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Artigos de revistas sobre o tema "Nuclear pore complex (NPCs)"

Autor: Grafiati

Publicado: 7 de dezembro de 2024

Última modificação: 19 de julho de 2025

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1

Rout, M. P., and G. Blobel. "Isolation of the yeast nuclear pore complex." Journal of Cell Biology 123, no. 4 (1993): 771–83. http://dx.doi.org/10.1083/jcb.123.4.771.

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Nuclear pore complexes (NPCs) have been isolated from the yeast Saccharomyces. Negative stain electron microscopy of the isolated NPCs and subsequent image reconstruction revealed the octagonal symmetry and many of the ultrastructural features characteristic of vertebrate NPCs. The overall dimensions of the yeast NPC, both in its isolated form as well as in situ, are smaller than its vertebrate counterpart. However, the diameter of the central structures are similar. The isolated yeast NPC has a sedimentation coefficient of approximately 310 S and an M(r) of approximately 66 MD. It retains all

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2

Hampoelz, Bernhard, Amparo Andres-Pons, Panagiotis Kastritis, and Martin Beck. "Structure and Assembly of the Nuclear Pore Complex." Annual Review of Biophysics 48, no. 1 (2019): 515–36. http://dx.doi.org/10.1146/annurev-biophys-052118-115308.

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Nuclear pore complexes (NPCs) mediate nucleocytoplasmic exchange. They are exceptionally large protein complexes that fuse the inner and outer nuclear membranes to form channels across the nuclear envelope. About 30 different protein components, termed nucleoporins, assemble in multiple copies into an intricate cylindrical architecture. Here, we review our current knowledge of the structure of nucleoporins and how those come together in situ. We delineate architectural principles on several hierarchical organization levels, including isoforms, posttranslational modifications, nucleoporins, and

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3

Reichelt, R., A. Holzenburg, E. L. Buhle, M. Jarnik, A. Engel, and U. Aebi. "Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components." Journal of Cell Biology 110, no. 4 (1990): 883–94. http://dx.doi.org/10.1083/jcb.110.4.883.

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Nuclear pore complexes (NPCs) prepared from Xenopus laevis oocyte nuclear envelopes were studied in "intact" form (i.e., unexposed to detergent) and after detergent treatment by a combination of conventional transmission electron microscopy (CTEM) and quantitative scanning transmission electron microscopy (STEM). In correlation-averaged CTEM pictures of negatively stained intact NPCs and of distinct NPC components (i.e., "rings," "spoke" complexes, and "plug-spoke" complexes), several fine structural features arranged with octagonal symmetry about a central axis could reproducibly be identifie

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4

Lyman, Susan K., and Larry Gerace. "Nuclear pore complexes: dynamics in unexpected places." Journal of Cell Biology 154, no. 1 (2001): 17–20. http://dx.doi.org/10.1083/jcb.200106071.

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In vivo studies on the dynamics of the nuclear pore complex (NPC) in yeast suggested that NPCs are highly mobile in the nuclear envelope. However, new evidence indicates that in mammalian cells NPCs are stably attached to a flexible lamina framework, but a peripheral component can exchange rapidly with an intranuclear pool.

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5

Akey, Christopher W., Ignacia Echeverria, Christna Ouch, et al. "Implications of a multiscale structure of the yeast Nuclear Pore Complex." Molecular Cell 83, no. 18 (2023): 3283–302. https://doi.org/10.5281/zenodo.8226857.

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Nuclear Pore Complexes (NPCs) direct the nucleocytoplasmic transport of macromolecules. Here we provide a composite multiscale structure of the yeast NPC based on improved 3D density maps from electron cryo-microscopy and AlphaFold2 atomic models. Key features of the inner and outer rings were integrated into a comprehensive model. We resolved flexible connectors that tie together the core scaffold, along with equatorial transmembrane complexes and a lumenal ring that anchor this channel within the pore membrane. The organization of the nuclear double outer ring reveals a common architecture t

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6

Allen, T. D., J. M. Cronshaw, S. Bagley, E. Kiseleva, and M. W. Goldberg. "The nuclear pore complex: mediator of translocation between nucleus and cytoplasm." Journal of Cell Science 113, no. 10 (2000): 1651–59. http://dx.doi.org/10.1242/jcs.113.10.1651.

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The enclosure of nuclear contents in eukaryotes means that cells require sites in the boundary that mediate exchange of material between nucleus and cytoplasm. These sites, termed nuclear pore complexes (NPCs), number 100–200 in yeast, a few thousand in mammalian cells and approximately 50 million in the giant nuclei of amphibian oocytes. NPCs are large (125 MDa) macromolecular complexes that comprise 50–100 different proteins in vertebrates. In spite of their size and complex structure, NPCs undergo complete breakdown and reformation at cell division. Transport through NPCs can be rapid (esti

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7

Makio, Tadashi, Leslie H. Stanton, Cheng-Chao Lin, David S. Goldfarb, Karsten Weis, and Richard W. Wozniak. "The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly." Journal of Cell Biology 185, no. 3 (2009): 459–73. http://dx.doi.org/10.1083/jcb.200810029.

