzhinina, M. & Steward, R.
Crosstalk between the actin cytoskeleton and Ran-mediated nuclear transport. BMC Cell Biol.
6, 32 (2005).
Hutten, S., Walde, S., Spillner, C., Hauber, J. & Kehlenbach, R. H.
The nuclear pore component Nup358 promotes transportin-dependent nuclear import. J. Cell Sci.
122, 1100–1110 (2009).
Ratcheting mRNA out of the nucleus. Mol. Cell
25, 327–330 (2007).
Wu, J., Matunis, M. J., Kraemer, D., Blobel, G. & Coutavas, E.
Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. J. Biol. Chem.
270, 14209–14213 (1995).
Matunis, M. J., Wu, J. & Blobel, G.
SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex. J. Cell Biol.
140, 499–509 (1998).
et al. In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies. Exp. Cell Res.
312, 1418–1430 (2006).
Reverter, D. & Lima, C. D.
Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature
435, 687–692 (2005).
Radtke, K., Döhner, K. & Sodeik, B.
Viral interactions with the cytoskeleton: a hitchhiker's guide to the cell. Cell. Microbiol
8, 387–400 (2006).
Roth, D. M., Moseley, G. W., Glover, D., Pouton, C. W. & Jans, D. A.
A microtubule-facilitated nuclear import pathway for cancer regulatory proteins. Traffic
8, 673–686 (2007).
Singer, R. H.
Highways for mRNA transport. Cell
134, 722–723 (2008).
Joseph, J. & Dasso, M.
The nucleoporin Nup358 associates with and regulates interphase microtubules. FEBS Lett.
582, 190–196 (2008).
Cho, K. I.
et al. RANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free system. EMBO Rep.
10, 480–486 (2009).
Three-dimensional imaging of cell ultrastructure with high resolution, low voltage SEM. Int. Phys. Conf. Ser.
98, 657–662 (1989).
Jarnik, M. & Aebi, U.
Toward a more complete 3-D structure of the nuclear pore complex. J. Struct. Biol.
107, 291–308 (1991).
Ris, H. & Malecki, M.
High-resolution field emission scanning electron microscope imaging of internal cell structures after Epon extraction from sections: a new approach to correlative ultrastructural and immunocytochemical studies. J. Struct. Biol.
111, 148–157 (1993).
Goldberg, M. W. & Allen, T. D.
High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores. J. Cell Biol.
119, 1429–1440 (1992). References 68 and 69 were among the first to provide clear structural evidence for the presence of a basket structure anchored to the nucleoplasmic face of the NPC and the existence of interconnecting fibrils spanning the distance between neighbouring nuclear pores, stretching both perpendicularly and in parallel to the nuclear envelope.
Stoffler, D., Goldie, K. N., Feja, B. & Aebi, U.
Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy. J. Mol. Biol.
287, 741–752 (1999).
Beck, M., Lucicc´, V., Förster, F., Baumeister, W. & Medalia, O.
Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature
449, 611–615 (2007).
et al. Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments. J. Struct. Biol.
145, 272–288 (2004).
A look at messenger RNP moving through the nuclear pore. Cell
88, 585–588 (1997).
Kiseleva, E., Goldberg, M. W., Allen, T. D. & Akey, C. W.
Active nuclear pore complexes in Chironomus: visualization of transporter configurations related to mRNP export. J. Cell Sci.
111, 223–236 (1998).
et al. Nup153 affects entry of messenger and ribosomal ribonucleoproteins into the nuclear basket during export. Mol. Biol. Cell
16, 5610–5620 (2005).
et al. Exclusion of mRNPs and ribosomal particles from a thin zone beneath the nuclear envelope revealed upon inhibition of transport. Exp. Cell Res.
316, 1028–1038 (2009). The nucleocytoplasmic transport of RNPs was examined by EM, revealing the presence of a basket-dependent 'exclusion-zone' lining the entire extent of the nuclear face of the nuclear envelope, which prevents unwanted macromolecules from encroaching on the nuclear transport channel.
et al. Protein Tpr is required for establishing nuclear pore-associated zones of heterochromatin exclusion. EMBO J.
