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Journal articles on the topic 'Nuclear pore complex inheritance'

Author: Grafiati

Published: 4 June 2021

Last updated: 5 February 2022

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1

Lusk, C. Patrick, and Paolo Colombi. "Toward a consensus on the mechanism of nuclear pore complex inheritance." Nucleus 5, no. 2 (February 25, 2014): 97–102. http://dx.doi.org/10.4161/nucl.28314.

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2

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 (July 26, 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 chromatin-associated Nup2 might function to bridge NPCs with chromatin during segregation, we provided an artificial link between NPCs and chromatin via Nup133 and histone H1. Using this approach, we bypassed the requirement of Nup2 for NPC segregation. This indicates that A. nidulans cells ensure accurate mitotic NPC segregation to daughter nuclei by linking mitotic DNA and NPC segregation via the mitotic specific chromatin association of Nup2.

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3

Schuldt, Alison. "Nuclear pore inheritance." Nature Reviews Molecular Cell Biology 14, no. 12 (November 22, 2013): 753. http://dx.doi.org/10.1038/nrm3714.

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4

Panté, N., and U. Aebi. "The nuclear pore complex." Journal of Cell Biology 122, no. 5 (September 1, 1993): 977–84. http://dx.doi.org/10.1083/jcb.122.5.977.

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5

Woodward, Cora L., and Samson A. Chow. "The nuclear pore complex." Nucleus 1, no. 1 (January 2010): 18–22. http://dx.doi.org/10.4161/nucl.1.1.10571.

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6

Davis, Laura I. "The Nuclear Pore Complex." Annual Review of Biochemistry 64, no. 1 (June 1995): 865–96. http://dx.doi.org/10.1146/annurev.bi.64.070195.004245.

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7

Hurt, Eduard C. "The nuclear pore complex." FEBS Letters 325, no. 1-2 (June 28, 1993): 76–80. http://dx.doi.org/10.1016/0014-5793(93)81417-x.

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8

Panté, Nelly. "Nuclear Pore Complex Structure." Developmental Cell 7, no. 6 (December 2004): 780–81. http://dx.doi.org/10.1016/j.devcel.2004.11.010.

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9

Fernandez-Martinez, Javier, and Michael P. Rout. "Nuclear pore complex biogenesis." Current Opinion in Cell Biology 21, no. 4 (August 2009): 603–12. http://dx.doi.org/10.1016/j.ceb.2009.05.001.

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10

Akey, Christopher W. "The nuclear pore complex." Current Biology 2, no. 5 (May 1992): 258. http://dx.doi.org/10.1016/0960-9822(92)90377-m.

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11

Bagley, S., M. W. Goldberg, J. M. Cronshaw, S. A. Rutherford, and T. D. Allen. "The nuclear pore complex." Journal of Cell Science 113, no. 22 (January 1, 2000): 3885–86. http://dx.doi.org/10.1242/jcs.113.22.3885.

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12

Kapon, Ruti, Bracha Naim, David Zbaida, Reinat Nevo, Onie Tsabari, and Ziv Reich. "Permeating the nuclear pore complex." Nucleus 1, no. 6 (November 2010): 475–80. http://dx.doi.org/10.4161/nucl.1.6.13112.

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13

Rout, Michael P., John D. Aitchison, Adisetyantari Suprapto, Kelly Hjertaas, Yingming Zhao, and Brian T. Chait. "The Yeast Nuclear Pore Complex." Journal of Cell Biology 148, no. 4 (February 21, 2000): 635–52. http://dx.doi.org/10.1083/jcb.148.4.635.

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An understanding of how the nuclear pore complex (NPC) mediates nucleocytoplasmic exchange requires a comprehensive inventory of the molecular components of the NPC and a knowledge of how each component contributes to the overall structure of this large molecular translocation machine. Therefore, we have taken a comprehensive approach to classify all components of the yeast NPC (nucleoporins). This involved identifying all the proteins present in a highly enriched NPC fraction, determining which of these proteins were nucleoporins, and localizing each nucleoporin within the NPC. Using these data, we present a map of the molecular architecture of the yeast NPC and provide evidence for a Brownian affinity gating mechanism for nucleocytoplasmic transport.