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We have established that two homologous nucleoporins, Nup170p and Nup157p, play an essential role in the formation of nuclear pore complexes (NPCs) in Saccharomyces cerevisiae. By regulating their synthesis, we showed that the loss of these nucleoporins triggers a decrease in NPCs caused by a halt in new NPC assembly. Preexisting NPCs are ultimately lost by dilution as cells grow, causing the inhibition of nuclear transport and the loss of viability. Significantly, the loss of Nup170p/Nup157p had distinct effects on the assembly of different architectural components of the NPC. Nucleoporins (n

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8

Akey, C. W. "Interactions and structure of the nuclear pore complex revealed by cryo-electron microscopy." Journal of Cell Biology 109, no. 3 (1989): 955–70. http://dx.doi.org/10.1083/jcb.109.3.955.

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Nuclear pore complexes (NPCs) play a central role in mediating nucleocytoplasmic transport and exchange processes in eukaryotic cells. The arrangement and interactions of NPCs within amphibian nuclear envelopes have been studied using cryo-electron microscopy of unfixed and frozen hydrated specimens. The nuclear lamina in Necturus forms an orthogonal network with crossover distances which vary between 1,600 and 4,000 A and which may be related to the basic filament repeat of lamins. Furthermore, the NPCs are attached randomly within the confines of the lamin network, presumably by their nucleo

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9

Stavru, Fabrizia, Gitte Nautrup-Pedersen, Volker C. Cordes, and Dirk Görlich. "Nuclear pore complex assembly and maintenance in POM121- and gp210-deficient cells." Journal of Cell Biology 173, no. 4 (2006): 477–83. http://dx.doi.org/10.1083/jcb.200601002.

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So far, POM121 and gp210 are the only known anchoring sites of vertebrate nuclear pore complexes (NPCs) within the lipid bilayer of the nuclear envelope (NE) and, thus, are excellent candidates for initiating the NPC assembly process. Indeed, we demonstrate that POM121 can recruit several nucleoporins, such as Nup62 or Nup358, to ectopic assembly sites. It thus appears to act as a nucleation site for the assembly of NPC substructures. Nonetheless, we observed functional NPCs and intact NEs in severely POM121-depleted cells. Double knockdowns of gp210 and POM121 in HeLa cells, as well as deplet

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10

Dultz, Elisa, Matthias Wojtynek, Ohad Medalia, and Evgeny Onischenko. "The Nuclear Pore Complex: Birth, Life, and Death of a Cellular Behemoth." Cells 11, no. 9 (2022): 1456. http://dx.doi.org/10.3390/cells11091456.

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Nuclear pore complexes (NPCs) are the only transport channels that cross the nuclear envelope. Constructed from ~500–1000 nucleoporin proteins each, they are among the largest macromolecular assemblies in eukaryotic cells. Thanks to advances in structural analysis approaches, the construction principles and architecture of the NPC have recently been revealed at submolecular resolution. Although the overall structure and inventory of nucleoporins are conserved, NPCs exhibit significant compositional and functional plasticity even within single cells and surprising variability in their assembly

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Dultz, Elisa, Matthias Wojtynek, Ohad Medalia, and Evgeny Onischenko. "The Nuclear Pore Complex: Birth, Life, and Death of a Cellular Behemoth." Cells 11, no. 9 (2022): 1456. http://dx.doi.org/10.3390/cells11091456.

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Nuclear pore complexes (NPCs) are the only transport channels that cross the nuclear envelope. Constructed from ~500–1000 nucleoporin proteins each, they are among the largest macromolecular assemblies in eukaryotic cells. Thanks to advances in structural analysis approaches, the construction principles and architecture of the NPC have recently been revealed at submolecular resolution. Although the overall structure and inventory of nucleoporins are conserved, NPCs exhibit significant compositional and functional plasticity even within single cells and surprising variability in their assembly

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Dultz, Elisa, Matthias Wojtynek, Ohad Medalia, and Evgeny Onischenko. "The Nuclear Pore Complex: Birth, Life, and Death of a Cellular Behemoth." Cells 11, no. 9 (2022): 1456. http://dx.doi.org/10.3390/cells11091456.

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Nuclear pore complexes (NPCs) are the only transport channels that cross the nuclear envelope. Constructed from ~500–1000 nucleoporin proteins each, they are among the largest macromolecular assemblies in eukaryotic cells. Thanks to advances in structural analysis approaches, the construction principles and architecture of the NPC have recently been revealed at submolecular resolution. Although the overall structure and inventory of nucleoporins are conserved, NPCs exhibit significant compositional and functional plasticity even within single cells and surprising variability in their assembly

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13

Suresh, Subbulakshmi, Sarine Markossian, Aysha H. Osmani, and Stephen A. Osmani. "Mitotic nuclear pore complex segregation involves Nup2 in Aspergillus nidulans." Journal of Cell Biology 216, no. 9 (2017): 2813–26. http://dx.doi.org/10.1083/jcb.201610019.