29, 1659–1673 (2010). RNA interference experiments were combined with EM analyses to show that the basket component TPR is involved in forming NPC-associated heterochromatin exclusion zones along the nuclear surface of the nuclear envelope, thus preventing macromolecular structures from interfering with nuclear transport.
Byrd, D. A.
et al. Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex. J. Cell Biol.
127, 1515–1526 (1994).
Kuznetsov, N. V.
et al. The evolutionarily conserved single-copy gene for murine Tpr encodes one prevalent isoform in somatic cells and lacks paralogs in higher eukaryotes. Chromosoma
111, 236–255 (2002).
Zimowska, G., Aris, J. P. & Paddy, M. R.
A Drosophila Tpr protein homolog is localized both in the extrachromosomal channel network and to nuclear pore complexes. J. Cell Sci.
110, 927–944 (1997).
et al. Megator, an essential coiled-coil protein that localizes to the putative spindle matrix during mitosis in Drosophila. Mol. Biol. Cell
15, 4854–4865 (2004).
Strambio-de-Castillia, C., Blobel, G. & Rout, M. P.
Proteins connecting the nuclear pore complex with the nuclear interior. J. Cell Biol.
144, 839–855 (1999).
Frosst, P., Guan, T., Subauste, C., Hahn, K. & 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, 617–630 (2002).
Krull, S., Thyberg, J., Björkroth, 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).
Cordes, V. C., Reidenbach, S., Rackwitz, H. R. & Franke, W. W.
Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments. J. Cell Biol.
136, 515–529 (1997).
Hase, M. E., Kuznetsov, N. V. & Cordes, V. C.
Amino acid substitutions of coiled-coil protein Tpr abrogate anchorage to the nuclear pore complex but not parallel, in-register homodimerization. Mol. Biol. Cell
12, 2433–2452 (2001).
et al. Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1. Cell
116, 63–73 (2004).
Zhao, X., Wu, C. Y. & Blobel, G.
Mlp-dependent anchorage and stabilization of a desumoylating enzyme is required to prevent clonal lethality. J. Cell Biol.
167, 605–611 (2004).
Casolari, J. M., Brown, C. R., Drubin, D. A., Rando, O. J. & Silver, P. A.
Developmentally induced changes in transcriptional program alter spatial organization across chromosomes. Genes Dev.
19, 1188–1198 (2005). Changes in nuclear organization that follow stimulation of S. cerevisiae cells by mating pheromone were studied to show that the yeast TPR homologue, Mlp1, has a role in determining nuclear organization in response to a developmental cue.
Niepel, M., Strambio-de-Castillia, C., Fasolo, J., Chait, B. T. & Rout, M. P.
The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly. J. Cell Biol.
170, 225–235 (2005).
Vinciguerra, P., Iglesias, N., Camblong, J., Zenklusen, D. & Stutz, F.
Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export. EMBO J.
24, 813–823 (2005). Chromatin immunoprecipitation, FISH and pulse-chase experiments were used to show that yeast TPR-like proteins help recruit nascent transcripts to the NPC and have a role in coupling mRNA biogenesis with export through the NPC.
Lewis, A., Felberbaum, R. & Hochstrasser, M.
A nuclear envelope protein linking nuclear pore basket assembly, SUMO protease regulation, and mRNA surveillance. J. Cell Biol.
178, 813–827 (2007).
et al. Nucleoporins prevent DNA damage accumulation by modulating Ulp1-dependent sumoylation processes. Mol. Biol. Cell
18, 2912–2923 (2007).
Xu, X. M.
et al. NUCLEAR PORE ANCHOR, the Arabidopsis homolog of Tpr/Mlp1/Mlp2/megator, is involved in mRNA export and SUMO homeostasis and affects diverse aspects of plant development. Plant Cell
19, 1537–1548 (2007).
Lee, S. H., Sterling, H., Burlingame, A. & McCormick, F.
Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-mediated mitotic spindle checkpoint. Genes Dev.
22, 2926–2931 (2008).
De Souza, C. P., Hashmi, S. B., Nayak, T., Oakley, B. & Osmani, S. A.
Mlp1 acts as a mitotic scaffold to spatially regulate spindle assembly checkpoint proteins in Aspergillus nidulans. Mol. Biol. Cell
20, 2146–2159 (2009).
et al. Spatiotemporal control of mitosis by the conserved spindle matrix protein Megator. J. Cell Biol.
184, 647–657 (2009). Megator, the D. melanogaster homologue of human TPR, is shown here to specifically interact with SAC proteins, thus mediating normal mitotic duration and checkpoint response.
et al. An endoribonuclease functionally linked to perinuclear mRNP quality control associates with the nuclear pore complexes. PLoS Biol.
7, e8 (2009).
Tan-Wong, S. M., Wijayatilake, H. D. & Proudfoot, N. J.
Gene loops function to maintain transcriptional memory through interaction with the nuclear pore complex. Genes Dev.
23, 2610–2624 (2009).
et al. DNA zip codes control an ancient mechanism for gene targeting to the nuclear periphery. Nature Cell Biol.
12, 111–118 (2010). Identification of specific gene-recuitment sequences, which function as DNA zip codes to recruit inducible S. cerevisiae genes from the nucleoplasm to the NPC and are required for full transcriptional activation of a subset of genes involved in adaptation to varying environmental conditions.
Vaquerizas, J. M.
et al. Nuclear pore proteins Nup153 and Megator define transcriptionally active regions in the Drosophila genome. PLoS Genet.
6, e1000846 (2010). Using chromatin immunoprecipitation combined with microarray hybridization, it was shown that the NPC acts as a global gene regulator in D. melanogaster by interacting with Nup-associated regions of the genome and thereby promoting chromosomal organization and transcriptional control.
Vinciguerra, P. & Stutz, F.
mRNA export: an assembly line from genes to nuclear pores. Curr. Opin. Cell Biol.
16, 285–292 (2004).
Skaggs, H. S.
et al. HSF1-TPR interaction facilitates export of stress-induced HSP70 mRNA. J. Biol. Chem.
282, 33902–33907 (2007).
Fasken, M. B. & Corbett, A. H.
Mechanisms of nuclear mRNA quality control. RNA Biol.
6, 237–241 (2009).
Akhtar, A. & Gasser, S. M.
The nuclear envelope and transcriptional control. Nature Rev. Genet.
8, 507–517 (2007).
Chekanova, J. A., Abruzzi, K. C., Rosbash, M. & Belostotsky, D. A.
Sus1, Sac3, and Thp1 mediate post-transcriptional tethering of active genes to the nuclear rim as well as to non-nascent mRNP. RNA
14, 66–77 (2008).
Schmid, M. & Jensen, T. H.
Quality control of mRNP in the nucleus. Chromosoma
117, 419–429 (2008).
Schmid, M. & Jensen, T. H.
The exosome: a multipurpose RNA-decay machine. Trends Biochem. Sci.
33, 501–510 (2008).
et al. Proteomic analysis identifies a new complex required for nuclear pre-mRNA retention and splicing. EMBO J.
23, 4, 847–856 (2004).
et al. Comprehensive mapping of long-range interactions reveals folding principles of the human genome. Science
326, 289–293 (2009).
Andrulis, E. D., Neiman, A. M., Zappulla, D. C. & Sternglanz, R.
Perinuclear localization of chromatin facilitates transcriptional silencing. Nature
394, 592–595 (1998).
Kosak, S. T.
et al. Subnuclear compartmentalization of immunoglobulin loci during lymphocyte development. Science
296, 158–162 (2002).
Sexton, T., Schober, H., Fraser, P. & Gasser, S. M.
Gene regulation through nuclear organization. Nature Struct. Mol. Biol.
14, 1049–1055 (2007).