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14

Wente, S. R., and M. P. Rout. "The Nuclear Pore Complex and Nuclear Transport." Cold Spring Harbor Perspectives in Biology 2, no. 10 (July 14, 2010): a000562. http://dx.doi.org/10.1101/cshperspect.a000562.

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15

Bano, Daniele, Michael O. Hengartner, and Pierluigi Nicotera. "Nuclear pore complex during neuronal degeneration." Nucleus 1, no. 2 (March 2010): 136–38. http://dx.doi.org/10.4161/nucl.10798.

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16

Bustamante, José Omar, Andrejs Liepins, and John Allan Hanover. "Nuclear pore complex ion channels (Review)." Molecular Membrane Biology 11, no. 3 (January 1994): 141–50. http://dx.doi.org/10.3109/09687689409162232.

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17

Talcott, Bradford, and Mary Shannon Moore. "Getting across the nuclear pore complex." Trends in Cell Biology 9, no. 8 (August 1999): 312–18. http://dx.doi.org/10.1016/s0962-8924(99)01608-6.

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18

Lim, Roderick Y. H. "Gate-Crashing the Nuclear Pore Complex." Structure 15, no. 8 (August 2007): 889–91. http://dx.doi.org/10.1016/j.str.2007.07.005.

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19

Walther, Tobias C., Peter Askjaer, Marc Gentzel, Anja Habermann, Gareth Griffiths, Matthias Wilm, Iain W. Mattaj, and Martin Hetzer. "RanGTP mediates nuclear pore complex assembly." Nature 424, no. 6949 (July 30, 2003): 689–94. http://dx.doi.org/10.1038/nature01898.

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20

Paschal, Bryce M. "Translocation through the nuclear pore complex." Trends in Biochemical Sciences 27, no. 12 (December 2002): 593–96. http://dx.doi.org/10.1016/s0968-0004(02)02227-2.

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21

Goldberg, Martin W., Sandra A. Rutherford, Mike Hughes, Laura A. Cotter, Steven Bagley, Elena Kiseleva, Terence D. Allen, and Paul R. Clarke. "Ran alters nuclear pore complex conformation." Journal of Molecular Biology 300, no. 3 (July 2000): 519–29. http://dx.doi.org/10.1006/jmbi.2000.3891.

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22

Eckardt, Nancy A. "The Nuclear Pore Complex in Arabidopsis." Plant Cell 22, no. 12 (December 2010): 3878. http://dx.doi.org/10.1105/tpc.110.221211.

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23

Short, Ben. "Mapping out the nuclear pore complex." Journal of Cell Biology 208, no. 3 (February 2, 2015): 257. http://dx.doi.org/10.1083/jcb.2083fta.

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24

Lim, Roderick YH, and Birthe Fahrenkrog. "The nuclear pore complex up close." Current Opinion in Cell Biology 18, no. 3 (June 2006): 342–47. http://dx.doi.org/10.1016/j.ceb.2006.03.006.

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25

Kahms, Martin, Jana Hüve, Ramona Wesselmann, Julia C. Farr, Viola Baumgärtel, and Reiner Peters. "Lighting up the nuclear pore complex." European Journal of Cell Biology 90, no. 9 (September 2011): 751–58. http://dx.doi.org/10.1016/j.ejcb.2011.04.004.

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26

Goldberg, Martin W., Irena Solovei, and Terence D. Allen. "Nuclear Pore Complex Structure in Birds." Journal of Structural Biology 119, no. 3 (August 1997): 284–94. http://dx.doi.org/10.1006/jsbi.1997.3877.

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27

Makio, Tadashi, Diego L. Lapetina, and Richard W. Wozniak. "Inheritance of yeast nuclear pore complexes requires the Nsp1p subcomplex." Journal of Cell Biology 203, no. 2 (October 28, 2013): 187–96. http://dx.doi.org/10.1083/jcb.201304047.

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In the yeast Saccharomyces cerevisiae, organelles and macromolecular complexes are delivered from the mother to the emerging daughter during cell division, thereby ensuring progeny viability. Here, we have shown that during mitosis nuclear pore complexes (NPCs) in the mother nucleus are actively delivered through the bud neck and into the daughter cell concomitantly with the nuclear envelope. Furthermore, we show that NPC movement into the daughter cell requires members of an NPC subcomplex containing Nsp1p and its interacting partners. NPCs lacking these nucleoporins (Nups) were blocked from entry into the daughter by a putative barrier at the bud neck. This selection process could be observed within individual cells such that NPCs containing Nup82p (an Nsp1p-interacting Nup) were transferred to the daughter cells while functionally compromised NPCs lacking Nup82p were retained in the mother. This mechanism is proposed to facilitate the inheritance of functional NPCs by daughter cells.