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Transport through nuclear pore complexes (NPCs) during interphase is facilitated by the nucleoporin Nup2 via its importin α– and Ran-binding domains. However, Aspergillus nidulans and vertebrate Nup2 also locate to chromatin during mitosis, suggestive of mitotic functions. In this study, we report that Nup2 is required for mitotic NPC inheritance in A. nidulans. Interestingly, the role of Nup2 during mitotic NPC segregation is independent of its importin α– and Ran-binding domains but relies on a central targeting domain that is necessary for localization and viability. To test whether mitotic

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14

Winey, Mark, Defne Yarar, Thomas H. Giddings, and David N. Mastronarde. "Nuclear Pore Complex Number and Distribution throughout theSaccharomyces cerevisiaeCell Cycle by Three-Dimensional Reconstruction from Electron Micrographs of Nuclear Envelopes." Molecular Biology of the Cell 8, no. 11 (1997): 2119–32. http://dx.doi.org/10.1091/mbc.8.11.2119.

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The number of nuclear pore complexes (NPCs) in individual nuclei of the yeast Saccharomyces cerevisiae was determined by computer-aided reconstruction of entire nuclei from electron micrographs of serially sectioned cells. Nuclei of 32 haploid cells at various points in the cell cycle were modeled and found to contain between 65 and 182 NPCs. Morphological markers, such as cell shape and nuclear shape, were used to determine the cell cycle stage of the cell being examined. NPC number was correlated with cell cycle stage to reveal that the number of NPCs increases steadily, beginning in G1-phas

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15

Lusk, C. Patrick, Taras Makhnevych, Marcello Marelli, John D. Aitchison, and Richard W. Wozniak. "Karyopherins in nuclear pore biogenesis." Journal of Cell Biology 159, no. 2 (2002): 267–78. http://dx.doi.org/10.1083/jcb.200203079.

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The mechanisms that govern the assembly of nuclear pore complexes (NPCs) remain largely unknown. Here, we have established a role for karyopherins in this process. We show that the yeast karyopherin Kap121p functions in the targeting and assembly of the nucleoporin Nup53p into NPCs by recognizing a nuclear localization signal (NLS) in Nup53p. This karyopherin-mediated function can also be performed by the Kap95p–Kap60p complex if the Kap121p-binding domain of Nup53p is replaced by a classical NLS, suggesting a more general role for karyopherins in NPC assembly. At the NPC, neighboring nucleopo

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16

Walther, Tobias C., Helen S. Pickersgill, Volker C. Cordes, et al. "The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import." Journal of Cell Biology 158, no. 1 (2002): 63–77. http://dx.doi.org/10.1083/jcb.200202088.

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The nuclear pore complex (NPC) mediates bidirectional macromolecular traffic between the nucleus and cytoplasm in eukaryotic cells. Eight filaments project from the NPC into the cytoplasm and are proposed to function in nuclear import. We investigated the localization and function of two nucleoporins on the cytoplasmic face of the NPC, CAN/Nup214 and RanBP2/Nup358. Consistent with previous data, RanBP2 was localized at the cytoplasmic filaments. In contrast, CAN was localized near the cytoplasmic coaxial ring. Unexpectedly, extensive blocking of RanBP2 with gold-conjugated antibodies failed to

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17

Chugani, D. C., L. H. Rome, and N. L. Kedersha. "Evidence that vault ribonucleoprotein particles localize to the nuclear pore complex." Journal of Cell Science 106, no. 1 (1993): 23–29. http://dx.doi.org/10.1242/jcs.106.1.23.

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Vaults are cytoplasmic ribonucleoprotein organelles that are highly conserved among diverse eukaryotic species. Their mass (12.9 MDa), diameter (26-35 nm) and shape (two halves, each with eightfold radial symmetry) have recently been determined and are similar to those ascribed to the central plug (or transporter) of the nuclear pore complex (NPC). The size and eightfold symmetry of the vault particle make it conducive to interacting physically in a complementary manner with NPCs. The present study demonstrates that vaults specifically associate with nuclei by both immunoblotting and immunoflu

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18

Fahrenkrog, Birthe, Eduard C. Hurt, Ueli Aebi, and Nelly Panté. "Molecular Architecture of the Yeast Nuclear Pore Complex: Localization of Nsp1p Subcomplexes." Journal of Cell Biology 143, no. 3 (1998): 577–88. http://dx.doi.org/10.1083/jcb.143.3.577.

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The nuclear pore complex (NPC), a supramolecular assembly of ∼100 different proteins (nucleoporins), mediates bidirectional transport of molecules between the cytoplasm and the cell nucleus. Extensive structural studies have revealed the three- dimensional (3D) architecture of Xenopus NPCs, and eight of the ∼12 cloned and characterized vertebrate nucleoporins have been localized within the NPC. Thanks to the power of yeast genetics, 30 yeast nucleoporins have recently been cloned and characterized at the molecular level. However, the localization of these nucleoporins within the 3D structure o

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19

Quimby, B. Booth, Alexei Arnaoutov, and Mary Dasso. "Ran GTPase Regulates Mad2 Localization to the Nuclear Pore Complex." Eukaryotic Cell 4, no. 2 (2005): 274–80. http://dx.doi.org/10.1128/ec.4.2.274-280.2005.

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ABSTRACT In yeast and mammalian cells, the spindle assembly checkpoint proteins Mad1p and Mad2p localize to the nuclear pore complex (NPC) during interphase. Deletion of MAD1 or MAD2 did not affect steady-state nucleocytoplasmic distribution of a classical nuclear localization signal-containing reporter, a nuclear export signal-containing reporter, or Ran localization. We utilized cells with conditional mutations in the yeast Ran GTPase pathway to examine the relationship between Ran and targeting of checkpoint regulators to the NPC. Mutations that disrupt the concentration of Ran in the nucle

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20

Hamed, Mohamed, and Wolfram Antonin. "Dunking into the Lipid Bilayer: How Direct Membrane Binding of Nucleoporins Can Contribute to Nuclear Pore Complex Structure and Assembly." Cells 10, no. 12 (2021): 3601. http://dx.doi.org/10.3390/cells10123601.