Dilworth, D. J.
et al. The mobile nucleoporin Nup2p and chromatin-bound Prp20p function in endogenous NPC-mediated transcriptional control. J. Cell Biol.
171, 955–965 (2005). Results obtained from proteomics, genomics and functional assays of boundary activity and epigenetic variegation suggest that the NPC plays an active part in chromatin organization by facilitating the transition of chromatin between activity states.
Dieppois, G., Iglesias, N. & Stutz, F.
Cotranscriptional recruitment to the mRNA export receptor Mex67p contributes to nuclear pore anchoring of activated genes. Mol. Cell. Biol.
26, 7, 858–870 (2006).
et al. Nup-PI: the nucleopore-promoter interaction of genes in yeast. Mol. Cell
21, 379–391 (2006).
et al. Nuclear pore association confers optimal expression levels for an inducible yeast gene. Nature
441, 774–778 (2006).
Brickner, D. G.
et al. H2A.Z-mediated localization of genes at the nuclear periphery confers epigenetic memory of previous transcriptional state. PLoS Biol.
5, e81 (2007).
Ishii, K., Arib, G., Lin, C., Van Houwe, G. & Laemmli, U. K.
Chromatin boundaries in budding yeast: the nuclear pore connection. Cell
109, 551–562 (2002). Genetic studies, immunolocalization, live imaging and chromatin immunoprecipitation experiments conducted on chromatin boundary activities identified in S. cerevisiae provided the initial evidence that tethering of genomic loci to the NPC can dramatically alter their epigenetic activity.
Brickner, J. H. & Walter, P.
Gene recruitment of the activated INO1 locus to the nuclear membrane. PLoS Biol.
2, e342 (2004).
Kundu, S., Horn, P. J. & Peterson, C. L.
SWI/SNF is required for transcriptional memory at the yeast GAL gene cluster. Genes Dev.
21, 997–1004 (2007).
Kundu, S. & Peterson, C. L.
Dominant role for signal transduction in transcriptional memory of yeast GAL genes. Mol. Cell. Biol.
30, 2330–2340 (2010).
et al. Nuclear pore association confers optimal expression levels for an inducible yeast gene. Nature
441, 774–778 (2006).
et al. SAGA interacting factors confine sub-diffusion of transcribed genes to the nuclear envelope. Nature
441, 770–773 (2006).
Kurshakova, M. M.
et al. SAGA and a novel Drosophila export complex anchor efficient transcription and mRNA export to NPC. EMBO J.
26, 4, 956–965 (2007).
et al. Actively transcribed GAL genes can be physically linked to the nuclear pore by the SAGA chromatin modifying complex. J. Biol. Chem.
282, 3042–3049 (2007).
Köhler, A., Schneider, M., Cabal, G. G., Nehrbass, U. & Hurt, E.
Yeast Ataxin-7 links histone deubiquitination with gene gating and mRNA export. Nature Cell Biol.
10, 707–715 (2008).
et al. THO/Sub2p functions to coordinate 3′-end processing with gene-nuclear pore association. Cell
135, 308–321 (2008).
et al. Sus1, Cdc31, and the Sac3 CID region form a conserved interaction platform that promotes nuclear pore association and mRNA export. Mol. Cell
33, 727–737 (2009).
et al. Mutational uncoupling of the role of Sus1 in nuclear pore complex targeting of an mRNA export complex and histone H2B deubiquitination. J. Biol. Chem.
284, 12049–12056 (2009).
Ellisdon, A. M., Jani, D., Kohler, A., Hurt, E. & Stewart, M.
Structural basis for the interaction between yeast Spt-Ada-Gcn5 acetyltransferase (SAGA) complex components Sgf11 and Sus1. J. Biol. Chem.
285, 3850–3856 (2010).
Hutchison, N. & Weintraub, H.
Localization of DNAase I-sensitive sequences to specific regions of interphase nuclei. Cell
43, 471–482 (1985).
Ragoczy, T., Bender, M. A., Telling, A., Byron, R. & Groudine, M.
The locus control region is required for association of the murine β-globin locus with engaged transcription factories during erythroid maturation. Genes Dev.