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28

Finlay, D. R., E. Meier, P. Bradley, J. Horecka, and D. J. Forbes. "A complex of nuclear pore proteins required for pore function." Journal of Cell Biology 114, no. 1 (July 1, 1991): 169–83. http://dx.doi.org/10.1083/jcb.114.1.169.

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A family of proteins bearing novel N-acetylglucosamine residues has previously been found to be required to form functional nuclear pores. To begin to determine which of the proteins in this family are essential for pore function, antisera were raised to each of three members of the family, p62, p58, and p54. With these antisera, it was possible to deplete nuclear reconstitution extracts of the proteins and to test the depleted nuclei for nuclear transport. In the course of the experiments, it was found that the three proteins exist as a complex; antisera to any one, while specific on a protein blot, coimmunoprecipitated all three proteins. This complex of pore proteins is stable to 2 M salt, 2 M urea, and the detergent Mega 10, indicating the presence of specific and tight protein-protein interactions. By gel filtration, the complex has a molecular mass of 550-600 kD. Nuclei containing pores depleted of the complex are found to be defective for nuclear transport; moreover, we observe a strict linear correlation between the amount of complex present in nuclei and the amount of nuclear transport of which those nuclei are capable. Thus, the p62-p58-p54 complex defines a group of proteins with strong protein-protein interactions that form a unit of pore structure essential for pore function.

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29

Leslie, Mitch. "Ensuring that yeast cells get their inheritance." Journal of Cell Biology 203, no. 2 (October 28, 2013): 167. http://dx.doi.org/10.1083/jcb.2032if.

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30

Panté, Nelly, and Ueli Aebi. "Molecular Dissection of the Nuclear Pore Complex." Critical Reviews in Biochemistry and Molecular Biology 31, no. 2 (January 1996): 153–99. http://dx.doi.org/10.3109/10409239609106583.

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31

Le Sage, Valerie, and Andrew Mouland. "Viral Subversion of the Nuclear Pore Complex." Viruses 5, no. 8 (August 16, 2013): 2019–42. http://dx.doi.org/10.3390/v5082019.

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32

Grima, Jonathan C., J. Gavin Daigle, Nicolas Arbez, Kathleen C. Cunningham, Ke Zhang, Joseph Ochaba, Charlene Geater, et al. "Mutant Huntingtin Disrupts the Nuclear Pore Complex." Neuron 94, no. 1 (April 2017): 93–107. http://dx.doi.org/10.1016/j.neuron.2017.03.023.

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33

Pai, C. "The nuclear pore complex and chromatin boundaries." Trends in Cell Biology 12, no. 10 (October 1, 2002): 452–55. http://dx.doi.org/10.1016/s0962-8924(02)02367-x.

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34

Hüve, Jana, Ramona Wesselmann, Martin Kahms, and Reiner Peters. "4Pi Microscopy of the Nuclear Pore Complex." Biophysical Journal 95, no. 2 (July 2008): 877–85. http://dx.doi.org/10.1529/biophysj.107.127449.

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35

Sakiyama, Yusuke, Radhakrishnan Panatala, and Roderick Y. H. Lim. "Structural dynamics of the nuclear pore complex." Seminars in Cell & Developmental Biology 68 (August 2017): 27–33. http://dx.doi.org/10.1016/j.semcdb.2017.05.021.

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36

Goldberg, Martin W. "Nuclear pore complex tethers to the cytoskeleton." Seminars in Cell & Developmental Biology 68 (August 2017): 52–58. http://dx.doi.org/10.1016/j.semcdb.2017.06.017.

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37

Akey, Christopher W. "Structural plasticity of the nuclear pore complex." Journal of Molecular Biology 248, no. 2 (January 1995): 273–93. http://dx.doi.org/10.1016/s0022-2836(95)80050-6.

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38

PANTE, N. "Nuclear Pore Complex StructureUnplugged and Dynamic Pores." Developmental Cell 7, no. 6 (December 2004): 780–81. http://dx.doi.org/10.1016/s1534-5807(04)00418-6.