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Nuclear pore complexes (NPCs) mediate the selective and highly efficient transport between the cytoplasm and the nucleus. They are embedded in the two membrane structure of the nuclear envelope at sites where these two membranes are fused to pores. A few transmembrane proteins are an integral part of NPCs and thought to anchor these complexes in the nuclear envelope. In addition, a number of nucleoporins without membrane spanning domains interact with the pore membrane. Here we review our current knowledge of how these proteins interact with the membrane and how this interaction can contribute

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21

Yang, Q., J.-F. Ménétret, I. V. Akey, K. Plath, T. A. Rapoport, and C. W. Akey. "Structural Studies of Translocation Channels: The Nuclear Pore Complex and the Translocon." Microscopy and Microanalysis 4, S2 (1998): 960–61. http://dx.doi.org/10.1017/s1431927600024922.

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Protein translocation plays a critical role in the targeting of both soluble and membrane proteins to their correct intra- and inter-cellular compartments. We are studying the 3D architecture of two rather different translocation machines, the Nuclear Pore Complex (NPC) and the ribosome-Sec61p complex (translocon), with the aim of understanding their physical mechanisms of gating and transport. Towards this end, we are using single particle electron cryomicroscopy and 3D reconstruction of frozen hydrated specimens to obtain interpretable maps that are biologically relevant.Previous work sugges

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22

Cohen, Merav, Naomi Feinstein, Katherine L. Wilson, and Yosef Gruenbaum. "Nuclear Pore Protein gp210 Is Essential for Viability in HeLa Cells and Caenorhabditis elegans." Molecular Biology of the Cell 14, no. 10 (2003): 4230–37. http://dx.doi.org/10.1091/mbc.e03-04-0260.

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Gp210 is an evolutionarily conserved membrane protein of the nuclear pore complex (NPC). We studied the phenotypes produced by RNAi-induced downregulation of gp210 in both human (HeLa) cells and Caenorhabditis elegans embryos. HeLa cell viability requires Gp210 activity. The dying cells accumulated clustered NPCs and aberrant membrane structures at the nuclear envelope, suggesting that gp210 is required directly or indirectly for nuclear pore formation and dilation as well as the anchoring or structural integrity of mature NPCs. Essential roles for gp210 were confirmed in C. elegans, where RNA

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Popken, Petra, Ali Ghavami, Patrick R. Onck, Bert Poolman, and Liesbeth M. Veenhoff. "Size-dependent leak of soluble and membrane proteins through the yeast nuclear pore complex." Molecular Biology of the Cell 26, no. 7 (2015): 1386–94. http://dx.doi.org/10.1091/mbc.e14-07-1175.

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Nuclear pore complexes (NPCs) allow selective import and export while forming a barrier for untargeted proteins. Using fluorescence microscopy, we measured in vivo the permeability of the Saccharomyces cerevisiae NPC for multidomain proteins of different sizes and found that soluble proteins of 150 kDa and membrane proteins with an extralumenal domain of 90 kDa were still partly localized in the nucleus on a time scale of hours. The NPCs thus form only a weak barrier for the majority of yeast proteins, given their monomeric size. Using FGΔ-mutant strains, we showed that specific combinations o

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Varberg, Joseph M., Jay R. Unruh, Andrew J. Bestul, Azqa A. Khan, and Sue L. Jaspersen. "Quantitative analysis of nuclear pore complex organization in Schizosaccharomyces pombe." Life Science Alliance 5, no. 7 (2022): e202201423. http://dx.doi.org/10.26508/lsa.202201423.

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The number, distribution, and composition of nuclear pore complexes (NPCs) in the nuclear envelope varies between cell types and changes during cellular differentiation and in disease. To understand how NPC density and organization are controlled, we analyzed the NPC number and distribution in the fission yeast Schizosaccharomyces pombe using structured illumination microscopy. The small size of yeast nuclei, genetic features of fungi, and our robust image analysis pipeline allowed us to study NPCs in intact nuclei under multiple conditions. Our data revealed that NPC density is maintained acr

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Terry, Laura J., and Susan R. Wente. "Nuclear mRNA export requires specific FG nucleoporins for translocation through the nuclear pore complex." Journal of Cell Biology 178, no. 7 (2007): 1121–32. http://dx.doi.org/10.1083/jcb.200704174.

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Trafficking of nucleic acids and large proteins through nuclear pore complexes (NPCs) requires interactions with NPC proteins that harbor FG (phenylalanine-glycine) repeat domains. Specialized transport receptors that recognize cargo and bind FG domains facilitate these interactions. Whether different transport receptors utilize preferential FG domains in intact NPCs is not fully resolved. In this study, we use a large-scale deletion strategy in Saccharomyces cerevisiae to generate a new set of more minimal pore (mmp) mutants that lack specific FG domains. A comparison of messenger RNA (mRNA)

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26

Wente, S. R., and G. Blobel. "A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic." Journal of Cell Biology 123, no. 2 (1993): 275–84. http://dx.doi.org/10.1083/jcb.123.2.275.