20, 1447–1457 (2006).
Donze, D. & Kamakaka, R. T.
Braking the silence: how heterochromatic gene repression is stopped in its tracks. Bioessays
24, 344–349 (2002).
et al. Chromatin-bound nuclear pore components regulate gene expression in higher eukaryotes. Cell
140, 372–383 (2010).
Kalverda, B., Pickersgill, H., Shloma, V. V. & Fornerod, M.
Nucleoporins directly stimulate expression of developmental and cell-cycle genes inside the nucleoplasm. Cell
140, 360–371 (2010).
et al. Telomere tethering at the nuclear periphery is essential for efficient DNA double strand break repair in subtelomeric region. J. Cell Biol.
172, 189–199 (2006).
Zhao, X. & Blobel, G.
A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proc. Natl Acad. Sci. USA
102, 4777–4782 (2005).
et al. Functional targeting of DNA damage to a nuclear pore-associated SUMO-dependent ubiquitin ligase. Science
322, 597–602 (2008).
Ii, T., Mullen, J. R., Slagle, C. E. & Brill, S. J.
Stimulation of in vitro sumoylation by Slx5-Slx8: evidence for a functional interaction with the SUMO pathway. DNA Repair
6, 1679–1691 (2007).
Oza, P. & Peterson, C. L.
Opening the DNA repair toolbox: localization of DNA double strand breaks to the nuclear periphery. Cell Cycle
9, 43–49 (2010).
et al. The DNA damage response at eroded telomeres and tethering to the nuclear pore complex. Nature Cell Biol.
11, 980–987 (2009). Single-cell analysis was used to show that double-stranded DNA breaks get recruited to the vicinity of the NPC where they can undergo specialized repair in an environment designed to favour chromatin stability.
Hanawalt, P. C.
Controlling the efficiency of excision repair. Mutat. Res.
485, 3–13 (2001).
et al. Genome-wide analysis of factors affecting transcription elongation and DNA repair: a new role for PAF and Ccr4-Not in transcription-coupled repair. PLoS Genet.
5, e1000364 (2009).
Zhang, L., Jones, K. & Gong, F.
The molecular basis of chromatin dynamics during nucleotide excision repair. Biochem. Cell Biol.
87, 265–272 (2009).
Faza, M. B.
et al. Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery. J. Cell Biol.
184, 833–846 (2009).
Fernandez-Martinez, J. & Rout, M. P.
Nuclear pore complex biogenesis. Curr. Opin. Cell Biol., 21, 603–612 (2009).
Guttinger, S., Laurell, E. & Kutay, U.
Orchestrating nuclear envelope disassembly and reassembly during mitosis. Nature Rev. Mol. Cell Biol.
10, 178–191 (2009).
Iouk, T., Kerscher, O., Scott, R. J., Basrai, M. A. & Wozniak, R. W.
The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint. J. Cell Biol.
159, 807–819 (2002).
Gillett, E. S., Espelin, C. W. & Sorger, P. K.
Spindle checkpoint proteins and chromosome-microtubule attachment in budding yeast. J. Cell Biol.
164, 535–546 (2004).
Scott, R. J., Lusk, C. P., Dilworth, D. J., Aitchison, J. D. & Wozniak, R. W.
Interactions between Mad1p and the nuclear transport machinery in the yeast Saccharomyces cerevisiae. Mol. Biol. Cell
16, 4362–4374 (2005).
Scott, R. J., Cairo, L. V., Van de Vosse, D. W. & Wozniak, R. W.
The nuclear export factor Xpo1p targets Mad1p to kinetochores in yeast. J. Cell Biol.
184, 21–29 (2009).
Katsani, K. R., Karess, R. E., Dostatni, N. & Doye, V.
In vivo dynamics of Drosophila nuclear envelope components. Mol. Biol. Cell
19, 3652–3666 (2008).
Nakano, H., Funasaka, T., Hashizume, C. & Wong, R. W.
