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Nuclear transport

  • RESEARCH ARTICLE
    Passive diffusion through nuclear pore complexes regulates levels of the yeast SAGA and SLIK coactivator complexes
    Tadashi Makio, Richard W. Wozniak
    Journal of Cell Science 2020 133: jcs237156 doi: 10.1242/jcs.237156 Published 26 March 2020

    Highlighted Article: By controlling passive diffusion across the nuclear envelope, nuclear pore complexes regulate levels of the SAGA and SLIK coactivator complexes, suggesting alterations in passive diffusion can modulate gene expression.

  • RESEARCH ARTICLE
    ERK1/2 phosphorylates HIF-2α and regulates its activity by controlling its CRM1-dependent nuclear shuttling
    Ioanna-Maria Gkotinakou, Christina Befani, George Simos, Panagiotis Liakos
    Journal of Cell Science 2019 132: jcs225698 doi: 10.1242/jcs.225698 Published 8 April 2019

    Summary: Phosphorylation by ERK1/2 stimulates transcriptional activity of hypoxia-inducible factor-2α by inhibiting its CRM1- and NES-dependent nuclear export.

  • RESEARCH ARTICLE
    Prolines in the α-helix confer the structural flexibility and functional integrity of importin-β
    Masahiro Kumeta, Hide A. Konishi, Wanzhen Zhang, Sayuri Sakagami, Shige H. Yoshimura
    Journal of Cell Science 2018 131: jcs206326 doi: 10.1242/jcs.206326 Published 4 January 2018

    Summary: Multiple prolines in the helical repeat of karyopherins play essential roles in the structural flexibility of these molecules and their passage through the nuclear pore complex, as well as in proper mitotic progression.

  • COMMENTARY
    Perforating the nuclear boundary – how nuclear pore complexes assemble
    Marion Weberruss, Wolfram Antonin
    Journal of Cell Science 2016 129: 4439-4447; doi: 10.1242/jcs.194753

    Summary: Nuclear pore complexes are the gatekeepers of the nuclear envelope. We summarize how these huge structures assemble from about a thousand individual proteins and integrate into the nuclear envelope.

  • RESEARCH ARTICLE
    Nuclear size is sensitive to NTF2 protein levels in a manner dependent on Ran binding
    Lidija D. Vuković, Predrag Jevtić, Zhaojie Zhang, Bradley A. Stohr, Daniel L. Levy
    Journal of Cell Science 2016 129: 1115-1127; doi: 10.1242/jcs.181263

    Summary: NTF2 reduces the diameter of the NPC, nuclear import of large cargos and nuclear size in a Ran-binding-dependent manner, in both Xenopus and mammalian cells.

  • RESEARCH ARTICLE
    Regulation of the phosphorylation and nuclear import and export of β-catenin by APC and its cancer-related truncated form
    Lili Wang, Xiaoyong Liu, Ekaterina Gusev, Chuanxin Wang, François Fagotto
    Journal of Cell Science 2014 127: 1647-1659; doi: 10.1242/jcs.131045
  • SHORT REPORT
    Karyopherin-independent spontaneous transport of amphiphilic proteins through the nuclear pore
    Masahiro Kumeta, Hideki Yamaguchi, Shige H. Yoshimura, Kunio Takeyasu
    Journal of Cell Science 2012 125: 4979-4984; doi: 10.1242/jcs.109520
  • RESEARCH ARTICLE
    RNA association and nucleocytoplasmic shuttling by ataxin-1
    Stuart Irwin, Mark Vandelft, Deborah Pinchev, Jenny L. Howell, Joanna Graczyk, Harry T. Orr, Ray Truant
    Journal of Cell Science 2005 118: 233-242; doi: 10.1242/jcs.01611
  • TARGETING TO THE NUCLEUS
    Nuclear transport in vitro
    DEBORAH R. FINLAY, DONALD D. NEWMEYER, PHILIPPE M. HARTL, JOSEPH HORECKA, DOUGLASS J. FORBES
    Journal of Cell Science 1989 1989: 225-242; doi: 10.1242/jcs.1989.Supplement_11.17

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