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NUP116 encodes a 116-kD yeast nuclear pore complex (NPC) protein that is not essential but its deletion (nup116 delta) slows cell growth at 23 degrees C and is lethal at 37 degrees C (Wente, S. R., M. P. Rout, and G. Blobel. 1992. J. Cell Biol. 119:705-723). Electron microscopic analysis of nup116 delta cells shifted to growth at 37 degrees C revealed striking perturbations of the nuclear envelope: a double membrane seal that was continuous with the inner and outer nuclear membranes had formed over the cytoplasmic face of the NPCs. Electron-dense material was observed accumulating between the

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Lau, Corine K., Thomas H. Giddings, and Mark Winey. "A Novel Allele of Saccharomyces cerevisiae NDC1 Reveals a Potential Role for the Spindle Pole Body Component Ndc1p in Nuclear Pore Assembly." Eukaryotic Cell 3, no. 2 (2004): 447–58. http://dx.doi.org/10.1128/ec.3.2.447-458.2004.

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ABSTRACT Both the spindle pole body (SPB) and the nuclear pore complex (NPC) are essential organelles embedded in the nuclear envelope throughout the life cycle of the budding yeast Saccharomyces cerevisiae. However, the mechanism by which these two multisubunit structures are inserted into the nuclear envelope during their biogenesis is not well understood. We have previously shown that Ndc1p is the only known integral membrane protein that localizes to both the SPBs and the NPCs and is required for SPB duplication. For this study, we generated a novel temperature-sensitive (ts) allele of NDC

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Chadrin, Anne, Barbara Hess, Mabel San Roman, et al. "Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution." Journal of Cell Biology 189, no. 5 (2010): 795–811. http://dx.doi.org/10.1083/jcb.200910043.

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The biogenesis of nuclear pore complexes (NPCs) represents a paradigm for the assembly of high-complexity macromolecular structures. So far, only three integral pore membrane proteins are known to function redundantly in NPC anchoring within the nuclear envelope. Here, we describe the identification and functional characterization of Pom33, a novel transmembrane protein dynamically associated with budding yeast NPCs. Pom33 becomes critical for yeast viability in the absence of a functional Nup84 complex or Ndc1 interaction network, which are two core NPC subcomplexes, and associates with the r

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Mitic, Kristina, Marianne Grafe, Petros Batsios, and Irene Meyer. "Partial Disassembly of the Nuclear Pore Complex Proteins during Semi-Closed Mitosis in Dictyostelium discoideum." Cells 11, no. 3 (2022): 407. http://dx.doi.org/10.3390/cells11030407.

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Dictyostelium cells undergo a semi-closed mitosis, during which the nuclear envelope (NE) persists; however, free diffusion between the cytoplasm and the nucleus takes place. To permit the formation of the mitotic spindle, the nuclear envelope must be permeabilized in order to allow diffusion of tubulin dimers and spindle assembly factors into the nucleus. In Aspergillus, free diffusion of proteins between the cytoplasm and the nucleus is achieved by a partial disassembly of the nuclear pore complexes (NPCs) prior to spindle assembly. In order to determine whether this is also the case in Dict

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Marelli, Marcello, David J. Dilworth, Richard W. Wozniak, and John D. Aitchison. "The dynamics of karyopherin-mediated nuclear transport." Biochemistry and Cell Biology 79, no. 5 (2001): 603–12. http://dx.doi.org/10.1139/o01-149.

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The regulated exchange of proteins and nucleic acids between the nucleus and cytoplasm demands a complex interplay between nuclear pore complexes (NPCs), which provide conduits in the nuclear envelope, and mobile transport receptors (or karyopherins, also known as importins/exportins) that bind and mediate the translocation of cargoes through the NPCs. Biochemical characterization of individual karyopherins has led to the identification of many of their cargoes and to the elucidation of the mechanisms by which they mediate transport. Likewise, the characterization of numerous NPC-associated co

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Orlova, А. V., S. G. Georgieva, and D. V. Kopytova. "Assembly and Disassembly of Nuclear Pore Complex: a View from Structural Side." Молекулярная биология 57, no. 4 (2023): 573–86. http://dx.doi.org/10.31857/s0026898423040171.

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Nucleocytoplasmic exchange in the cell occurs through the nuclear pore complexes (NPCs). NPCs are large multiprotein complexes with octagonal symmetry about their axis and imperfect mirror symmetry about a plane parallel with the nuclear envelop (NE). NPC fuses the inner and outer nuclear membranes and opens up а channel between nucleus and cytoplasm. NPC is built of nucleoporins. Each nucleoporin occurs in at least eight copies per NPC. Inside the NPC forms a permeability barrier by which NPC can ensure fast and selectable transport of molecules from one side of nuclear membrane to another. N

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Rexach, Michael. "Piecing together nuclear pore complex assembly during interphase." Journal of Cell Biology 185, no. 3 (2009): 377–79. http://dx.doi.org/10.1083/jcb.200904022.