Nucleoporin Tpr associates with dynein complex preventing chromosome lagging formation during mitosis. J. Biol. Chem.
285, 10841–10849 (2010).
Rao, C. V., Yamada, H. Y., Yao, Y. & Dai, W.
Enhanced genomic instabilities caused by deregulated microtubule dynamics and chromosome segregation: a perspective from genetic studies in mice. Carcinogenesis
30, 1469–1474 (2009).
Pemberton, L. F. & Paschal, B. M.
Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic
6, 187–198 (2005).
Tran, E. J., Bolger, T. A. & Wente, S. R.
SnapShot: nuclear transport. Cell
131, 420 (2007).
Cullen, B. R.
Viral RNAs: lessons from the enemy. Cell
136, 592–597 (2009).
Oza, P., Jaspersen, S. L., Miele, A., Dekker, J. & Peterson, C. L.
Mechanisms that regulate localization of a DNA double-strand break to the nuclear periphery. Genes Dev.
23, 912–927 (2009).
Schober, H., Ferreira, H., Kalck, V., Gehlen, L. R. & Gasser, S. M.
Yeast telomerase and the SUN domain protein Mps3 anchor telomeres and repress subtelomeric recombination. Genes Dev.
23, 928–938 (2009).
Jaspersen, S. L., Giddings, T. H. & Winey, M.
Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p. J. Cell Biol.
159, 945–956 (2002).
et al. SUN1 is required for telomere attachment to nuclear envelope and gametogenesis in mice. Dev. Cell
12, 863–872 (2007).
Gartenberg, M. R.
Life on the edge: telomeres and persistent DNA breaks converge at the nuclear periphery. Genes Dev.
23, 1027–1031 (2009).
et al. Functional association of Sun1 with nuclear pore complexes. J. Cell Biol.
178, 785–798 (2007).
Mekhail, K., Seebacher, J., Gygi, S. P. & Moazed, D.
Role for perinuclear chromosome tethering in maintenance of genome stability. Nature
456, 667–670 (2008).
Mans, B. J., Anantharaman, V., Aravind, L. & Koonin, E. V.
Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex. Cell Cycle
3, 1612–1637 (2004).
Grund, S. E.
et al. The inner nuclear membrane protein Src1 associates with subtelomeric genes and alters their regulated gene expression. J. Cell Biol.
182, 897–910 (2008).
Gonzalez-Barrera, S., Garcia-Rubio, M. & Aguilera, A.
Transcription and double-strand breaks induce similar mitotic recombination events in Saccharomyces cerevisiae. Genetics
162, 603–614 (2002).
Jimeno, S., Rondon, A. G., Luna, R. & Aguilera, A.
The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability. EMBO J.
21, 3526–3535 (2002).
Gaillard, H., Wellinger, R. E. & Aguilera, A.
A new connection of mRNP biogenesis and export with transcription-coupled repair. Nucleic Acids Res.
35, 3893–3906 (2007).
et al. Different physiological relevance of yeast THO/TREX subunits in gene expression and genome integrity. Mol. Genet. Genomics
279, 123–132 (2008).
Schneider, M., Noegel, A. A. & Karakesisoglou, I.
KASH-domain proteins and the cytoskeletal landscapes of the nuclear envelope. Biochem. Soc. Trans.
36, 1368–1372 (2008).
Kelly, S. M. & Corbett, A. H.
Messenger RNA export from the nucleus: a series of molecular wardrobe changes. Traffic
10, 1199–1208 (2009).
Luna, R., Gaillard, H., Gonzalez-Aguilera, C. & Aguilera, A.
Biogenesis of mRNPs: integrating different processes in the eukaryotic nucleus. Chromosoma
117, 319–331 (2008).
Hacker, S. & Krebber, H.
Differential export requirements for shuttling serine/arginine-type mRNA-binding proteins. J. Biol. Chem.
279, 5049–5052 (2004).
Iglesias, N. & Stutz, F.
Regulation of mRNP dynamics along the export pathway. FEBS Lett.
582, 1987–1996 (2008).