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Long unfolded linkers facilitate membrane protein import through the nuclear pore complex

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Anne C Meinema
  • ,
  • Justyna K Laba
  • ,
  • Rizqiya A Hapsari
  • ,
  • Renee Otten
  • ,
  • Frans A.A. Mulder
  • Annemarie Kralt
  • ,
  • Geert van den Bogaart
  • ,
  • C Patrick Lusk
  • ,
  • Bert Poolman
  • ,
  • Liesbeth M Veenhoff
Active nuclear import of soluble cargo involves transport factors that shuttle cargo through the nuclear pore complex (NPC) by binding to phenylalanine-glycine (FG) domains. How nuclear membrane proteins cross through the NPC to reach the inner membrane is presently unclear. We found that at least a 120-residue-long intrinsically disordered linker was required for the import of membrane proteins carrying a nuclear localization signal for the transport factor karyopherin-α. We propose an import mechanism for membrane proteins in which an unfolded linker slices through the NPC scaffold to enable binding between the transport factor and the FG domains in the center of the NPC.
Original languageEnglish
Pages (from-to)90-3
Number of pages4
Publication statusPublished - 2011

    Research areas

  • Active Transport, Cell Nucleus, Amino Acid Sequence, Endoplasmic Reticulum, Karyopherins, Membrane Proteins, Models, Biological, Molecular Sequence Data, Nuclear Envelope, Nuclear Localization Signals, Nuclear Pore, Nuclear Pore Complex Proteins, Nuclear Proteins, Protein Folding, Protein Structure, Tertiary, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins

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