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All nucleocytoplasmic traffic of macromolecules occurs through nuclear pore complexes (NPCs), which function as stents in the nuclear envelope to keep nuclear pores open but gated. Three studies in this issue (Flemming, D., P. Sarges, P. Stelter, A. Hellwig, B. Böttcher, and E. Hurt. 2009. J. Cell Biol. 185:387–395; Makio, T., L.H. Stanton, C.-C. Lin, D.S. Goldfarb, K. Weis, and R.W. Wozniak. 2009. J. Cell Biol. 185:459–491; Onishchenko, E., L.H. Stanton, A.S. Madrid, T. Kieselbach, and K. Weis. 2009. J. Cell Biol. 185:475–491) further our understanding of the NPC assembly process by reporting

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33

Dange, Thomas, David Grünwald, Antje Grünwald, Reiner Peters, and Ulrich Kubitscheck. "Autonomy and robustness of translocation through the nuclear pore complex: a single-molecule study." Journal of Cell Biology 183, no. 1 (2008): 77–86. http://dx.doi.org/10.1083/jcb.200806173.

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All molecular traffic between nucleus and cytoplasm occurs via the nuclear pore complex (NPC) within the nuclear envelope. In this study we analyzed the interactions of the nuclear transport receptors kapα2, kapβ1, kapβ1ΔN44, and kapβ2, and the model transport substrate, BSA-NLS, with NPCs to determine binding sites and kinetics using single-molecule microscopy in living cells. Recombinant transport receptors and BSA-NLS were fluorescently labeled by AlexaFluor 488, and microinjected into the cytoplasm of living HeLa cells expressing POM121-GFP as a nuclear pore marker. After bleaching the dom

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Theerthagiri, Gandhi, Nathalie Eisenhardt, Heinz Schwarz, and Wolfram Antonin. "The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex." Journal of Cell Biology 189, no. 7 (2010): 1129–42. http://dx.doi.org/10.1083/jcb.200912045.

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All transport across the nuclear envelope (NE) is mediated by nuclear pore complexes (NPCs). Despite their enormous size, ∼60 MD in vertebrates, they are comprised of only ∼30 distinct proteins (nucleoporins or Nups), many of which form subcomplexes that act as building blocks for NPC assembly. One of these evolutionarily conserved subcomplexes, the Nup93 complex, is a major structural component linking the NPC to the membranes of the NE. Using in vitro nuclear assembly assays, we show that two components of the Nup93 complex, Nup188 and Nup205, are dispensable for NPC formation. However, nucl

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Kann, Michael, Beate Sodeik, Angelika Vlachou, Wolfram H. Gerlich, and Ari Helenius. "Phosphorylation-dependent Binding of Hepatitis B Virus Core Particles to the Nuclear Pore Complex." Journal of Cell Biology 145, no. 1 (1999): 45–55. http://dx.doi.org/10.1083/jcb.145.1.45.

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Although many viruses replicate in the nucleus, little is known about the processes involved in the nuclear import of viral genomes. We show here that in vitro generated core particles of human hepatitis B virus bind to nuclear pore complexes (NPCs) in digitonin-permeabilized mammalian cells. This only occurred if the cores contained phosphorylated core proteins. Binding was inhibited by wheat germ agglutinin, by antinuclear pore complex antibodies, and by peptides corresponding either to classical nuclear localization signals (NLS) or to COOH-terminal sequences of the core protein. Binding wa

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Kiseleva, Elena, Sandra Rutherford, Laura M. Cotter, Terence D. Allen, and Martin W. Goldberg. "Steps of nuclear pore complex disassembly and reassembly during mitosis in earlyDrosophilaembryos." Journal of Cell Science 114, no. 20 (2001): 3607–18. http://dx.doi.org/10.1242/jcs.114.20.3607.

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The mechanisms of nuclear pore complex (NPC) assembly and disassembly during mitosis in vivo are not well defined. To address this and to identify the steps of the NPC disassembly and assembly, we investigated Drosophila embryo nuclear structure at the syncytial stage of early development using field emission scanning electron microscopy (FESEM), a high resolution surface imaging technique, and transmission electron microscopy. Nuclear division in syncytial embryos is characterized by semi-closed mitosis, during which the nuclear membranes are ruptured only at the polar regions and are arrange

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Gaik, Monika, Dirk Flemming, Alexander von Appen, et al. "Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold." Journal of Cell Biology 208, no. 3 (2015): 283–97. http://dx.doi.org/10.1083/jcb.201411003.

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Nuclear pore complexes (NPCs) are huge assemblies formed from ∼30 different nucleoporins, typically organized in subcomplexes. One module, the conserved Nup82 complex at the cytoplasmic face of NPCs, is crucial to terminate mRNA export. To gain insight into the structure, assembly, and function of the cytoplasmic pore filaments, we reconstituted in yeast the Nup82–Nup159–Nsp1–Dyn2 complex, which was suitable for biochemical, biophysical, and electron microscopy analyses. Our integrative approach revealed that the yeast Nup82 complex forms an unusual asymmetric structure with a dimeric array of

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Mitic, Kristina, Irene Meyer, Ralph Gräf, and Marianne Grafe. "Temporal Changes in Nuclear Envelope Permeability during Semi-Closed Mitosis in Dictyostelium Amoebae." Cells 12, no. 10 (2023): 1380. http://dx.doi.org/10.3390/cells12101380.