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39

Sheffield, Lynette G., Hayley B. Miskiewicz, Lindsey B. Tannenbaum, and Suzanne S. Mirra. "Nuclear Pore Complex Proteins in Alzheimer Disease." Journal of Neuropathology and Experimental Neurology 65, no. 1 (January 2006): 45–54. http://dx.doi.org/10.1097/01.jnen.0000195939.40410.08.

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40

Robinson, Richard. "No waiting at the nuclear pore complex." Journal of Cell Biology 183, no. 1 (September 29, 2008): 2. http://dx.doi.org/10.1083/jcb.1831iti1.

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41

Monette, Anne, Nelly Panté, and Andrew J. Mouland. "HIV-1 remodels the nuclear pore complex." Journal of Experimental Medicine 208, no. 6 (June 6, 2011): i16. http://dx.doi.org/10.1084/jem2086oia16.

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42

Leslie, Mitch. "A portrait of the nuclear pore complex." Journal of Cell Biology 171, no. 2 (October 24, 2005): 194–95. http://dx.doi.org/10.1083/jcb1712fta3.

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43

Pemberton, Lucy F., Günter Blobel, and Jonathan S. Rosenblum. "Transport routes through the nuclear pore complex." Current Opinion in Cell Biology 10, no. 3 (June 1998): 392–99. http://dx.doi.org/10.1016/s0955-0674(98)80016-1.

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44

Rout, M. P., and G. Blobel. "Isolation of the yeast nuclear pore complex." Journal of Cell Biology 123, no. 4 (November 15, 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 but one of the eight known NPC proteins. In addition it contains as many as 80 uncharacterized proteins that are candidate NPC proteins.

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45

Burke, B. "CELL BIOLOGY: Nuclear Pore Complex Models Gel." Science 314, no. 5800 (November 3, 2006): 766a—767a. http://dx.doi.org/10.1126/science.1135739.

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46

Stuwe, T., A. R. Correia, D. H. Lin, M. Paduch, V. T. Lu, A. A. Kossiakoff, and A. Hoelz. "Architecture of the nuclear pore complex coat." Science 347, no. 6226 (February 12, 2015): 1148–52. http://dx.doi.org/10.1126/science.aaa4136.

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47

Maimon, Tal, and Ohad Medalia. "Perspective on the metazoan nuclear pore complex." Nucleus 1, no. 5 (September 2010): 383–86. http://dx.doi.org/10.4161/nucl.1.5.12332.

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48

Monette, Anne, Nelly Panté, and Andrew J. Mouland. "HIV-1 remodels the nuclear pore complex." Journal of Cell Biology 193, no. 4 (May 16, 2011): 619–31. http://dx.doi.org/10.1083/jcb.201008064.

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Human immunodeficiency virus type 1 (HIV-1) commandeers host cell proteins and machineries for its replication. Our earlier work showed that HIV-1 induced the cytoplasmic retention of nucleocytoplasmic shuttling and ribonucleic acid (RNA)–binding proteins. This retention is dependent on nuclear export of the viral genomic RNA and on changes in the localization and expression level of the nucleoporin (Nup) p62 (Nup62). To further characterize the extent of perturbation induced by HIV-1, we performed proteomics analyses of nuclear envelopes (NEs) isolated from infected T cells. Infection induced extensive changes in the composition of the NE and its associated proteins, including a remarkable decrease in the abundance of Nups. Immunogold electron microscopy revealed the translocation of Nups into the cytoplasm. Nup62 was identified as a component of purified virus, and small interfering RNA depletion studies revealed an important role for this Nup in virus gene expression and infectivity. This detailed analysis highlights the profound effects on NE composition induced by HIV-1 infection, providing further evidence of the magnitude of viral control over the cell biology of its host.

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49

R. K. Mofrad, Mohammad. "Mechanobiology of the Nuclear Pore Complex Machinery." Molecular & Cellular Biomechanics 16, S2 (2019): 19–20. http://dx.doi.org/10.32604/mcb.2019.07429.

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50

Doerr, Allison. "Action shots of the nuclear pore complex." Nature Methods 4, no. 11 (November 2007): 881. http://dx.doi.org/10.1038/nmeth1107-881.

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