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The Amoebozoan Dictyostelium discoideum exhibits a semi-closed mitosis in which the nuclear membranes remain intact but become permeabilized to allow tubulin and spindle assembly factors to access the nuclear interior. Previous work indicated that this is accomplished at least by partial disassembly of nuclear pore complexes (NPCs). Further contributions by the insertion process of the duplicating, formerly cytosolic, centrosome into the nuclear envelope and nuclear envelope fenestrations forming around the central spindle during karyokinesis were discussed. We studied the behavior of several

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Zhang, Wanlu, Annett Neuner, Diana Rüthnick, et al. "Brr6 and Brl1 locate to nuclear pore complex assembly sites to promote their biogenesis." Journal of Cell Biology 217, no. 3 (2018): 877–94. http://dx.doi.org/10.1083/jcb.201706024.

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The paralogous Brr6 and Brl1 are conserved integral membrane proteins of the nuclear envelope (NE) with an unclear role in nuclear pore complex (NPC) biogenesis. Here, we analyzed double-degron mutants of Brr6/Brl1 to understand this function. Depletion of Brr6 and Brl1 caused defects in NPC biogenesis, whereas the already assembled NPCs remained unaffected. This NPC biogenesis defect was not accompanied by a change in lipid composition. However, Brl1 interacted with Ndc1 and Nup188 by immunoprecipitation, and with transmembrane and outer and inner ring NPC components by split yellow fluoresce

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Makarov, Alexandr A., Norma E. Padilla-Mejia, and Mark C. Field. "Evolution and diversification of the nuclear pore complex." Biochemical Society Transactions 49, no. 4 (2021): 1601–19. http://dx.doi.org/10.1042/bst20200570.

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The nuclear pore complex (NPC) is responsible for transport between the cytoplasm and nucleoplasm and one of the more intricate structures of eukaryotic cells. Typically composed of over 300 polypeptides, the NPC shares evolutionary origins with endo-membrane and intraflagellar transport system complexes. The modern NPC was fully established by the time of the last eukaryotic common ancestor and, hence, prior to eukaryote diversification. Despite the complexity, the NPC structure is surprisingly flexible with considerable variation between lineages. Here, we review diversification of the NPC i

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Allen, T. D., E. V. Kiseleva, and M. W. Goldberg. "Internal organisation of the nuclear pore complex by surface imaging with field emission in lens SEM (FEISEM)." Proceedings, annual meeting, Electron Microscopy Society of America 54 (August 11, 1996): 822–23. http://dx.doi.org/10.1017/s0424820100166579.

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We have been working towards a 3 dimensional structural understanding of the Nuclear Pore Complex (NPC) with a view to investigating structural alterations associated with the molecular mechanism of transport across the nuclear envelope. FEISEM allows direct visualisation of changes in individual NPCs which will complement information from TEM 3D reconstructions. FEISEM has produced significant new information on the more peripheral elements of the NPC, most notably the nuclear pore basket or ‘fishtrap’ and the nuclear envelope lattice. NPC baskets have been recognised in both avian and insect

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Kuersten, Scott, Gert-Jan Arts, Tobias C. Walther, Ludwig Englmeier, and Iain W. Mattaj. "Steady-State Nuclear Localization of Exportin-t Involves RanGTP Binding and Two Distinct Nuclear Pore Complex Interaction Domains." Molecular and Cellular Biology 22, no. 16 (2002): 5708–20. http://dx.doi.org/10.1128/mcb.22.16.5708-5720.2002.

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ABSTRACT Vertebrate tRNA export receptor exportin-t (Xpo-t) binds to RanGTP and mature tRNAs cooperatively to form a nuclear export complex. Xpo-t shuttles bidirectionally through nuclear pore complexes (NPCs) but is mainly nuclear at steady state. The steady-state distribution of Xpo-t is shown to depend on its interaction with RanGTP. Two distinct Xpo-t NPC interaction domains that bind differentially to peripherally localized nucleoporins in vitro are identified. The N terminus binds to both Nup153 and RanBP2/Nup358 in a RanGTP-dependent manner, while the C terminus binds to CAN/Nup214 inde

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Hawryluk-Gara, Lisa A., Melpomeni Platani, Rachel Santarella, Richard W. Wozniak, and Iain W. Mattaj. "Nup53 Is Required for Nuclear Envelope and Nuclear Pore Complex Assembly." Molecular Biology of the Cell 19, no. 4 (2008): 1753–62. http://dx.doi.org/10.1091/mbc.e07-08-0820.

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Transport across the nuclear envelope (NE) is mediated by nuclear pore complexes (NPCs). These structures are composed of various subcomplexes of proteins that are each present in multiple copies and together establish the eightfold symmetry of the NPC. One evolutionarily conserved subcomplex of the NPC contains the nucleoporins Nup53 and Nup155. Using truncation analysis, we have defined regions of Nup53 that bind to neighboring nucleoporins as well as those domains that target Nup53 to the NPC in vivo. Using this information, we investigated the role of Nup53 in NE and NPC assembly using Xen

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Sachdev, Ruchika, Cornelia Sieverding, Matthias Flötenmeyer, and Wolfram Antonin. "The C-terminal domain of Nup93 is essential for assembly of the structural backbone of nuclear pore complexes." Molecular Biology of the Cell 23, no. 4 (2012): 740–49. http://dx.doi.org/10.1091/mbc.e11-09-0761.

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Nuclear pore complexes (NPCs) are large macromolecular assemblies that control all transport across the nuclear envelope. They are formed by about 30 nucleoporins (Nups), which can be roughly categorized into those forming the structural skeleton of the pore and those creating the central channel and thus providing the transport and gating properties of the NPC. Here we show that the conserved nucleoporin Nup93 is essential for NPC assembly and connects both portions of the NPC. Although the C-terminal domain of the protein is necessary and sufficient for the assembly of a minimal structural b

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Stanley, George J., Ariberto Fassati, and Bart W. Hoogenboom. "Atomic force microscopy reveals structural variability amongst nuclear pore complexes." Life Science Alliance 1, no. 4 (2018): e201800142. http://dx.doi.org/10.26508/lsa.201800142.

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The nuclear pore complex (NPC) is a proteinaceous assembly that regulates macromolecular transport into and out of the nucleus. Although the structure of its scaffold is being revealed in increasing detail, its transport functionality depends upon an assembly of intrinsically disordered proteins (called FG-Nups) anchored inside the pore's central channel, which have hitherto eluded structural characterization. Here, using high-resolution atomic force microscopy, we provide a structural and nanomechanical analysis of individual NPCs. Our data highlight the structural diversity and complexity at

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Shevelyov, Yuri Y. "The Role of Nucleoporin Elys in Nuclear Pore Complex Assembly and Regulation of Genome Architecture." International Journal of Molecular Sciences 21, no. 24 (2020): 9475. http://dx.doi.org/10.3390/ijms21249475.

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For a long time, the nuclear lamina was thought to be the sole scaffold for the attachment of chromosomes to the nuclear envelope (NE) in metazoans. However, accumulating evidence indicates that nuclear pore complexes (NPCs) comprised of nucleoporins (Nups) participate in this process as well. One of the Nups, Elys, initiates NPC reassembly at the end of mitosis. Elys directly binds the decondensing chromatin and interacts with the Nup107–160 subcomplex of NPCs, thus serving as a seeding point for the subsequent recruitment of other NPC subcomplexes and connecting chromatin with the re-forming

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Galy, Vincent, Iain W. Mattaj, and Peter Askjaer. "Caenorhabditis elegans Nucleoporins Nup93 and Nup205 Determine the Limit of Nuclear Pore Complex Size Exclusion In Vivo." Molecular Biology of the Cell 14, no. 12 (2003): 5104–15. http://dx.doi.org/10.1091/mbc.e03-04-0237.

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Nuclear pore complexes (NPCs) span the nuclear envelope and mediate communication between the nucleus and the cytoplasm. To obtain insight into the structure and function of NPCs of multicellular organisms, we have initiated an extensive analysis of Caenorhabditis elegans nucleoporins. Of 20 assigned C. elegans nucleoporin genes, 17 were found to be essential for embryonic development either alone or in combination. In several cases, depletion of nucleoporins by RNAi caused severe defects in nuclear appearance. More specifically, the C. elegans homologs of vertebrate Nup93 and Nup205 were each

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Shimi, Takeshi, and Hiroshi Kimura. "A mosaic of old and young nucleoporins." Journal of Cell Biology 218, no. 2 (2019): 385–86. http://dx.doi.org/10.1083/jcb.201811170.

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Some nucleoporins, the nuclear pore complex (NPC) components, have exceptionally long lifetimes. In this issue, Toyama et al. (2019. J. Cell Biol. https://doi.org/10.1083/jcb.201809123) report that NPCs are maintained by a slow piecemeal replacement of NPC components in dividing and terminally differentiated cells and by whole-pore exchange in quiescent cells.

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Lin, Daniel H., and André Hoelz. "The Structure of the Nuclear Pore Complex (An Update)." Annual Review of Biochemistry 88, no. 1 (2019): 725–83. http://dx.doi.org/10.1146/annurev-biochem-062917-011901.

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The nuclear pore complex (NPC) serves as the sole bidirectional gateway of macromolecules in and out of the nucleus. Owing to its size and complexity (∼1,000 protein subunits, ∼110 MDa in humans), the NPC has remained one of the foremost challenges for structure determination. Structural studies have now provided atomic-resolution crystal structures of most nucleoporins. The acquisition of these structures, combined with biochemical reconstitution experiments, cross-linking mass spectrometry, and cryo–electron tomography, has facilitated the determination of the near-atomic overall architectur

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Allen, T. D., G. R. Bcnnion, S. A. Rutherford, E. Kiscleva, and M. W. Goldberg. "FEISEM, Form and Function in the Nuclear Pore Complex." Microscopy and Microanalysis 4, S2 (1998): 958–59. http://dx.doi.org/10.1017/s1431927600024910.

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Recent initiatives have resulted in a considerable increase in our understanding of the structure of the nuclear pore complex (NPC). The biochemical factors involved in both import and export have been rapidly characterised, with steady progress in the molecular dissection of the structural elements of the NPC, which is a unit of considerable molecular architecture (MW 125 kD), comprising an estimated 50- 100 different proteins. Despite this progress, the crucial molecular interactions involved in the mechanics of transport through the central transporter of the NPC remain unclear. NPC structu

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